Microbial proteases applications

Frontiers in Bioengineering and Biotechnology

Volumn 7, Issue JUN, 2019, Pages

  Razzaq, Abdul ^a   Shamsi, Sadia ^b   Ali, Arfan ^c   Ali, Qurban ^d   Sajjad, Muhammad ^d   Malik, Arif ^d   Ashraf, Muhammad ^d  

^a INSTITUTE OF PLANT PROTECTION   (China)

^b UNIVERSITY OF ABERDEEN   (United Kingdom)

^c Four Brothers Group   (Pakistan)

^d UNIVERSITY OF LAHORE   (Pakistan)

Author keywords

Bacterial enzymes; Industrial enzyme; Microbial proteases; Proteolytic enzymes; Substrate specific proteases

Indexed keywords

ALKALINITY; BACTERIA; BACTERIOLOGY;

BACTERIAL ENZYMES; ENVIRONMENTAL-FRIENDLY; EVOLUTIONARY RELATIONSHIPS; INDUSTRIAL ENZYMES; MICROBIAL PROTEASE; PROTEIN SEQUENCES; PROTEOLYTIC ENZYME; SUBSTRATE SPECIFICITY;

ENZYMES;

EID: 85068782615     PISSN: None     EISSN: 22964185     Source Type: Journal    
DOI: 10.3389/fbioe.2019.00110     Document Type: Review

References (339)

