Marine enzymes and food industry: Insight on existing and potential interactions

Frontiers in Marine Science

Volumn 1, Issue OCT, 2014, Pages

  Fernandes, Pedro ^a,b  

^a INSTITUTO SUPERIOR TÉCNICO   (Portugal)

^b UNIVERSIDADE LUSÓFONA DE HUMANIDADES E TECNOLOGIAS   (Portugal)

Author keywords

Biocatalysis; Food industry; Food processing; Marine enzymes; Marine microorganisms

Indexed keywords

EID: 85008881145     PISSN: None     EISSN: 22967745     Source Type: Journal    
DOI: 10.3389/fmars.2014.00046     Document Type: Review

References (153)

1. Afinah, S., Yazid, A. M., Anis Shobirin, M. H., and Shuhaimi, M. (2010). Phytase: application in food industry. Int. Food Res. J. 17, 13-21.
2. Aguilar, C. N., and Gutierrez-Sanchez, G. (2001). Review: sources, properties, applications and potential uses of Tannin Acyl Hydrolase. Food Sci. Technol. Int. 7, 373-382. doi: 10.1106/69M3-B30K-CF7Q-RJ5G
3. Aiyer, P. V. (2005). Amylases and their applications. Afr. J. Biotechnol. 4, 1525-1529.
4. Aravindan, R., Anbumathi, P., and Viruthagiri, T. (2007). Lipase applications in food industry. Indian J. Biotechnol. 6, 141-158.
5. Arnosti, C., Bell, C., Moorhead, D. L., Sinsabaugh, R. L., Steen, A. D., Stromberger, M., et al. (2014). Extracellular enzymes in terrestrial, freshwater, and marine environments: perspectives on system variability and common research needs. Biogeochemistry 117, 5-21. doi: 10.1007/s10533-013-9906-5
6. Atichokudomchai, N., Jane, J.-L., and Hazlewood, G. (2006). Reaction pattern of a novel thermostable a-amylase. Carbohydr. Polymers 64, 582-588. doi: 10.1016/j.carbpol.2005.11.014
7. Basso, A., Spizzo, P., Ferrario, V., Knapic, L., Savko, N., Braiuca, P., et al. (2010). Endo-and exo-inulinases: enzyme-substrate interaction and rational immobilization. Biotechnol. Prog. 26, 397-405. doi: 10.1002/btpr.33
8. Bauvois, C., Jacquamet, L., Huston, A. L., Borel, F., Feller, G., and Ferrer, J. L. (2008). Crystal Structure of the Cold-active Aminopeptidase from Colwellia psychrerythraea, a Close Structural Homologue of the Human Bifunctional Leukotriene A4 Hydrolase. J. Biol. Chem. 283, 23315-23325. doi: 10.1074/jbc.M802158200
9. Beena, P. S., Soorej, M. B., Elyas, K. K., Sarita, G. B., and Chandrasekaran, M. (2010). Acidophilic Tannase from Marine Aspergillus awamori BTMFW032. J. Microbiol. Biotechnol. 20, 1403-1414. doi: 10.4014/jmb.1004.04038
10. Beena, P. S., Soorej, M. B., Sarita, G. B., Bahkali, A. H., and Chandrasekaran, M. (2011). Propyl gallate synthesis using acidophilic tannase and simultaneous production of tannase and gallic acid by marine Aspergillus awamori BTMFW032. Appl. Biochem. Biotechnol. 164, 612-628. doi: 10.1007/s12010-011-9162-x
11. Beg, Q. K., Kapoor, M., Mahajan, L., and Hoondal, G. S. (2001). Microbial xylanases and their industrial applications: a review. Appl. Microbiol. Biotechnol. 56, 326-338. doi: 10.1007/s002530100704
12. Bekhit, A. A., Hopkins, D. L., Geesink, G., Bekhit, A. A., and Franks, P. (2013). Exogenous proteases for meat tenderization. Crit. Rev. Food Sci. Nutr. 54, 1012-1031. doi: 10.1080/10408398.2011.623247
13. Belancic, A., Gunata, Z., Vallier, M. J., and Agosin, E. (2003). ß-glucosidase from the grape native yeast Debaryomyces vanrijiae: purification, characterization, and its effect on monoterpene content of a muscat grape juice. J. Agric. Food Chem. 51, 1453-1459. doi: 10.1021/jf025777l
14. Benediktsson, B., and Bjarnason, J. B. (2001). Protein hydrolysates produced with the use of marine proteases. WO Patent Application 2001028353 A2.
15. Bertoft, E. (2004). "Analysing starch structure, " in Starch in Food-Structure, Function and Applications, ed A.-C. Eliasson (Cambridge: Woodhead Publishing Limited), 57-96.