1. Achstetter, T., Emter, O., Ehmann, C., and Wolf, D. H. (1984). Proteolysis in eukaryotic cells. Identification of multiple proteolytic enzymes in yeast. J. Biol. Chem. 259, 13334-13343.
2. Adetunji, C. O., and Adejumo, I. O. (2018). Efficacy of crude and immobilizedenzymes from Bacillus licheniformis for production of biodegraded feather meal and their assessment on chickens. Environ. Technol. Innov. 11, 116-124. doi: 10.1016/j.eti.2018.05.002
3. Adinarayana, K., Ellaiah, P., and Prasad, D. S. (2003). Purification and partial characterization of thermostable serine alkaline protease from a newly isolated Bacillus subtilis PE-11. AAPS PharmSciTech 4, 440-448. doi: 10.1208/pt040456
4. Adrio, J., and Demain, A. (2014). Microbial enzymes: tools for biotechnological processes. Biomolecules 4, 117-139. doi: 10.3390/biom4010117
5. Aehle, W., Sobek, H., Amory, A., Vetter, R., Wilke, D., and Schomburg, D. (1993). Rational protein engineering and industrial application: Structure prediction by homology and rational design of protein-variants with improved 'washing performance'-the alkaline protease from Bacillus alcalophilus. J. Biotechnol. 28, 31-40. doi: 10.1016/0168-1656(93)90123-5
6. Agyei, D., Ongkudon, C. M., Wei, C. Y., Chan, A. S., and Danquah, M. K. (2016). Bioprocess challenges to the isolation and purification of bioactive peptides. Food Bioprod. Process. 98, 244-256. doi: 10.1016/j.fbp.2016.02.003
7. Ahmed, S. A., Al-Domany, R. A., El-Shayeb, N. M., Radwan, H. H., and Saleh, S. A. (2008). Optimization, immobilization of extracellular alkaline protease and characterization of its enzymatic properties. Res. J. Agric. Biol. Sci. 4, 434-446.
8. Aiken, C. T., Kaake, R. M., Wang, X., and Huang, L. (2011). Oxidative stress-mediated regulation of proteasome complexes. Mol. Cell. Proteomics 10:R110.006924. doi: 10.1074/mcp. R110.006924
9. Ali, N., Ullah, N., Qasim, M., Rahman, H., Khan, S. N., Sadig, A., et al. (2016). Molecular characterization and growth optimization of halo-tolerant protease producing Bacillus subtilis Strain BLK-1.5 isolated from salt mines of Karak, Pakistan. Extremophiles 20, 395-402. doi: 10.1007/s00792-016-0830-1
10. Amoozegar, M. A., Fatemi, A. Z., Karbalaei-Heidari, H. R., and Razavi, M. R. (2007). Production of an extracellular alkaline metalloprotease from a newly isolated, moderately halophile, Salinivibrio sp. strain AF-2004. Microbiol. Res. 162, 369-377. doi: 10.1016/j.micres.2006.02.007
11. Anbu, P. (2013). Characterization of solvent stable extracellular protease from Bacillus koreensis (BK-P21A). Int. J. Biol. Macromol. 56, 162-168. doi: 10.1016/j.ijbiomac.2013.02.014
12. Annapurna, S. A., Singh, A., Garg, S., Kumar, A., and Kumar, H. (2012). Screening, isolation and characterisation of protease producing moderately halophilic microorganisms. Asian J. Microbiol. Biotech. Environ. Sci. 14, 603-612.
13. Antink, M. M. H., Sewczyk, T., Kroll, S., Árki, P., Beutel, S., Rezwan, K., et al. (2019). Proteolytic ceramic capillary membranes for the production of peptides under flow. Biochem. Eng. J. 147, 89-99. doi: 10.1016/j.bej.2019.04.005
14. Araujo, R., Casal, M., and Cavaco-Paulo, A. (2008). Application of enzymes for textile fibres processing. Biocatal. Biotransformation 26, 332-349. doi: 10.1080/10242420802390457
15. Ariyaei, A., Farhadi, A., Moradian, F., and Mianji, G. R. (2019). Cloning, expression and characterization of a novel alkaline serine protease gene from native Iranian Bacillus sp.; a producer of protease for use in livestock. Gene 69, 310-315. doi: 10.1016/j.gene.2019.01.020
16. Arora, N. K., and Mishra, J. (2016). Prospecting the roles of metabolites and additives in future bioformulations for sustainable agriculture. Appl. Soil Ecol. 107, 405-407. doi: 10.1016/j.apsoil.2016.05.020
17. Aruna, K., Shah, J., and Birmole, R. (2014). Production and partial characterization of alkaline protease from Bacillus tequilensis strains CSGAB0139 isolated from spoilt cottage cheese. Int J Appl Biol Pharm. 5, 201-221.
18. Asgher, M., Bashir, F., and Iqbal, H. M. (2018). Protease-based cross-linked enzyme aggregates with improved catalytic stability, silver removal, dehairing potentials. Int. J. Biol. Macromol. 118, 1247-1256. doi: 10.1016/j.ijbiomac.2018.06.107
19. Awad, H. M., Mostafa, E.-S. E., Saad, M. M., Selim, M. H., and Hassan, H. M. (2013). Partial purification and characterization of extracellular protease from a halophilic and thermotolerant strain Streptomyces pseudogrisiolus NRC-15. Indian. J. Biochem. Biophys. 50, 305-311.
20. Baker, P. J., and Numata, K. (2012). Chemoenzymatic synthesis of poly (L-alanine) in aqueous environment. Biomacromolecules 13, 947-951. doi: 10.1021/bm201862z
21. Banerjee, G., and Ray, A. K. (2017). Impact of microbial proteases on biotechnological industries. Biotechnol. Genet. Eng. Rev. 33, 119-143. doi: 10.1080/02648725.2017.1408256
22. Banerjee, U. C., Sani, R. K., Azmi, W., and Soni, R. (1999). Thermostable alkaline protease from Bacillus brevis and its characterization as a laundry detergent additive. Process Biochem. 35, 213-219. doi: 10.1016/S0032-9592(99)00053-9
23. Barrett, A. J. (1995). Methods in Enzymology. Proteolytic Enzymes: Aspartic and Metallo Peptidases, Vol. 248. Cambridge: Academic Press.
24. Barrett, A. J., and McDonald, J. K. (1986). Nomenclature: protease, proteinase and peptidase. Biochem. J. 237:935. doi: 10.1042/bj2370935
25. Barthomeuf, C., Pourrat, H., and Pourrat, A. (1992). Collagenolytic activity of a new semi-alkaline protease from Aspergillus niger. Journal of fermentation and bioengineering 73, 233-236. doi: 10.1016/0922-338X(92)90168-T
26. Bas, D., and Boyaci, I. H. (2007). Modeling and optimization I: usability of response surface methodology. J. Food Eng. 78, 836-845. doi: 10.1016/j.jfoodeng.2005.11.024
27. Bayoudh, A., Gharsallah, N., Chamkha, M., Dhouib, A., Ammar, S., and Nasri, M. (2000). Purification and characterization of an alkaline protease from Pseudomonas aeruginosa MN1. J. Ind. Microbiol. Biotechnol. 24, 291-295. doi: 10.1038/sj.jim.2900822
28. Bech, L. M., Branner, S., Breddam, K., and Groen, H. (1993). Oxidation Stable Detergent Enzymes. Google Patents.
29. Beg, Q. K., and Gupta, R. (2003). Purification and characterization of an oxidation-stable, thiol-dependent serine alkaline protease from Bacillus mojavensis. Enzyme Microb. Technol. 32, 294-304. doi: 10.1016/S0141-0229(02)00293-4
30. Beg, Q. K., Sahai, V., and Gupta, R. (2003). Statistical media optimization and alkaline protease production from Bacillus mojavensis in a bioreactor. Process Biochem. 39, 203-209. doi: 10.1016/S0032-9592(03)00064-5
31. Beg, Q. K., Saxena, R., and Gupta, R. (2002). Kinetic constants determination for an alkaline protease from Bacillus mojavensis using response surface methodology. Biotechnol. Bioeng. 78, 289-295. doi: 10.1002/bit.10203
32. Berchtold, M. W., Brinkmeier, H., and Muntener, M. (2000). Calcium ion in skeletal muscle: its crucial role for muscle function, plasticity, and disease. Physiol. Rev. 80, 1215-1265. doi: 10.1152/physrev.2000.80.3.1215
33. Bettiol, J.-L. P., and Showell, M. S. (2002). Detergent Compositions Comprising a Mannanase and a Protease. Google Patents.
34. Bhaskar, N., Sudeepa, E., Rashmi, H., and Selvi, A. T. (2007). Partial purification and characterization of protease of Bacillus proteolyticus CFR3001 isolated from fish processing waste and its antibacterial activities. Bioresour. Technol. 98, 2758-2764. doi: 10.1016/j.biortech.2006.09.033
35. Biolo, G., Fleming, R. D., and Wolfe, R. R. (1995). Physiologic hyperinsulinemia stimulates protein synthesis and enhances transport of selected amino acids in human skeletal muscle. J. Clin. Invest. 95, 811-819. doi: 10.1172/JCI117731
36. Blanch, H. W., and Moo-Young, M. (1985). Comprehensive Biotechnology: The Principles, Applications and Regulations of Biotechnology in Industry, Agriculture and Medicine. 3rd Edn. Oxford; Toronto, ON: Pergamon Press.
37. Bloor, A. E., and Cranenburgh, R. M. (2006). An efficient method of selectable marker gene excision by Xer recombination for gene replacement in bacterial chromosomes. Appl. Environ. Microbiol. 72, 2520-2525. doi: 10.1128/AEM.72.4.2520-2525.2006
38. Bohacz, J., and Kornillowicz-Kowalska, T. (2019). Fungal diversity and keratinolytic activity of fungi from lignocellulosic composts with chicken feathers. Process Biochem. 80, 119-128. doi: 10.1016/j.procbio.2019.02.012
39. Bond, J. S., and Beynon, R. J. (1986). Meprin: a membrane-bound metallo-endopeptidase. Curr. Top. Cell. Regul. 28, 263-290. doi: 10.1016/B978-0-12-152828-7.50009-3
40. Bond, J. S., and Beynon, R. J. (1995). The astacin family of metalloendopeptidases. Prot. Sci. 4, 1247-1261. doi: 10.1002/pro.5560040701
41. Bordusa, F. (2002). Proteases in organic synthesis. Chem. Rev. 102, 4817-4868. doi: 10.1021/cr010164d
42. Bornscheuer, U., Huisman, G., Kazlauskas, R., Lutz, S., Moore, J., and Robins, K. (2012). Engineering the third wave of biocatalysis. Nature 485:185. doi: 10.1038/nature11117
43. Boyer, P. D., and Krebs, E. G. (1986). The Enzymes. Vol. 17. Cambridge: Academic Press.
44. Brandelli, A., Daroit, D. J., and Riffel, A. (2010). Biochemical features of microbial keratinases and their production and applications. Appl. Microbiol. Biotechnol. 85, 1735-1750. doi: 10.1007/s00253-009-2398-5
45. Breuer, M., Ditrich, K., Habicher, T., Hauer, B., Keβeler, M., Stürmer, R., et al. (2004). Industrial methods for the production of optically active intermediates. Angew. Chem. Int. Ed. 43, 788-824. doi: 10.1002/anie.200300599
46. Calin, M., Constantinescu-Aruxandei, D., Alexandrescu, E., Raut, I., Doni, M. B., Arsene, M.-L., et al. (2017). Degradation of keratin substrates by keratinolytic fungi. Electron. J. Biotechnol. 28, 101-112. doi: 10.1016/j.ejbt.2017.05.007
47. Cappello, J., Crissman, J., Dorman, M., Mikolajczak, M., Textor, G., Marquet, M., et al. (1990). Genetic engineering of structural protein polymers. Biotechnol. Prog. 6, 198-202. doi: 10.1021/bp00003a006
48. Castilla, A., Panizza, P., Rodríguez, D., Bonino, L., Díaz, P., Irazoqui, G., et al. (2017). A novel thermophilic and halophilic esterase from Janibacter sp. R02, the first member of a new lipase family (Family XVII). Enzyme Microb. Technol. 98, 86-95. doi: 10.1016/j.enzmictec.2016.12.010
49. Cavello, I. A., Crespo, J. M., García, S. S., Zapiola, J. M., Luna, M. F., and Cavalitto, S. F. (2015). Plant growth promotion activity of keratinolytic fungi growing on a recalcitrant waste known as "Hair Waste". Biotechnol. Res. Int. 2015:952921. doi: 10.1155/2015/952921
50. Centeno, R., Espino, T., and Mercado, M. (1996). Purification and partial characterization of alkaline protease from Bacillus subtilis NRRL B-3749. Phil. J. Biotechol. 7, 25-34.
51. Chalamaiah, M., Hemalatha, R., and Jyothirmayi, T. (2012). Fish protein hydrolysates: Proximate composition, amino acid composition, antioxidant activities and applications: a review. Food Chem. 135, 3020-3038. doi: 10.1016/j.foodchem.2012.06.100
52. Chalker, J. M., Wood, C. S., and Davis, B. G. (2009). A convenient catalyst for aqueous and protein Suzuki-Miyaura cross-coupling. J. Am. Chem. Soc. 131, 16346-16347. doi: 10.1021/ja907150m
53. Charles, P., Devanathan, V., Anbu, P., Ponnuswamy, M., Kalaichelvan, P., and Hur, B. K. (2008). Purification, characterization and crystallization of an extracellular alkaline protease from Aspergillus nidulans HA-10. J. Basic Microbiol. 48, 347-352. doi: 10.1002/jobm.200800043
54. Chatterjee, J., Giri, S., Maity, S., Sinha, A., Ranjan, A., Rajshekhar, et al. (2015). Production and characterization of thermostable alkaline protease of Bacillus subtilis (ATCC 6633) from optimized solid-state fermentation. Biotechnol. Appl. Biochem. 62, 709-718. doi: 10.1002/bab.1309
55. Chavan, V., and Patil, N. (2007). Study of leukocytic hydrolytic enzymes in patients with acute stage of coronary heart disease. Indian J. Med. Sci. 61, 73-82.
56. Cheng, S.-W., Hu, H.-M., Shen, S.-W., Takagi, H., Asano, M., and Tsai, Y. C. (1995). Production and characterization of keratinase of a feather-degrading Bacillus licheniformis PWD-1. Biosci. Biotechnol. Biochem. 59, 2239-2243. doi: 10.1271/bbb.59.2239
57. Chi, C.-F., Wang, B., Wang, Y.-M., Zhang, B., and Deng, S.-G. (2015). Isolation and characterization of three antioxidant peptides from protein hydrolysate of bluefin leatherjacket (Navodon septentrionalis) heads. J. Funct. Foods 12, 1-10. doi: 10.1016/j.jff.2014.10.027
58. Chou, J. J., Matsuo, H., Duan, H., and Wagner, G. (1998). Solution structure of the RAIDD CARD and model for CARD/CARD interaction in caspase-2 and caspase-9 recruitment. Cell 94, 171-180. doi: 10.1016/S0092-8674(00)81417-8
59. Chou, K.-C. (2004). Structural bioinformatics and its impact to biomedical science. Curr. Med. Chem. 11, 2105-2134. doi: 10.2174/0929867043364667
60. Chou, K.-C. (2006). Structural bioinformatics and its impact to biomedical science and drug discovery. Front. Med. Chem. 3, 455-502. doi: 10.2174/978160805206610603010455
61. Chou, K.-C., and Howe, W. J. (2002). Prediction of the tertiary structure of the β-secretase zymogen. Biochem. Biophys. Res. Commun. 292, 702-708. doi: 10.1006/bbrc.2002.6686
62. Chou, K.-C., Jones, D., and Heinrikson, R. L. (1997). Prediction of the tertiary structure and substrate binding site of caspase-8. FEBS Lett. 419, 49-54. doi: 10.1016/S0014-5793(97)01246-5
63. Chou, K.-C., Tomasselli, A. G., and Heinrikson, R. L. (2000). Prediction of the tertiary structure of a caspase-9/inhibitor complex. FEBS Lett. 470, 249-256. doi: 10.1016/S0014-5793(00)01333-8
64. Chou, K.-C., Wei, D.-Q., and Zhong, W.-Z. (2003). Binding mechanism of coronavirus main proteinase with ligands and its implication to drug design against SARS. Biochem. Biophys. Res. Commun. 308, 148-151. doi: 10.1016/S0006-291X(03)01342-1
65. Clemente, A. (2000). Enzymatic protein hydrolysates in human nutrition. Trends Food Sci. Technol. 11, 254-262. doi: 10.1016/S0924-2244(01)00007-3
66. Coker, J. A. (2016). Extremophiles and biotechnology: current uses and prospects. F1000Res. 5:F1000 Faculty Rev-396. doi: 10.12688/f1000research.7432.1
67. Connelly, M. B., Young, G. M., and Sloma, A. (2004). Extracellular proteolytic activity plays a central role in swarming motility in Bacillus subtilis. J. Bacteriol. 186, 4159-4167. doi: 10.1128/JB.186.13.4159-4167.2004
68. Corral, J. C. C., de los Santos Villalobos, S., Barrgàn, L. A. P., Figueroa, J. J. B., Vásquez-Murrieta, M. S., Estrada Alvarado, M. I., et al. (2018). Isolation of moderately halophilic bacteria in saline environments of Sonora State searching for proteolytic hydrolases. Open Agric. 3, 207-213. doi: 10.1515/opag-2018-0021
69. Csuk, R., and Glaenzer, B. I. (1991). Baker's yeast mediated transformations in organic chemistry. Chem. Rev. 91, 49-97. doi: 10.1021/cr00001a004
70. Cunningham, E. L., and Agard, D. A. (2003). Interdependent folding of the N- and C-terminal domains defines the cooperative folding of a-lytic protease. Biochemistry 42, 13212-13219. doi: 10.1021/bi035409q
71. da Silva, O. S., Gomes, M. H. G., de Oliveira, R. L., Porto, A. L. F., Converti, A., and Porto, T. S. (2017). Partitioning and extraction protease from Aspergillus tamarii URM4634 using PEG-citrate aqueous two-phase systems. Biocatal. Agric. Biotechnol. 91, 68-73. doi: 10.1016/j.bcab.2016.12.012
72. D'Amico, S., Claverie, P., Collins, T., Georlette, D., Gratia, E., Hoyoux, A., et al. (2002). Molecular basis of cold adaptation. Philos. Trans. R. Soc. Lond. Series B Biol. Sci. 357, 917-925. doi: 10.1098/rstb.2002.1105
73. Das, G., and Prasad, M. (2010). Isolation, purification & mass production of protease enzyme from Bacillus subtilis. Int. Res. J. Microbiol. 1, 26-31.
74. Davidenko, T. (1999). Immobilization of alkaline protease on polysaccharides of microbial origin. Pharma. Chem. J. 33, 487-489. doi: 10.1007/BF02510074
75. Dawson, P. E., and Kent, S. B. (2000). Synthesis of native proteins by chemical ligation. Annu. Rev. Biochem. 69, 923-960. doi: 10.1146/annurev.biochem.69.1.923
76. De Maayer, P., Anderson, D., Cary, C., and Cowan, D. A. (2014). Some like it cold: Understanding the survival strategies of psychrophiles. EMBO Rep. 15, 508-517. doi: 10.1002/embr.201338170
77. de Souza Vandenberghe, L. P., Karp, S. G., Pagnoncelli, M. G. B., Rodrigues, C., Medeiros, A. B. P., and Soccol, C. R. (2019). "Digestive enzymes: industrial applications in food products," in Green Bio-processes, eds B. Parameswaran, S. Varjani, and S. Raveendran (Singapore: Springer), 267-291. doi: 10.1007/978-981-13-3263-0_14
78. De Virgilio, C., Bürckert, N., Bell, W., Jenö, P., Boller, T., and Wiemken, A. (1993). Disruption of TPS2, the gene encoding the 100-kDa subunit of the trehalose-6-phosphate synthase/phosphatase complex in Saccharomyces cerevisiae, causes accumulation of trehalose-6-phosphate and loss of trehalose-6-phosphate phosphatase activity. Eur. J. Biochem. 212, 315-323. doi: 10.1111/j.1432-1033.1993.tb17664.x
79. De Vos, W. M. (1987). Gene cloning and expression in lactic streptococci. FEMS Microbiol. Rev. 3, 281-295. doi: 10.1016/0378-1097(87)90113-3
80. Deng, A., Wu, J., Zhang, Y., Zhang, G., and Wen, T. (2010). Purification and characterization of a surfactant-stable high-alkaline protease from Bacillus sp. B001. Bioresour. Technol. 101, 7100-7106. doi: 10.1016/j.biortech.2010.03.130
81. Desautels, M., and Goldberg, A. (1982). Demonstration of an ATP-dependent, vanadate-sensitive endoprotease in the matrix of rat liver mitochondria. J. Biol. Chem. 257, 11673-11679.
82. Dhawan, S., and Kaur, J. (2007). Microbial mannanases: an overview of production and applications. Crit. Rev. Biotechnol. 27, 197-216. doi: 10.1080/07388550701775919
83. Dias, D. R., Vilela, D. M., Silvestre, M. P. C., and Schwan, R. F. (2008). Alkaline protease from Bacillus sp. isolated from coffee bean grown on cheese whey. World J. Microbiol. Biotechnol. 24, 2027-2034. doi: 10.1007/s11274-008-9706-6
84. Dodia, M., Rawal, C., Bhimani, H., Joshi, R., Khare, S., and Singh, S. P. (2008). Purification and stability characteristics of an alkaline serine protease from a newly isolated Haloalkaliphilic bacterium sp. AH-6. J. Ind. Microbiol. Biotechnol. 35, 121-131. doi: 10.1007/s10295-007-0273-x
85. dos Santos Aguilar, J. G., and Sato, H. H. (2018). Microbial proteases: production and application in obtaining protein hydrolysates. Food Res. Int. 103, 253-262. doi: 10.1016/j.foodres.2017.10.044
86. Drew, S., Daniel, I. W., Moo-Young, M., and Blanch, H. W. (1985). Comprehensive Biotechnology: The Principles, Applications and Regulations of Biotechnology in Industry, Agriculture and Medicine. Oxford: Pergamon Press.
87. Driscoll, J., Brown, M. G., Finley, D., and Monaco, J. J. (1993). MHC-linked LMP gene products specifically alter peptidase activities of the proteasome. Nature 365:262. doi: 10.1038/365262a0
88. Dumas, A., Spicer, C. D., Gao, Z., Takehana, T., Lin, Y. A., Yasukohchi, T., et al. (2013). Self-liganded Suzuki-Miyaura coupling for site-selective protein PEGylation. Angew. Chem. Int. Ed. 52, 3916-3921. doi: 10.1002/anie.201208626
89. Eichler, J. (2001). Biotechnological uses of archaeal extremozymes. Biotechnol. Adv. 19, 261-278. doi: 10.1016/S0734-9750(01)00061-1
90. El-Gamal, M. S., Abdel-Shakour, E. H., Abdel-Rahman, M. A., and Attia, A. A. (2012). Protease productivity by some thermoalkalotolerant gram positive bacteria isolated from manure. Egypt J. Biotechnol. 41, 1-25.
91. Ellaiah, P., Srinivasulu, B., and Adinarayana, K. (2002). A review on microbial alkaline proteases. J. Sci. Ind. Res. 61, 690-704.
92. Epstein, D., and Wensink, P. (1988). The alpha-lytic protease gene of Lysobacter enzymogenes. The nucleotide sequence predicts a large prepro-peptide with homology to pro-peptides of other chymotrypsin-like enzymes. J. Biol. Chem. 263, 16586-16590.
93. Estell, D. A., Graycar, T. P., and Wells, J. A. (1985). Engineering an enzyme by site-directed mutagenesis to be resistant to chemical oxidation. J. Biol. Chem. 260, 6518-6521.
94. Fagan, J. M., Waxman, L., and Goldberg, A. L. (1987). Skeletal muscle and liver contain a soluble ATP+ ubiquitin-dependent proteolytic system. Biochem. J. 243, 335-343. doi: 10.1042/bj2430335
95. Fang, Z., Yong, Y.-C., Zhang, J., Du, G., and Chen, J. (2017a). Keratinolytic protease: a green biocatalyst for leather industry. Appl. Microbiol. Biotechnol. 101, 7771-7779. doi: 10.1007/s00253-017-8484-1
96. Fang, Z., Zhang, J., Du, G., and Chen, J. (2017b). Rational protein engineering approaches to further improve the keratinolytic activity and thermostability of engineered keratinase KerSMD. Biochem. Eng. J. 127, 147-153. doi: 10.1016/j.bej.2017.08.010
97. Fang, Z., Zhang, J., Liu, B., Du, G., and Chen, J. (2016). Enhancement of the catalytic efficiency and thermostability of Stenotrophomonas sp. keratinase KerSMD by domain exchange with KerSMF. Microb. Biotechnol. 9, 35-46. doi: 10.1111/1751-7915.12300
98. Fitzgerald, P., McKeever, B., VanMiddlesworth, J. F., Springer, J. P., Heimbach, J. C., Leu, C. T., et al. (1990). Crystallographic analysis of a complex between human immunodeficiency virus type 1 protease and acetyl-pepstatin at 2.0-A resolution. J. Biol. Chem. 265, 14209-14219. doi: 10.2210/pdb5hvp/pdb