16. Bhatia, Y., Mishra, S., and Bisaria, V. S. (2002). Microbial beta-glucosidases: cloning, properties, and applications. Crit. Rev. Biotechnol. 22, 375-407. doi: 10.1080/07388550290789568
17. Bindiya, P., and Ramana, T. (2012). Optimization of lipase production from an indigenously isolated marine Aspergillus sydowii of Bay of Bengal. J. Biochem. Technol. 3, S203-S211.
18. Blanchard, P. H., and Katz, F. R. (2006). "Starch hydrolysates, " in Food Polysaccharides and Their Applications, eds A. M. Stephen, G. O. Phillips, and P. A. Williams (Boca Raton, FL: CRC Press), 119-145.
19. Bohlin, C., Praestgaard, E., Baumann, M. J., Borch, K., Praestgaard, J., Monrad, R. N., et al. (2013). A comparative study of hydrolysis and transglycosylation activities of fungal ß-glucosidases. Appl. Microbiol. Biotechnol. 97, 159-169. doi: 10.1007/s00253-012-3875-9
20. Borchert, M., Gjermansen, M., Clark, S., Henrissat, B., Silow, M. B., and Hallin, P. F. (2011). Pullulanase variants and uses thereof. WIPO Patent Application WO/2011/087836 A2.
21. Chakraborty, S., Raut, G., Khopade, A., Mahadik, K., and Kokare, C. (2012). Study on calcium ion independent a-amylase from haloalkaliphilic marine Streptomyces strain A3. Indian J. Biotechnol. 11, 427-437.
22. Chen, H., Yan, X., Zhu, P., and Lin, J. (2006). Antioxidant activity and hepatoprotective potential of agaro-oligosaccharides in vitro and in vivo. Nutrition J. 5, 31. doi: 10.1186/1475-2891-5-31
23. Chen, X. L., Xie, B. B., Lu, J. T., He, H. L., and Zhang, Y. Z. (2007a). A novel type of subtilase from the psychrotolerant bacterium Pseudoalteromonas sp. SM9913: catalytic and structural properties of deseasin MCP-01. Microbiology 153, 2116-2125. doi: 10.1099/mic.0.2007/006056-0
24. Chen, X. L., Zhang, Y. Z., Gao, P. J., and Luan, X. W. (2003). Two different proteases produced by a deep-sea psychrotrophic strain Pseudoaltermonas sp. SM9913. Mar. Biol. 143, 989-993. doi: 10.1007/s00227-003-1128-2
25. Chen, X. L., Zhang, Y. Z., Lu, J. T., Xie, B. B., Sun, C. Y., and Guo, B. (2007b). Autolysis of a novel multidomain subtilase-cold-adapted deseasin MCP-01 is pH-dependent and the surface loops in its catalytic domain, the linker, and the P_proprotein domain are susceptible to proteolytic attack. Biochem. Biophys. Res. Commun. 358, 704-709. doi: 10.1016/j.bbrc.2007.04.193
26. Chi, W. J., Chang, Y. K., and Hong, S. K. (2012). Agar degradation by microorganisms and agar-degrading enzymes. Appl. Microbiol. Biotechnol. 94, 917-930. doi: 10.1007/s00253-012-4023-2
27. Chu, X., He, H., Guo, C., and Sun, B. (2008). Identification of two novel esterases from a marine metagenomic library derived from South China Sea. Appl. Microbiol. Biotechnol. 80, 615-625. doi: 10.1007/s00253-008-1566-3
28. Claverie-MartÌn, F., and Vega-Hernàndez, M. (2007). "Aspartic proteases used in cheese making, " in Industrial Enzymes, eds J. Polaina and A. MacCabe (New York, NY: Springer), 207-219.
29. Cui, F., Dong, S., Shi, X., Zhao, X., and Zhang, X.-H. (2014). Overexpression and characterization of a novel thermostable ß-Agarase YM01-3, from marine bacterium Catenovulum agarivorans YM01T. Mar. Drugs 12, 2731-2747. doi: 10.3390/md12052731
30. Dar, Y. L. (2014). "Starches as food texturizing systems, " in Functionalizing Carbohydrates for Food Applications, ed M. E. Embuscado (Lancaster, PA: DEStech Publications, Inc.), 41-79.
31. Delattre, C., Fenoradosoa, T. A., and Michaud, P. (2011). Galactans: an overview of their most important sourcing and applications as natural polysaccharides. Braz. Arch. Biol. Technol. 54, 1075-1092. doi: 10.1590/S1516-89132011000600002
32. Dionisi, H. M., Lozada, M., and Olivera, N. L. (2012). Bioprospection of marine microorganisms: biotechnological applications and methods. Rev. Argentina Microbiol. 44, 49-60. doi: 10.1590/S0325-75412012000100010