99. Foegeding, E. A., Davis, J. P., Doucet, D., and McGuffey, M. K. (2002). Advances in modifying and understanding whey protein functionality. Trends Food Sci. Technol. 13, 151-159. doi: 10.1016/S0924-2244(02)00111-5
100. Gamblin, D. P., Scanlan, E. M., and Davis, B. G. (2008). Glycoprotein synthesis: an update. Chem. Rev. 109, 131-163. doi: 10.1021/cr078291i
101. Gessesse, A. (1997). The use of nug meal as a low-cost substrate for the production of alkaline protease by the alkaliphilic Bacillus sp. AR-009 and some properties of the enzyme. Bioresour. Technol. 62, 59-61. doi: 10.1016/S0960-8524(97)00059-X
102. Giménez, M. I., Studdert, C. A., Sánchez, J. J., and De Castro, R. E. (2000). Extracellular protease of Natrialba magadii: purification and biochemical characterization. Extremophiles 4, 181-188. doi: 10.1007/s007920070033
103. Godfrey, T., and West, S. (1996a). Textiles. Ind. Enzymol. 3, 60-71.
104. Godfrey, T., and West, S. (1996b). "Introduction to industrial enzymology," in Industrial Enzymology, eds T. Godfrey and S. West (London: Mac. Millan Press).
105. Goll, D. E., Thompson, V. F., Taylor, R. G., and Zalewska, T. (1992). Is calpain activity regulated by membranes and autolysis or by calcium and calpastatin? Bioessays 14, 549-556. doi: 10.1002/bies.950140810
106. Gomes, A. V., Zong, C., Edmondson, R. D., Li, X., Stefani, E., Jones, R. C., et al. (2006). Mapping the murine cardiac 26S proteasome complexes. Circ. Res. 99, 362-371. doi: 10.1161/01.RES.0000237386.98506.f7
107. Gómez-Guillén, M., Giménez, B., López-Caballero, M., and Montero, M. P. (2011). Functional and bioactive properties of collagen and gelatin from alternative sources: a review. Food Hydrocoll. 25, 1813-1827. doi: 10.1016/j.foodhyd.2011.02.007
108. Govinden, G., and Puchooa, D. (2012). Isolation and characterization of feather degrading bacteria from Mauritian soil. Afr. J. Biotechnol. 11, 13591-13600. doi: 10.5897/AJB12.1683
109. Greene, R. V., Cotta, M. A., and Griffin, H. L. (1989). A novel, symbiotic bacterium isolated from marine shipworm secretes proteolytic activity. Curr. Microbiol. 19, 353-356. doi: 10.1007/BF01570881
110. Guillaume, B., Chapiro, J., Stroobant, V., Colau, D., Van Holle, B., Parvizi, G., et al. (2010). Two abundant proteasome subtypes that uniquely process some antigens presented by HLA class I molecules. Proc. Natl. Acad. Sci. U.S.A. 107, 18599-18604. doi: 10.1073/pnas.1009778107
111. Guleria, S., Walia, A., Chauhan, A., and Shirkot, C. (2016). Molecular characterization of alkaline protease of Bacillus amyloliquefaciens SP1 involved in biocontrol of Fusarium oxysporum. Int. J. Food Microbiol. 232, 134-143. doi: 10.1016/j.ijfoodmicro.2016.05.030
112. Gupta, A., Joseph, B., Mani, A., and Thomas, G. (2008). Biosynthesis and properties of an extracellular thermostable serine alkaline protease from Virgibacillus pantothenticus. World J. Microbiol. Biotechnol. 24, 237-243. doi: 10.1007/s11274-007-9462-z
113. Gupta, A., and Khare, S. (2007). Enhanced production and characterization of a solvent stable protease from solvent tolerant Pseudomonas aeruginosa PseA. Enzyme Microb. Technol. 42, 11-16. doi: 10.1016/j.enzmictec.2007.07.019
114. Gupta, R., Beg, Q., and Lorenz, P. (2002). Bacterial alkaline proteases: molecular approaches and industrial applications. Appl. Microbiol. Biotechnol. 59, 15-32. doi: 10.1007/s00253-002-0975-y
115. Gupta, R., Gupta, K., Saxena, R., and Khan, S. (1999). Bleach-stable, alkaline protease from Bacillus sp. Biotechnol. Lett. 21, 135-138. doi: 10.1023/A:1005478117918
116. Gupta, R., and Ramnani, P. (2006). Microbial keratinases and their prospective applications: an overview. Appl. Microbiol. Biotechnol. 70:21. doi: 10.1007/s00253-005-0239-8
117. Haddar, A., Agrebi, R., Bougatef, A., Hmidet, N., Sellami-Kamoun, A., and Nasri, M. (2009a). Two detergent stable alkaline serine-proteases from Bacillus mojavensis A21: purification, characterization and potential application as a laundry detergent additive. Bioresour. Technol. 100, 3366-3373. doi: 10.1016/j.biortech.2009.01.061
118. Haddar, A., Bougatef, A., Agrebi, R., Sellami-Kamoun, A., and Nasri, M. (2009b). A novel surfactant-stable alkaline serine-protease from a newly isolated Bacillus mojavensis A21. Purification and characterization. Process Biochem. 44, 29-35. doi: 10.1016/j.procbio.2008.09.003
119. Haki, G., and Rakshit, S. (2003). Developments in industrially important thermostable enzymes: a review. Bioresour. Technol. 89, 17-34. doi: 10.1016/S0960-8524(03)00033-6
120. Hamza, T. A. (2017a). Bacterial protease enzyme: Safe and good alternative for industrial and commercial use. Int. J. Chem. Biomol. Sci. 3, 1-10.
121. Hamza, T. A. (2017b). Isolation and screening of protease producing bacteria from local environment for detergent additive. Am. J. Life Sci. 5:116. doi: 10.11648/j.ajls.20170505.11
122. He, R., Girgih, A. T., Malomo, S. A., Ju, X., and Aluko, R. E. (2013). Antioxidant activities of enzymatic rapeseed protein hydrolysates and the membrane ultrafiltration fractions. J. Funct. Foods 5, 219-227. doi: 10.1016/j.jff.2012.10.008
123. Heck, T., Faccio, G., Richter, M., and Thöny-Meyer, L. (2013). Enzyme-catalyzed protein crosslinking. Appl. Microbiol. Biotechnol. 97, 461-475. doi: 10.1007/s00253-012-4569-z
124. Helianti, I., Furgeva, N., Mulyawati, L., Ferniah, R. S., and Kusumaningrum, H. P. (2018). Cloning of a gene encoding protease from Bacillus halodurans CM1 into Escherichia coli DH5a and expression analyses of the gene product. Makara J. Sci. 22, 113-120. doi: 10.7454/mss.v22i3.9900
125. Henderson, G., Krygsman, P., Liu, C., Davey, C. C., and Malek, L. T. (1987). Characterization and structure of genes for proteases A and B from Streptomyces griseus. J. Bacteriol. 169, 3778-3784. doi: 10.1128/jb.169.8.3778-3784.1987
126. Henner, D. J., Yang, M., Band, L., and Wells, J. (1985). "Expression of cloned protease genes in Bacillus subtilis," in Proceedings of the 9th International Spore Conference, 95-103.
127. Hershko, A., and Ciechanover, A. (1998). The ubiquitin system. Ann. Rev. 67, 425-479. doi: 10.1007/978-1-4899-1922-9_1
128. Hockemeyer, D., Wang, H., Kiani, S., Lai, C. S., Gao, Q., Cassady, J. P., et al. (2011). Genetic engineering of human pluripotent cells using TALE nucleases. Nat. Biotechnol. 29:731. doi: 10.1038/nbt.1927
129. Hogdson, J. (1994). The changing bulk biocatalyst market: recombinant DNA techniques have changed bulk enzyme production dramatically. Biotechnology 12, 789-790. doi: 10.1038/nbt0894-789
130. Homaei, A., Lavajoo, F., and Sariri, R. (2016). Development of marine biotechnology as a resource for novel proteases and their role in modern biotechnology. Int. J. Biol. Macromol. 88, 542-552. doi: 10.1016/j.ijbiomac.2016.04.023
131. Hossain, M. M., Sultana, F., and Islam, S. (2017). "Plant growth-promoting fungi (PGPF): phytostimulation and induced systemic resistance," in Plant-Microbe Interactions in Agro-Ecological Perspectives, eds D. P. Singh, H. B. Singh, and R. Prabha (Singapore: Springer), 135-191. doi: 10.1007/978-981-10-6593-4_6
132. Hosse, R. J., Rothe, A., and Power, B. E. (2006). A new generation of protein display scaffolds for molecular recognition. Prot. Sci. 15, 14-27. doi: 10.1110/ps.051817606
133. Hough, R. F., Pratt, G. W., and Rechsteiner, M. (1988). "Ubiquitin/ATP-dependent protease," in Ubiquitin, ed M. Rechsteiner (Boston, MA: Springer), 101-134. doi: 10.1007/978-1-4899-2049-2_5
134. Hsiao, H.-Y., Fodge, D. W., and LaLonde, J. J. (1994). Alkaline Proteases Stable in Heavy-Duty Detergent Liquids. Google Patents.
135. Huang, M., Chen, R., and Ren, G. (2017). Secretory expression and purification of Bacillus licheniformis keratinase in insect cells. PLoS ONE 12:e0183764. doi: 10.1371/journal.pone.0183764
136. Hwang, D. H., Kim, J. C., Kim, J., Byun, S. M., and Chun, M. (1993). Molecular cloning and nucleotide sequence of the protease B gene from Streptomyces griseus ATCC 10137. Korean Biochem. J. 181, 707-713.
137. Ichida, J. M., Krizova, L., LeFevre, C. A., Keener, H. M., Elwell, D. L., Burtt, Jr., et al. (2001). Bacterial inoculum enhances keratin degradation and biofilm formation in poultry compost. J. Microbiol. Methods 47, 199-208. doi: 10.1016/S0167-7012(01)00302-5
138. Idbeaa, A., and Omar, I. (2016). Alkaline Protease Production Using Submerged Fermentation From Different Species of Bacillus. Biotechnology and Bioengineering Sam Higginbottom Institute of Agriculture, Technology and Sciences, Allahabad.
139. Illanes, A. (2008). Enzyme Biocatalysis. Principles and Applications. New York, NY: Springer-Verlag New York Inc. doi: 10.1007/978-1-4020-8361-7
140. Intarasirisawat, R., Benjakul, S., Wu, J., and Visessanguan, W. (2013). Isolation of antioxidative and ACE inhibitory peptides from protein hydrolysate of skipjack (Katsuwana pelamis) roe. J. Funct. Foods 5, 1854-1862. doi: 10.1016/j.jff.2013.09.006
141. Ito, S., Kobayashi, T., Ara, K., Ozaki, K., Kawai, S., and Hatada, Y. (1998). Alkaline detergent enzymes from alkaliphiles: enzymatic properties, genetics, and structures. Extremophiles 2, 185-190. doi: 10.1007/s007920050059
142. Jäckel, C., and Koksch, B. (2005). Fluorine in peptide design and protein engineering. Eur. J. Org. Chem. 2005, 4483-4503. doi: 10.1002/ejoc.200500205
143. Jacobs, M. F. (1995). Expression of the subtilisin Carlsberg-encoding gene in Bacillus licheniformis and Bacillus subtilis. Gene 152, 69-74. doi: 10.1016/0378-1119(94)00655-C
144. Jacobson, J. W., Glick, J. L., and Madello, K. L. (1985). Composition for Cleaning Drains Clogged With Deposits Containing Hair. Google Patents.
145. Jadhav, U., and Hocheng, H. (2012). A review of recovery of metals from industrial waste. J. Achiev. Mater. Manufac. Eng. 54, 159-167.
146. Jakubke, H. D. (1994). Protease-catalyzed peptide synthesis: basic principles, new synthesis strategies and medium engineering. J. Chinese Chem. Soc. 41, 355-370. doi: 10.1002/jccs.199400049
147. Jaouadi, B., Abdelmalek, B., and Jaouadi Zaraî, B. N. (2011). "The bioengineering and industrial applications of bacterial alkaline proteases: the case of SAPB and KERAB," in Progress in Molecular and Environmental Bioengineering-From Analysis and Modeling to Technology Applications, ed A. Carpi (InTechOpen) 445-466. doi: 10.5772/23850
148. Jaouadi, B., Ellouz-Chaabouni, S., Rhimi, M., and Bejar, S. (2008). Biochemical and molecular characterization of a detergent-stable serine alkaline protease from Bacillus pumilus CBS with high catalytic efficiency. Biochimie 90, 1291-1305. doi: 10.1016/j.biochi.2008.03.004
149. Jaouadi, N. Z., Jaouadi, B., Aghajari, N., and Bejar, S. (2012). The overexpression of the SAPB of Bacillus pumilus CBS and mutated sapB-L31I/T33S/N99Y alkaline proteases in Bacillus subtilis DB430: new attractive properties for the mutant enzyme. Bioresour. Technol. 105, 142-151. doi: 10.1016/j.biortech.2011.11.115
150. Jeong, Y. J., Baek, S. C., and Kim, H. (2018). Cloning and characterization of a novel intracellular serine protease (IspK) from Bacillus megaterium with a potential additive for detergents. Int. J. Biol. Macromol. 108, 808-816. doi: 10.1016/j.ijbiomac.2017.10.173
151. Johnvesly, B., and Naik, G. (2001). Studies on production of thermostable alkaline protease from thermophilic and alkaliphilic Bacillus sp. JB-99 in a chemically defined medium. Process Biochem. 37, 139-144. doi: 10.1016/S0032-9592(01)00191-1
152. Joo, H.-S., Kumar, C. G., Park, G.-C., Kim, K. T., Paik, S. R., and Chang, C.-S. (2002). Optimization of the production of an extracellular alkaline protease from Bacillus horikoshii. Process Biochem. 38, 155-159. doi: 10.1016/S0032-9592(02)00061-4
153. Joo, H.-S., Kumar, C. G., Park, G.-C., Paik, S. R., and Chang, C.-S. (2004). Bleach-resistant alkaline protease produced by a Bacillus sp. isolated from the Korean polychaete, Periserrula leucophryna. Process Biochem. 39, 1441-1447. doi: 10.1016/S0032-9592(03)00260-7
154. Joshi, S., and Satyanarayana, T. (2013). Characteristics and applications of a recombinant alkaline serine protease from a novel bacterium Bacillus lehensis. Bioresour. Technol. 131, 76-85. doi: 10.1016/j.biortech.2012.12.124
155. Kalaiarasi, K., and Sunitha, P. (2009). Optimization of alkaline protease production from Pseudomonas fluorescens isolated from meat waste contaminated soil. Afr. J. Biotechnol. 8, 7035-7041. doi: 10.5897/AJB2009.000-9547
156. Kalaikumari, S. S., Vennila, T., Monika, V., Chandraraj, K., Gunasekaran, P., and Rajendhran, J. (2019). Bioutilization of poultry feather for keratinase production and its application in leather industry. J. Clean. Prod. 208, 44-53. doi: 10.1016/j.jclepro.2018.10.076
157. Kalisz, H. M. (1988). "Microbial proteinasesm" in Enzyme Studies. Advances in Biochemical Engineering/Biotechnology, Vol. 36, ed A. Fiechter (Berlin; Heidelberg: Springer), 1-65. doi: 10.1007/BFb0047944
158. Kaneko, R., Koyama, N., Tsai, Y.-C., Juang, R.-Y., Yoda, K., and Yamasaki, M. (1989). Molecular cloning of the structural gene for alkaline elastase YaB, a new subtilisin produced by an alkalophilic Bacillus strain. J. Bacteriol. 171, 5232-5236. doi: 10.1128/jb.171.9.5232-5236.1989
159. Kang, S. G., Kim, I. S., Rho, Y. T., and Lee, K. J. (1995). Production dynamics of extracellular proteases accompanying morphological differentiation of Streptomyces albidoflavus SMF301. Microbiology 141, 3095-3103. doi: 10.1099/13500872-141-12-3095
160. Kanmani, R., Dhivya, S., Jayalakshmi, S., and Vijayabaskar, P. (2011). Studies on detergent additives of protease enzyme from an estuarine bacterium Bacillus cereus. Int. Res. J. Biotechnol. 2, 157-163.
161. Keil, B. (2012). Specificity of Proteolysis. Berlin; Heidelberg: Springer Science and Business Media; Springer-Verlag.
162. Kenny, J. (1986). Cell surface peptidases are neither peptide-nor organ-specific. Trends Biochem. Sci. 11, 40-42. doi: 10.1016/0968-0004(86)90231-8
163. Kittiphattanabawon, P., Benjakul, S., Visessanguan, W., and Shahidi, F. (2012). Gelatin hydrolysate from blacktip shark skin prepared using papaya latex enzyme: antioxidant activity and its potential in model systems. Food Chem. 135, 1118-1126. doi: 10.1016/j.foodchem.2012.05.080
164. Kleinschmidt, J. A., Escher, C., and Wolf, D. H. (1988). Proteinase yscE of yeast shows homology with the 20 S cylinder particles of Xenopus laevis. FEBS Lett. 239, 35-40. doi: 10.1016/0014-5793(88)80540-4
165. Kloetzel, P. M. (2004). Generation of major histocompatibility complex class I antigens: functional interplay between proteasomes and TPPII. Nat. Immunol. 5:661. doi: 10.1038/ni1090
166. Kocher, G., and Mishra, S. (2009). Immobilization of Bacillus circulans MTCC 7906 for enhanced production of alkaline protease under batch and packed bed fermentation conditions. Internet J. Microbiol. 7, 359-378. doi: 10.5580/2599
167. Kohno, H., Kanda, S., and Kanno, T. (1986). Immunoaffinity purification and characterization of leucine aminopeptidase from human liver. J. Biol. Chem. 261, 10744-10748.
168. Kostyleva, E., Sereda, A., Velikoretskaya, I., Nefedova, L., Sharikov, A. Y., Tsurikova, N., et al. (2016). A new Bacillus licheniformis mutant strain producing serine protease efficient for hydrolysis of soy meal proteins. Microbiology 85, 462-470. doi: 10.1134/S0026261716040123
169. Kotb, E. (2013). Activity assessment of microbial fibrinolytic enzymes. Appl. Microbiol. Biotechnol. 97, 6647-6665. doi: 10.1007/s00253-013-5052-1
170. Krasileva, K. V. (2019a). The role of transposable elements and DNA damage repair mechanisms in gene amplification and protein domain shuffling in plant genomes. PeerJ Preprints 7:e27486v1. doi: 10.7287/peerj.preprints.27486v1
171. Krasileva, K. V. (2019b). The role of transposable elements and DNA damage repair mechanisms in gene duplications and gene fusions in plant genomes. Curr. Opin. Plant Biol. 48, 18-25. doi: 10.1016/j.pbi.2019.01.004
172. Krishnaveni, K., Kumar, D. M., Balakumaran, M., Ramesh, S., and Kalaichelvan, P. (2012). Production and optimization of extracellular Alkaline Protease from Bacillus subtilis isolated from dairy effluent. Der Pharm. Lett. 4, 98-109.
173. Kuhad, R. C., Gupta, R., and Singh, A. (2011). Microbial cellulases and their industrial applications. Enzyme Res. (2011) 2011:280696. doi: 10.4061/2011/280696
174. Kumar, C. G., Malik, R., and Tiwari, M. (1998). Novel enzyme-based detergents: an Indian perspective. Curr. Sci. 75, 1312-1318.
175. Kumar, C. G., and Takagi, H. (1999). Microbial alkaline proteases: from a bioindustrial viewpoint. Biotechnol. Adv. 17, 561-594. doi: 10.1016/S0734-9750(99)00027-0
176. Kumar, D. M., Premavathi, V., Govindarajan, N., Balakumaran, M., and Kalaichelvan, P. (2012). Production and purification of alkaline protease from Bacillus sp. MPTK 712 isolated from dairy sludge. Global Vet. 8, 433-439.
177. Kumar, N. S., Nazeer, R., and Jaiganesh, R. (2012). Purification and identification of antioxidant peptides from the skin protein hydrolysate of two marine fishes, horse mackerel (Magalaspis cordyla) and croaker (Otolithes ruber). Amino Acids 42, 1641-1649. doi: 10.1007/s00726-011-0858-6
178. Lasekan, A., Bakar, F. A., and Hashim, D. (2013). Potential of chicken by-products as sources of useful biological resources. Waste Manage. 33, 552-565. doi: 10.1016/j.wasman.2012.08.001
179. Lateef, A., Adelere, I. A., and Gueguim-Kana, E. B. (2015). Bacillus safensis LAU 13: a new source of keratinase and its multi-functional biocatalytic applications. Biotech. Biotechnol. Equip. 29, 54-63. doi: 10.1080/13102818.2014.986360
180. Li, J., Chi, Z., Wang, X., Peng, Y., and Chi, Z. (2009). The selection of alkaline protease-producing yeasts from marine environments and evaluation of their bioactive peptide production. Chinese J. Oceanol. Limnol. 27:753. doi: 10.1007/s00343-009-9198-8
181. Li, Q., Yi, L., Marek, P., and Iverson, B. L. (2013). Commercial proteases: present and future. FEBS Lett. 587, 1155-1163. doi: 10.1016/j.febslet.2012.12.019
182. Li, Y., Jiang, B., Zhang, T., Mu, W., and Liu, J. (2008). Antioxidant and free radical-scavenging activities of chickpea protein hydrolysate (CPH). Food Chem. 106, 444-450. doi: 10.1016/j.foodchem.2007.04.067
183. Liu, B., Zhang, J., Fang, Z., Du, G., Chen, J., and Liao, X. (2014). Functional analysis of the C-terminal propeptide of keratinase from Bacillus licheniformis BBE11-1 and its effect on the production of keratinase in Bacillus subtilis. Process Biochem. 49, 1538-1542. doi: 10.1016/j.procbio.2014.04.021
184. Liu, J., Sharma, A., Niewiara, M. J., Singh, R., Ming, R., and Yu, Q. (2018). Papain-like cysteine proteases in Carica papaya: lineage-specific gene duplication and expansion. BMC Genomics 19:26. doi: 10.1186/s12864-017-4394-y
185. Ljungdahl, P. O. (2009). Amino-Acid-Induced Signalling via the SPS-Sensing Pathway in Yeast. Stockholm: Portland Press Limited, 242-247. doi: 10.1042/BST0370242
186. Machado, A. R. G. M., Teixeira, M. F. S., de Souza Kirsch, L., Campelo, M. d C. L., and de Aguiar Oliveira, I. M. (2016). Nutritional value and proteases of Lentinus citrinus produced by solid state fermentation of lignocellulosic waste from tropical region. Saudi J. Biol. Sci. 23, 621-627. doi: 10.1016/j.sjbs.2015.07.002
187. Madern, D., Ebel, C., and Zaccai, G. (2000). Halophilic adaptation of enzymes. Extremophiles 4, 91-98. doi: 10.1007/s007920050142
188. Mahajan, R., Chaudhari, G., and Chopadaa, M. (2016). Report on Biotechnological applications of proteolytic enzymes from lattices of euphorbian plants. J. Appl. Biotechnol. Rep. 2, 333-337. doi: 10.21276/ijlssr.2016.2.4.7
189. Manirujjaman, M., Amin, R., Nahid, A., and Alam, M. (2016). Isolation and characterization of feather degrading bacteria from poultry waste. Afr. J. Bacteriol. Res. 8, 14-21.
190. Margesin, R., Neuner, G., and Storey, K. B. (2007). Cold-loving microbes, plants, and animals-fundamental and applied aspects. Naturwissenschaften 94, 77-99. doi: 10.1007/s00114-006-0162-6
191. Margesin, R., and Schinner, F. (2001). Potential of halotolerant and halophilic microorganisms for biotechnology. Extremophiles 5, 73-83. doi: 10.1007/s007920100184
192. Mascini, M., Palchetti, I., and Tombelli, S. (2012). Nucleic acid and peptide aptamers: fundamentals and bioanalytical aspects. Angew. Chem. Int. Ed. 51, 1316-1332. doi: 10.1002/anie.201006630
193. Masui, A., Yasuda, M., Fujiwara, N., and Ishikawa, H. (2004). Enzymatic hydrolysis of gelatin layers on used lith film using thermostable alkaline protease for recovery of silver and PET film. Biotechnol. Prog. 20, 1267-1269. doi: 10.1021/bp030058s
194. Mehde, A. A., Mehdi, W. A., Özacar, M., and Özacar, Z. Z. (2018). Evaluation of different saccharides and chitin as eco-friendly additive to improve the magnetic cross-linked enzyme aggregates (CLEAs) activities. Int. J. Biol. Macromol. 118, 2040-2050. doi: 10.1016/j.ijbiomac.2018.07.075
195. Melloni, E., and Pontremoli, S. (1989). The calpains. Trends Neurosci. 12, 438-444. doi: 10.1016/0166-2236(89)90093-3
196. Mienda, B. S., and Yahya, A. (2011). Engineering of microbial proteases: improving stability and catalytic performances. IIOAB J. 2, 10-15.
197. Mitsuiki, S., Ichikawa, M., Oka, T., Sakai, M., Moriyama, Y., Sameshima, Y., et al. (2004). Molecular characterization of a keratinolytic enzyme from an alkaliphilic Nocardiopsis sp. TOA-1. Enzyme Microb. Technol. 34, 482-489. doi: 10.1016/j.enzmictec.2003.12.011
198. Mittler, R., and Blumwald, E. (2010). Genetic engineering for modern agriculture: challenges and perspectives. Annu. Rev. Plant Biol. 61, 443-462. doi: 10.1146/annurev-arplant-042809-112116
199. Miyaji, T., Otta, Y., Nakagawa, T., Watanabe, T., Niimura, Y., and Tomizuka, N. (2006). Purification and molecular characterization of subtilisin-like alkaline protease BPP-A from Bacillus pumilus strain MS-1. Lett. Appl. Microbiol. 42, 242-247. doi: 10.1111/j.1472-765X.2005.01851.x
200. Moraga, J., Gomes, W., Pinedo, C., Cantoral, J. M., Hanson, J. R., Carbú, M., et al. (2019). The current status on secondary metabolites produced by plant pathogenic Colletotrichum species. Phytochem. Rev. 18, 1-25. doi: 10.1007/s11101-018-9590-0
201. Mota, T. R., Linhares, H. V., Araújo-Filho, J. H., Veras, D. M., Costa, H. P., Souza, C. M., et al. (2019). Protein extract from Cereus jamacaru (DC.) inhibits Colletotrichum gloeosporioides growth by stimulating ROS generation and promoting severe cell membrane damage. Microb. Pathog. 130, 71-80. doi: 10.1016/j.micpath.2019.02.033
202. Mótyán, J., Tóth, F., and Tozsér, J. (2013). Research applications of proteolytic enzymes in molecular biology. Biomolecules 3, 923-942. doi: 10.3390/biom3040923
203. Mukesh, D., Rajan, R., Lawrence, L., Priyadarshini, S., Chittybabu, S., and Kalaichelvan, P. (2012). Distaining and de-hairing capability of partially purified Bacillus subtilis protease from optimized fermentation medium. Asian J. Exp. Biol. Sci. 3, 613-620.
204. Mukherjee, A. K., and Rai, S. K. (2011). A statistical approach for the enhanced production of alkaline protease showing fibrinolytic activity from a newly isolated Gram-negative Bacillus sp. strain AS-S20-I. New Biotechnol. 28, 182-189. doi: 10.1016/j.nbt.2010.11.003
205. Naidu, K. S. (2011). Characterization and purification of protease enzyme. J. Appl. Pharma. Sci. 1:17.
206. Najafi, M. F., Deobagkar, D., and Deobagkar, D. (2005). Potential application of protease isolated from Pseudomonas aeruginosa PD100. Electron. J. Biotechnol. 8, 79-85. doi: 10.2225/vol8-issue2-fulltext-5
207. Nakiboglu, N., Toscali, D., and Yasa, I. (2001). Silver recovery from waste photographic films by using enzymatic method. Turk. J. Chem. 25, 349-353.
208. Nalinanon, S., Benjakul, S., Kishimura, H., and Shahidi, F. (2011). Functionalities and antioxidant properties of protein hydrolysates from the muscle of ornate threadfin bream treated with pepsin from skipjack tuna. Food Chem. 124, 1354-1362. doi: 10.1016/j.foodchem.2010.07.089
209. Narasimhan, M. K., Chandrasekaran, M., and Rajesh, M. (2015). Fibrinolytic enzyme production by newly isolated Bacillus cereus SRM-001 with enhanced in-vitro blood clot lysis potential. J. Gen. Appl. Microbiol. 61, 157-164. doi: 10.2323/jgam.61.157
210. Narhi, L., Stabinsky, Y., Levitt, M., Miller, L., Sachdev, R., Finley, S., et al. (1991). Enhanced stability of subtilisin by three point mutations. Biotechnol. Appl. Biochem. 13, 12-24.
211. Neklyudov, A., Ivankin, A., and Berdutina, A. (2000). Properties and uses of protein hydrolysates. Appl. Biochem. Microbiol. 36, 452-459. doi: 10.1007/BF02731888
212. Nicolia, A., Manzo, A., Veronesi, F., and Rosellini, D. (2014). An overview of the last 10 years of genetically engineered crop safety research. Crit. Rev. Biotechnol. 34, 77-88. doi: 10.3109/07388551.2013.823595
213. Nisha, N., and Divakaran, J. (2014). Optimization of alkaline protease production from Bacillus subtilis NS isolated from sea water. Afr. J. Biotechnol. 13, 1707-1713. doi: 10.5897/AJB2014.13652
214. Nongonierma, A. B., and FitzGerald, R. J. (2015). The scientific evidence for the role of milk protein-derived bioactive peptides in humans: a review. J. Funct. Foods 17, 640-656. doi: 10.1016/j.jff.2015.06.021
215. Oberoi, R., Beg, Q. K., Puri, S., Saxena, R., and Gupta, R. (2001). Characterization and wash performance analysis of an SDS-stable alkaline protease from a Bacillus sp. World J. Microbiol. Biotechnol. 17, 493-497. doi: 10.1023/A:1011918806201
216. Onaizi, S. A. (2018). Enzymatic removal of protein fouling from self-assembled cellulosic nanofilms: experimental and modeling studies. Eur. Biophys. J. 47, 951-960. doi: 10.1007/s00249-018-1320-4
217. Ottesen, M., and Rickert, W. (1970). The isolation and partial characterization of an acid protease produced by Mucor miehei. C. R. Trav. Lab. Carlsberg 37, 301-325.
218. Özacar, M., Mehde, A. A., Mehdi, W. A., Özacar, Z. Z., and Severgün, O. (2019). The novel multi cross-linked enzyme aggregates of protease, lipase, and catalase production from the sunflower seeds, characterization and application. Colloids Surf. B Biointerfaces 173, 58-68. doi: 10.1016/j.colsurfb.2018.09.042
219. Page, M. J., and Di Cera, E. (2008). Evolution of peptidase diversity. J. Biol. Chem. 283, 30010-30014. doi: 10.1074/jbc. M804650200
220. Palanivel, P., Ashokkumar, L., and Balagurunathan, R. (2013). Production, purification and fibrinolytic characterization of alkaline protease from extremophilic soil fungi. Int. J. Pharm. Bio. Sci. 4, 101-110.
221. Palsaniya, P., Mishra, R., Beejawat, N., Sethi, S., and Gupta, B. L. (2012). Optimization of alkaline protease production from bacteria isolated from soil. J. Microbiol. Biotechnol. Res. 2, 695-701.
222. Palumbo, J. D., Sullivan, R. F., and Kobayashi, D. Y. (2003). Molecular characterization and expression in Escherichia coli of three β-1, 3-glucanase genes from Lysobacter enzymogenes strain N4-7. J. Bacteriol. 185, 4362-4370. doi: 10.1128/JB.185.15.4362-4370.2003
223. Panda, M. K., Sahu, M. K., and Tayung, K. (2013). Isolation and characterization of a thermophilic Bacillus sp. with protease activity isolated from hot spring of Tarabalo, Odisha, India. Iran. J. Microbiol. 5:159.
224. Pastor, M. D., Lorda, G. S., and Balatti, A. (2001). Protease obtention using Bacillus subtilis 3411 and amaranth seed meal medium at different aeration rates. Braz. J. Microbiol. 32, 6-9. doi: 10.1590/S1517-83822001000100002
225. Patil, U., and Chaudhari, A. (2009). Purification and characterization of solvent-tolerant, thermostable, alkaline metalloprotease from alkalophilic Pseudomonas aeruginosa MTCC 7926. J. Chem. Technol. Biotechnol. 84, 1255-1262. doi: 10.1002/jctb.2169
226. Perkins, D.N., Pappin, D. J., Creasy, D. M., and Cottrell, J. S. (1999). Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 20, 3551-3567. doi: 10.1002/(SICI)1522-2683(19991201)20:18<3551::AID-ELPS3551>3.0.CO;2-2
227. Phoenix, D. A., Dennison, S. R., and Harris, F. (2012). Antimicrobial Peptides. Wiley-VCH Verlag GmbH & Co. KGaA.
228. Power, O., Jakeman, P., and FitzGerald, R. (2013). Antioxidative peptides: enzymatic production, in vitro and in vivo antioxidant activity and potential applications of milk-derived antioxidative peptides. Amino acids 44, 797-820. doi: 10.1007/s00726-012-1393-9
229. Prabhavathy, G., Rajasekara Pandian, M., and Senthilkumar, B. (2012). Optimization and production of extracellular alkaline protease by solid state fermentation using Bacillus subtilis. J. Acad. Ind. Res. 17, 427-430. doi: 10.1016/j.jtusci.2014.04.010
230. Prabhavathy, G., Rajasekara, M., and Senthilkumar, B. (2013). Identification of industrially important alkaline protease producing Bacillus subtilis by 16s rRNA sequence analysis and its applications. Int. J. Res. Pharma. Biomed. Sci. 4, 332-338.
231. Prakasham, R., Rao, C. S., Rao, R. S., Rajesham, S., and Sarma, P. (2005). Optimization of alkaline protease production by Bacillus sp. using Taguchi methodology. Appl. Biochem. Biotechnol. 120, 133-144. doi: 10.1385/ABAB:120:2:133
232. Prakasham, R., Rao, C. S., and Sarma, P. (2006). Green gram husk-an inexpensive substrate for alkaline protease production by Bacillus sp. in solid-state fermentation. Bioresour. Technol. 97, 1449-1454. doi: 10.1016/j.biortech.2005.07.015
233. Priya, V., Preethi, S., Karthikeyan, S., and Babu, R. (2016). Isolation and identification of protease producing bacteria from soil. Int. J. Res. Eng. Technol. 3, 1362-1365.
234. Puente, X. S., Sánchez, L. M., Overall, C. M., and López-Otín, C. (2003). Human and mouse proteases: a comparative genomic approach. Nat. Rev. Genet. 4:544. doi: 10.1038/nrg1111
235. Pursel, V. G., Pinkert, C. A., Miller, K. F., Bolt, D. J., Campbell, R. G., Palmiter, R. D., et al. (1989). Genetic engineering of livestock. Science 244, 1281-1288. doi: 10.1126/science.2499927
236. Pushpam, P. L., Rajesh, T., and Gunasekaran, P. (2011). Identification and characterization of alkaline serine protease from goat skin surface metagenome. AMB Express 1:3. doi: 10.1186/2191-0855-1-3
237. Qian, G., Xu, F., Venturi, V., Du, L., and Liu, F. (2014). Roles of a solo LuxR in the biological control agent Lysobacter enzymogenes strain OH11. Phytopathology 104, 224-231. doi: 10.1094/PHYTO-07-13-0188-R
238. Qian, G.-L., Hu, B.-S., Jiang, Y.-H., and Liu, F.-Q. (2009). Identification and characterization of Lysobacter enzymogenes as a biological control agent against some fungal pathogens. Agric. Sci. China 8, 68-75. doi: 10.1016/S1671-2927(09)60010-9
239. Radha, S., Sridevi, A., HimakiranBabu, R., Nithya, V., Prasad, N., and Narasimha, G. (2017). Medium optimization for acid protease production from Aspergillus sps under solid state fermentation and mathematical modelling of protease activity. J. Microbiol. Biotechnol. Res. 2, 6-16.
240. Ramesh, S., Rajesh, M., and Mathivanan, N. (2009). Characterization of a thermostable alkaline protease produced by marine Streptomyces fungicidicus MML1614. Bioprocess Biosyst. Eng. 32, 791-800. doi: 10.1007/s00449-009-0305-1
241. Rani, K., Rana, R., and Datt, S. (2012). Review on latest overview of proteases. Int. J. Curr. Life Sci. 2, 12-18.
242. Rao, C. S., Sathish, T., Ravichandra, P., and Prakasham, R. (2009). Characterization of thermo-and detergent stable serine protease from isolated Bacillus circulans and evaluation of eco-friendly applications. Process Biochem. 44, 262-268. doi: 10.1016/j.procbio.2008.10.022
243. Rao, M. B., Tanksale, A. M., Ghatge, M. S., and Deshpande, V. V. (1998). Molecular and biotechnological aspects of microbial proteases. Microbiol. Mol. Biol. Rev. 62, 597-635.
244. Rao, R. R., Vimudha, M., Kamini, N., Gowthaman, M., Chandrasekran, B., and Saravanan, P. (2017). Alkaline protease production from Brevibacterium luteolum (MTCC 5982) under solid-state fermentation and its application for sulfide-free unhairing of cowhides. Appl. Biochem. Biotechnol. 182, 511-528. doi: 10.1007/s12010-016-2341-z
245. Rathakrishnan, P., and Nagarajan, P. (2012). Optimizing factors affecting protease production by a Bacillus cereus using groundnut shell under solid substrate fermentation. Int. J. Sci. Invent. Todays 1, 114-129.
246. Rattenholl, A., Lilie, H., Grossmann, A., Stern, A., Schwarz, E., and Rudolph, R. (2001). The pro-sequence facilitates folding of human nerve growth factor from Escherichia coli inclusion bodies. Eur. J. Biochem. 268, 3296-3303. doi: 10.1046/j.1432-1327.2001.02232.x
247. Ravikumar, G., Gomathi, D., Kalaiselvi, M., and Uma, C. (2012). A protease from the medicinal mushroom Pleurotus sajor-caju; production, purification and partial characterization. Asian Pac. J. Trop. Biomed. 2, S411-S417. doi: 10.1016/S2221-1691(12)60198-1
248. Rawlings, N. D., Tolle, D. P., and Barrett, A. J. (2004). MEROPS: the peptidase database. Nucleic Acids Res. 32, D160-D164. doi: 10.1093/nar/gkh071
249. Ray, A. (2012). Protease enzyme-potential industrial scope. Int. J. Tech. 2, 1-4.
250. Reddy, L., Wee, Y.-J., Yun, J.-S., and Ryu, H.-W. (2008). Optimization of alkaline protease production by batch culture of Bacillus sp. RKY3 through Plackett-Burman and response surface methodological approaches. Bioresour. Technol. 99, 2242-2249. doi: 10.1016/j.biortech.2007.05.006
251. Rehman, R., Ahmed, M., Siddique, A., Hasan, F., Hameed, A., and Jamal, A. (2017). Catalytic role of thermostable metalloproteases from Bacillus subtilis KT004404 as dehairing and destaining agent. Appl. Biochem. Biotechnol. 181, 434-450. doi: 10.1007/s12010-016-2222-5
252. Reichenbach, H. (2006). The Genus Lysobacter. The Prokaryotes: Volume 6: Proteobacteria: Gamma Subclass. Singapore: Springer Science+Business Media LLC, 939-957.
253. Rifaat, H. M., El-Said, O. H., Hassanein, S. M., and Selim, M. S. (2007). Protease activity of some mesophilic streptomycetes isolated from Egyptian habitats. J. Cult. Collect. 5, 16-24.
254. Rivett, A. J. (1989). The multicatalytic proteinase of mammalian cells. Arch. Biochem. Biophys. 268, 1-8. doi: 10.1016/0003-9861(89)90558-4
255. Rock, K. L., and Goldberg, A. L. (1999). Degradation of cell proteins and the generation of MHC class I-presented peptides. Annu. Rev. Immunol. 17, 739-779. doi: 10.1146/annurev.immunol.17.1.739
256. Roja Rani, M., Lalitha Kumara, B., and Siva Prasad, D. (2012). Isolation and screening of alkaline protease producing bacteria and induction of overproducing Bacillus licheniformis mutants through UV irradiation. IOSR J. Pharmacy 1, 1-14. doi: 10.9790/3013-0110114
257. Romsomsa, N., Chim-anagae, P., and Jangchud, A. (2010). Optimization of silk degumming protease production from Bacillus subtilis C4 using Plackett-Burman design and response surface methodology. Sci. Asia 36, 118-124. doi: 10.2306/scienceasia1513-1874.2010.36.118
258. Ruigrok, V. J., Levisson, M., Eppink, M. H., Smidt, H., and Van Der Oost, J. (2011). Alternative affinity tools: more attractive than antibodies? Biochem. J. 436, 1-13. doi: 10.1042/BJ20101860
259. Saeki, K., Ozaki, K., Kobayashi, T., and Ito, S. (2007). Detergent alkaline proteases: enzymatic properties, genes, and crystal structures. J. Biosci. Bioeng. 103, 501-508. doi: 10.1263/jbb.103.501
260. Sandhya, C., Sumantha, A., Szakacs, G., and Pandey, A. (2005). Comparative evaluation of neutral protease production by Aspergillus oryzae in submerged and solid-state fermentation. Process Biochem. 40, 2689-2694. doi: 10.1016/j.procbio.2004.12.001
261. Sarmadi, B.H., and Ismail, A. (2010). Antioxidative peptides from food proteins: a review. Peptides 31, 1949-1956. doi: 10.1016/j.peptides.2010.06.020
262. Sathishkumar, R., Ananthan, G., and Arun, J. (2015). Production, purification and characterization of alkaline protease by ascidian associated Bacillus subtilis GA CAS8 using agricultural wastes. Biocatal. Agric. Biotechnol. 4, 214-220. doi: 10.1016/j.bcab.2014.12.003
263. Satyanarayana, T., Sharma, A., Mehta, D., Puri, A. K., Kumar, V., Nisha, M., et al. (2012). "Biotechnological applications of biocatalysts from the Firmicutes bacillus and Geobacillus species," in Microorganisms in Sustainable Agriculture and Biotechnology, eds T. Satyanarayana, B. Johri, and Anil Prakash (Dordrecht: Springer), 343-379. doi: 10.1007/978-94-007-2214-9_17
264. Schomburg, D., and Salzmann, M. (1991). Enzyme Handbook. Berlin; Heidelberg: Springer-Verlag, 1-1175. doi: 10.1007/978-3-642-76729-6_1
265. Sellami-Kamoun, A., Haddar, A., Ali, N. E.-H., Ghorbel-Frikha, B., Kanoun, S., and Nasri, M. (2008). Stability of thermostable alkaline protease from Bacillus licheniformis RP1 in commercial solid laundry detergent formulations. Microbiol. Res. 163, 299-306. doi: 10.1016/j.micres.2006.06.001
266. Sen, S., Dasu, V., Dutta, K., and Mandal, B. (2011). Characterization of a novel surfactant and organic solvent stable high-alkaline protease from new Bacillus pseudofirmus SVB1. Res. J. Microbiol. 6, 769-783. doi: 10.3923/jm.2011.769.783
267. Shahid, M., Mohammad, F., Chen, G., Tang, R.-C., and Xing, T. (2016). Enzymatic processing of natural fibres: white biotechnology for sustainable development. Green Chem. 18, 2256-2281. doi: 10.1039/C6GC00201C
268. Shankar, S., More, S., and Laxman, R. S. (2010). Recovery of silver from waste X-ray film by alkaline protease from Conidiobolus coronatus. Kathmandu Univ. J. Sci. Eng. Technol. 6, 60-69. doi: 10.3126/kuset.v6i1.3311
269. Shankar, S., Rao, M., and Laxman, R. S. (2011). Purification and characterization of an alkaline protease by a new strain of Beauveria sp. Process Biochem. 46, 579-585. doi: 10.1016/j.procbio.2010.10.013
270. Shanlin, F., Stocker, R., and Davies, M. J. (1997). Biochemistry and pathology of radical-mediated protein oxidation. Biochem. J. 324, 1-18. doi: 10.1042/bj3240001
271. Shinmyo, A., Mitsushima, K., and Terui, G. (1972). Kinetic studies on enzyme production by microbes. IX. Some properties of auto-induction of acid protease in Aspergillus niger. J. Ferment. Technol. 50, 647-654.
272. Siar, E.-H., Morellon-Sterling, R., Zidoune, M. N., and Fernandez-Lafuente, R. (2019). Amination of ficin extract to improve its immobilization on glyoxyl-agarose: improved stability and activity versus casein. Int. J. Biol. Macromol. 133, 412-419. doi: 10.1016/j.ijbiomac.2019.04.123
273. Siddiqui, K.S., and Cavicchioli, R. (2006). Cold-adapted enzymes. Annu. Rev. Biochem. 75, 403-433. doi: 10.1146/annurev.biochem.75.103004.142723
274. Sielecki, A., Fujinaga, M., Read, R., and James, M. (1991). Refined structure of porcine pepsinogen at 1 · 8 Å resolution. J. Mol. Biol. 219, 671-692. doi: 10.1016/0022-2836(91)90664-R
275. Silen, J., Frank, D., Fujishige, A., Bone, R., and Agard, D. A. (1989). Analysis of prepro-alpha-lytic protease expression in Escherichia coli reveals that the pro region is required for activity. J. Bacteriol. 171, 1320-1325. doi: 10.1128/jb.171.3.1320-1325.1989
276. Silen, J., McGrath, C., Smith, K., and Agard, D. (1988). Molecular analysis of the gene encoding a-lytic protease: evidence for a preproenzyme. Gene 69, 237-244. doi: 10.1016/0378-1119(88)90434-9
277. Simkhada, J.R., Mander, P., Cho, S. S., and Yoo, J. C. (2010b). A novel fibrinolytic protease from Streptomyces sp. CS684. Process Biochem. 45, 88-93. doi: 10.1016/j.procbio.2009.08.010
278. Simkhada, J. R., Cho, S. S., Park, S. J., Mander, P., Choi, Y. H., Lee, H. J., et al. (2010a). An oxidant-and organic solvent-resistant alkaline metalloprotease from Streptomyces olivochromogenes. Appl. Biochem. Biotechnol. 162, 1457-1470. doi: 10.1007/s12010-010-8925-0
279. Singh, J., Vohra, R., and Sahoo, D. K. (1999). Alkaline protease from a new obligate alkalophilic isolate of Bacillus sphaericus. Biotechnol. Lett. 21, 921-924. doi: 10.1023/A:1005502824637
280. Singh, P., Rani, A., and Chaudhary, N. (2015). Isolation and characterization of protease producing Bacillus sp from soil. Int. J. Pharma Sci. Res. 6, 633-639.
281. Singh, R., Mittal, A., Kumar, M., and Mehta, P. K. (2016). Microbial protease in commercial applications. J. Pharm. Chem. Biol. Sci. 4, 365-374.
282. Singhal, P., Nigam, V., and Vidyarthi, A. (2012). Studies on production, characterization and applications of microbial alkaline proteases. Int. J. Adv. Biotechnol. Res. 3, 653-669.
283. Sloma, A., Rudolph, C., Rufo, G., Sullivan, B., Theriault, K., Ally, D., et al. (1990). Gene encoding a novel extracellular metalloprotease in Bacillus subtilis. J. Bacteriol. 172, 1024-1029. doi: 10.1128/jb.172.2.1024-1029.1990
284. Sodek, J., and Hofmann, T. (1970). Large-scale preparation and some properties of penicillopepsin, the acid proteinase of Penicillium janthinellum. Can. J. Biochem. 48, 425-431. doi: 10.1139/o70-069
285. Somkuti, G., and Babel, F. (1967). Conditions influencing the synthesis of acid protease by Mucor pusillus Lindt. Appl. Environ. Microbiol. 15, 1309-1312.
286. Soroor, M. A., Hendawy, H., Ghazy, A., Semary, N., Khalil, K., and Aziz, A. (2009). Characterization of an alkaline metalloprotease secreted by the entomopathogenic bacterium Photorhabdus sp. strain EK1. Res. J. Agric. Biol. Sci. 5, 349-360.
287. Sørvig, E., Mathiesen, G., Naterstad, K., Eijsink, V. G., and Axelsson, L. (2005). High-level, inducible gene expression in Lactobacillus sakei and Lactobacillus plantarum using versatile expression vectors. Microbiology 151, 2439-2449. doi: 10.1099/mic.0.28084-0
288. Souza, P. M., Bittencourt, M. L. d. A., Caprara, C. C., Freitas, M., de, Almeida, R. P. C., de Silveira, D., et al. (2015). A biotechnology perspective of fungal proteases. Braz. J. Microbiol. 46, 337-346. doi: 10.1590/S1517-838246220140359
289. Stabile, M. R., Lai, W. G., DeSantis, G., Gold, M., Jones, J. B., Mitchinson, C., et al. (1996). Probing the specificity of the S1 binding site of M222 mutants of subtilisin B. lentus with boronic acid inhibitors. Bioorg. Med. Chem. Lett. 6, 2501-2506. doi: 10.1016/0960-894X(96)00466-0
290. Stack, C. M., Lowther, J., Cunningham, E., Donnelly, S., Gardiner, D. L., Trenholme, K. R., et al. (2007). Characterization of the Plasmodium falciparum M17 leucyl aminopeptidase A protease involved in amino acid regulation with potential for antimalarial drug development. J. Biol. Chem. 282, 2069-2080. doi: 10.1074/jbc. M609251200
291. Steele, D. B., Fiske, M. J., Steele, B. P., and Kelley, V. C. (1992). Production of a low-molecular-weight, alkaline-active, thermostable protease by a novel, spiral-shaped bacterium, Kurthia spiroforme sp. nov. Enzyme Microb. Technol. 14, 358-360. doi: 10.1016/0141-0229(92)90003-7
292. Sumantha, A., Larroche, C., and Pandey, A. (2006). Microbiology and industrial biotechnology of food-grade proteases: a perspective. Food Technol. Biotechnol. 44:211.
293. Suntornsuk, W., and Suntornsuk, L. (2003). Feather degradation by Bacillus sp. FK 46 in submerged cultivation. Bioresour. Technol. 86, 239-243. doi: 10.1016/S0960-8524(02)00177-3
294. Suwannaphan, S., Fufeungsombut, E., Promboon, A., and Chim-Anage, P. (2017). A serine protease from newly isolated Bacillus sp. for efficient silk degumming, sericin degrading and colour bleaching activities. Int. Biodeter. Biodegrad. 117, 141-149. doi: 10.1016/j.ibiod.2016.12.009
295. Suzuki, K. (1987). Calcium activated neutral protease: domain structure and activity regulation. Trends Biochem. Sci. 12, 103-105. doi: 10.1016/0968-0004(87)90048-X
296. Takami, H., Nakamura, S., Aono, R., and Horikoshi, K. (1992). Degradation of human hair by a thermostable alkaline protease from alkaliphilic Bacillus sp. no. AH-101. Biosci. Biotechnol. Biochem. 56, 1667-1669. doi: 10.1271/bbb.56.1667
297. Tammawong, S. (2005). Cloning and Expression of Neutral Protease (npr) Gene from Bacillus cereus MFKU33 in Escherichia coli. Bangkok: Kasetsart University.
298. Tamreihao, K., Devi, L. J., Khunjamayum, R., Mukherjee, S., Ashem, R. S., and Ningthoujam, D. S. (2017). Biofertilizing potential of feather hydrolysate produced by indigenous keratinolytic Amycolatopsis sp. MBRL 40 for rice cultivation under field conditions. Biocatal. Agric. Biotechnol. 10, 317-320. doi: 10.1016/j.bcab.2017.04.010
299. Tanaka, K., Yoshimura, T., Kumatori, A., Ichihara, A., Ikai, A., Nishigai, M., et al. (1988). Proteasomes (multi-protease complexes) as 20 S ring-shaped particles in a variety of eukaryotic cells. J. Biol. Chem. 263, 16209-16217.
300. Tavano, O. L. (2013). Protein hydrolysis using proteases: an important tool for food biotechnology. J. Mol. Catal. B Enzym. 90, 1-11. doi: 10.1016/j.molcatb.2013.01.011
301. Tavano, O. L., A. Berenguer-Murcia Secundo, F., and Fernandez-Lafuente, R. (2018). Biotechnological applications of proteases in food technology. Compr. Rev. Food Sci. Food Saf. 17, 412-436. doi: 10.1111/1541-4337.12326
302. Taylor, A., Volz, K. W., Lipscomb, W. N., and Takemoto, L. (1984). Leucine aminopeptidase from bovine lens and hog kidney. Comparison using immunological techniques, electron microscopy, and X-ray diffraction. J. Biol. Chem. 259, 14757-14761.
303. Thiansilakul, Y., Benjakul, S., and Shahidi, F. (2007). Compositions, functional properties and antioxidative activity of protein hydrolysates prepared from round scad (Decapterus maruadsi). Food Chem. 103, 1385-1394. doi: 10.1016/j.foodchem.2006.10.055
304. Thirumurugan, D., and Vijayakumar, R. (2015). Characterization and structure elucidation of antibacterial compound of Streptomyces sp. ECR77 isolated from East Coast of India. Curr. Microbiol. 70, 745-755. doi: 10.1007/s00284-015-0780-3
305. Tomkinson, B., Wernstedt, C., Hellman, U., and Zetterqvist, O. (1987). Active site of tripeptidyl peptidase II from human erythrocytes is of the subtilisin type. Proc. Natl. Acad. Sci. U.S.A. 84, 7508-7512. doi: 10.1073/pnas.84.21.7508
306. Tomoda, K., and Shimazono, H. (1964). Acid protease produced by trametes sanguinea, a wood-destroying fungus: part purification I, and crystallization of the enzyme part I physical I, and enzymological properties of the enzyme. Agric. Biol. Chem. 28, 770-778. doi: 10.1080/00021369.1964.10858303
307. Udenigwe, C. C. (2014). Bioinformatics approaches, prospects and challenges of food bioactive peptide research. Trends Food Sci. Technol. 36, 137-143. doi: 10.1016/j.tifs.2014.02.004
308. Vadlamani, S., and Parcha, S. R. (2011). Studies on industrially important alkaline protease production from locally isolated superior microbial strain from soil microorganisms. Int. J. Biotechnol. Appl. 3, 102-105. doi: 10.9735/0975-2943.3.3.102-105
309. Varela, H., Ferrari, M. D., Belobrajdic, L., Vazquez, A., and Loperena, M. L. (1997). Skin unhairing proteases of Bacillus subtilis: production andpartial characterization. Biotechnol. Lett. 19, 755-758. doi: 10.1023/A:1018384025181
310. Vasantha, N., Thompson, L., Rhodes, C., Banner, C., Nagle, J., and Filpula, D. (1984). Genes for alkaline protease and neutral protease from Bacillus amyloliquefaciens contain a large open reading frame between the regions coding for signal sequence and mature protein. J. Bacteriol. 159, 811-819.
311. Verma, A., Singh, H., Anwar, M. S., Kumar, S., Ansari, M. W., and Agrawal, S. (2016). Production of thermostable organic solvent tolerant keratinolytic protease from Thermoactinomyces sp. RM4: IAA production and plant growth promotion. Front. Microbiol. 7:1189. doi: 10.3389/fmicb.2016.01189
312. Verma, T., and Agarwa, S. (2016). Isolation and screening of haloalkaline protease producing bacteria from tannery solid waste. Int. J. Res. Eng. Technol. 5, 237-244. doi: 10.15623/ijret.2016.0501048
313. Vijayaraghavan, P., Jebamalar, T. R. J., and Vincent, S. G. P. (2012). Biosynthesis optimization and purification of a solvent stable alkaline serine protease from Halobacterium sp. Ann. Microbiol. 62, 403-410. doi: 10.1007/s13213-011-0276-8
314. Vijayaraghavan, P., Lazarus, S., and Vincent, S. G. P. (2014). De-hairing protease production by an isolated Bacillus cereus strain AT under solid-state fermentation using cow dung: biosynthesis and properties. Saudi J. Biol. Sci. 21, 27-34. doi: 10.1016/j.sjbs.2013.04.010
315. Vijayaraghavan, P., and Vincent, S. P. (2015). A low cost fermentation medium for potential fibrinolytic enzyme production by a newly isolated marine bacterium, Shewanella sp. IND20. Biotechnol. Rep. 7, 135-142. doi: 10.1016/j.btre.2015.06.005
316. Vojcic, L., Pitzler, C., Koerfer, G., Jakob, F., Martinez, R., Maurer, K.-H., et al. (2015). Advances in protease engineering for laundry detergents. New Biotechnol. 32, 629-634. doi: 10.1016/j.nbt.2014.12.010
317. Wang, W., Vinocur, B., and Altman, A. (2003). Plant responses to drought, salinity and extreme temperatures: towards genetic engineering for stress tolerance. Planta 218, 1-14. doi: 10.1007/s00425-003-1105-5
318. Wang, Y., Qian, G., Li, Y., Wang, Y., Wang, Y., Wright, S., et al. (2013). Biosynthetic mechanism for sunscreens of the biocontrol agent Lysobacter enzymogenes. PLoS ONE 8:e66633. doi: 10.1371/journal.pone.0066633
319. Watabe, S., and Kimura, T. (1985). ATP-dependent protease in bovine adrenal cortex. Tissue specificity, subcellular localization, and partial characterization. J. Biol. Chem. 260, 5511-5517.
320. Weaver, L., Kester, W., and Matthews, B. (1977). A crystallographic study of the complex of phosphoramidon with thermolysin. A model for the presumed catalytic transition state and for the binding of extended substrates. J. Mol. Biol. 114, 119-132. doi: 10.1016/0022-2836(77)90286-8
321. Weston, J. (2005). Mode of action of bi-and trinuclear zinc hydrolases and their synthetic analogues. Chem. Rev. 105, 2151-2174. doi: 10.1021/cr020057z
322. Woessner, J. F., Woessner, J. F., and Nagase, H. (2000). Matrix Metalloproteinases and TIMPs. Oxford: Oxford University Press.
323. Wolff, A., Showell, M., Venegas, M., Barnett, B., and Wertz, W. (1996). "Laundry performance of subtilisin proteases," in Subtilisin Enzymes. Advances in Experimental Medicine and Biology, Vol. 379, eds R. Bott, and C. Betzel (Boston, MA: Springer), 113-120. doi: 10.1007/978-1-4613-0319-0_12
324. Wu, H.-C., Chen, H.-M., and Shiau, C.-Y. (2003). Free amino acids and peptides as related to antioxidant properties in protein hydrolysates of mackerel (Scomber austriasicus). Food Res. Int. 36, 949-957. doi: 10.1016/S0963-9969(03)00104-2
325. Xing, X., Jia, J.-Q., Zhang, J.-F., Zhou, Z.-W., Li, J., Wang, N., et al. (2019). CALB immobilized onto magnetic nanoparticles for efficient kinetic resolution of racemic secondary alcohols: long-term stability and reusability. Molecules 24:490. doi: 10.3390/molecules24030490
326. Xu, M.-Q., Wang, S.-S., Li, L.-N., Gao, J., and Zhang, Y.-W. (2018). Combined cross-linked enzyme aggregates as biocatalysts. Catalysts 8:460. doi: 10.3390/catal8100460
327. Xue, B., Dunker, A. K., and Uversky, V. N. (2012). Orderly order in protein intrinsic disorder distribution: disorder in 3500 proteomes from viruses and the three domains of life. J. Biomol. Struct. Dyn. 30, 137-149. doi: 10.1080/07391102.2012.675145
328. Yadav, S. K., Bisht, D., Shikha, S., and Darmwal, N. S. (2011). Oxidant and solvent stable alkaline protease from Aspergillus flavus and its characterization. Afr. J. Biotechnol. 10, 8630-8640. doi: 10.5897/AJB10.1611
329. Yadav, S. K., Bisht, D., Tiwari, S., and Darmwal, N. S. (2015). Purification, biochemical characterization and performance evaluation of an alkaline serine protease from Aspergillus flavus MTCC 9952 mutant. Biocatal. Agric. Biotechnol. 4, 667-677. doi: 10.1016/j.bcab.2015.08.007
330. Yamagata, Y., Abe, R., Fujita, Y., and Ichishima, E. (1995). Molecular cloning and nucleotide sequence of the 90k serine protease gene, hspK, from Bacillus subtilis (natto) No. 16. Curr. Microbiol. 31, 340-344. doi: 10.1007/BF00294696
331. Yang, J.-K., Shih, L., Tzeng, Y.-M., and Wang, S.-L. (2000). Production and purification of protease from a Bacillus subtilis that can deproteinize crustacean wastes. Enzyme Microb. Technol. 26, 406-413. doi: 10.1016/S0141-0229(99)00164-7
332. Yang, S., Du, G., Chen, J., and Kang, Z. (2017). Characterization and application of endogenous phase-dependent promoters in Bacillus subtilis. Appl. Microbiol. Biotechnol. 101, 4151-4161. doi: 10.1007/s00253-017-8142-7
333. Yang, Y., Jiang, L., Zhu, L., Wu, Y., and Yang, S. (2000). Thermal stable and oxidation-resistant variant of subtilisin E. J. Biotechnol. 81, 113-118. doi: 10.1016/S0168-1656(00)00272-8
334. Yongquan, L. (2001). Sheep-pelt bating with acid protease. J. Am. Leather Chem. Assoc. 96, 398-400.
335. Younes, I., and Rinaudo, M. (2015). Chitin and chitosan preparation from marine sources. Structure, properties and applications. Marine Drugs 13, 1133-1174. doi: 10.3390/md13031133
336. Zhang, G., Wang, H., Zhang, X., and Ng, T. (2010). Helvellisin, a novel alkaline protease from the wild ascomycete mushroom Helvella lacunosa. J. Biosci. Bioeng. 109, 20-24. doi: 10.1016/j.jbiosc.2009.06.022
337. Zhang, S., Xu, Z., Sun, H., Sun, L., Shaban, M., Yang, X., et al. (2019). Genome-wide identification of papain-like cysteine proteases in Gossypium hirsutum and functional characterization in response to Verticillium dahliae. Front. Plant Sci. 10:134. doi: 10.3389/fpls.2019.00134
338. Zheng, S., Wang, H., and Zhang, G. (2011). A novel alkaline protease from wild edible mushroom Termitomyces albuminosus. Acta Biochim. Pol. 58, 269-273. doi: 10.18388/abp.2011_2277
339. Zhou, C., Liu, H., Yuan, F., Chai, H., Wang, H., Liu, F., et al. (2019). Development and application of a CRISPR/Cas9 system for Bacillus licheniformis genome editing. Int. J. Biol. Macromol. 122, 329-337. doi: 10.1016/j.ijbiomac.2018.10.170