33. El-Gendy, M. M. A. (2012). Production of glucoamylase by marine endophytic Aspergillus sp. JAN-25 under optimized solid-state fermentation conditions on agro residues. Aust. J. Basic Appl. Sci. 6, 41-54.
34. Enoki, T., Okuda, S., Kudo, Y., Takashima, F., Sagawa, H., and Kato, I. (2010). Oligosaccharides from agar inhibit pro-inflammatory mediator release by inducing heme oxygenase 1. Biosci. Biotechnol. Biochem. 74, 766-770. doi: 10.1271/bbb.90803
35. Farnet, A. M., Criquet, S., Pocachard, E., Gil, G., and Ferre, E. (2002). Purification of a new isoform of laccase from a Marasmius quercophilus strain isolated from a cork oak litter (Quercus suber L). Mycologia 94, 735-740. doi: 10.2307/3761687
36. Fernandes, P. (2010a). Enzymes in food processing: a condensed overview on strategies for better biocatalysts. Enzyme Res. 2010, 862537. doi: 10.4061/2010/862537
37. Fernandes, P. (2010b). "Enzymes in sugar industries, " in Enzymes in Food Processing: Fundamentals and Potential Applications, eds P. Panesar, S. S. Marwaha and H. K. Chopra (New Delhi:.K. International Publishing House), 165-197.
38. Ferreira-Dias, S., Sandoval, G., Plou, F., and Valero, F. (2013). The potential use of lipases in the production of fatty acid derivatives for the food and nutraceutical industries. Elect. J. Biotechnol. 16, 1-38. doi: 10.2225/vol16-issue3-fulltext-5
39. Flament, D., Barbeyron, T., Jam, M., Potin, P., Czjzek, M., Kloareg, B., et al. (2007). Alpha-agarases define a new family of Glycoside Hydrolases, distinct from beta-agarase families. Appl. Environ. Microbiol. 73, 4691-4694. doi: 10.1128/AEM.00496-07
40. Freitas, A. C., Rodrigues, D., Rocha-Santos, T. A., Gomes, A. M., and Duarte, A. C. (2012). Marine biotechnology advances towards applications in new functional foods. Biotechnol. Adv. 30, 1506-1515. doi: 10.1016/j.biotechadv.2012.03.006
41. Fu, X. T., and Kim, S. M. (2010). Agarase: review of major sources, categories, purification method, enzyme characteristics and applications. Mar. Drugs 26, 200-218. doi: 10.3390/md8010200
42. Fulzele, R., DeSa, E., Yadav, A., Shouche, Y., and Bhadekar, R. (2011). Characterization of novel extracellular protease produced by marine bacterial isolate from the Indian Ocean. Braz. J. Microbiol. 42, 1364-1373. doi: 10.1590/S1517-83822011000400018
43. Gantelet, H., and Duchiron, F. (1998). Purification and properties of a thermoactive and thermostable pullulanase from Thermococcus hydrothermalis, a hyperthermophilic archaeon isolated from a deep-sea hydrothermal vent. Appl. Microbiol. Biotechnol. 49, 770-777. doi: 10.1007/s002530051245
44. Gao, L., Chi, Z., Sheng, J., Wang, L., Li, J., and Gong, F. (2007). Inulinase-producing marine yeasts: evaluation of their diversity and inulin hydrolysis by their crude enzymes. Microb. Ecol. 54, 722-729. doi: 10.1007/s00248-007-9231-4
45. Gelse, K., Pöschl, E., and Aigner, T. (2003). Collagens-Structure, function, and biosynthesis. Adv. Drug Deliv. Rev. 28, 1531-1546. doi: 10.1016/j.addr.2003.08.002
46. Goyal, K., Selvakumar, P., and Hayashi, K. (2001). Characterization of a thermostable ß-glucosidase (BglB) from Thermotoga maritima showing transglycosylation activity. J. Mol. Catal. B Enzymatic 15, 45-53. doi: 10.1016/S1381-1177(01)00003-0
47. Gudmundsdottir, A. B. J. (2007). "Applications of cold adapted proteases in the food industry, " in Novel Enzyme Technology for Food Applications, ed B. Rastall (Cambridge: Woodhead Publishing Limited), 205-214.
48. Günata, Z. (2003). "Flavor enhancement in fruit juices and derived beverages by exogenous glycosidases and consequences of the use of enzyme preparations, " in The Handbook of Food Enzymology, eds J. R. Whitaker, A. G. J. Voragen, and D. W. S. Wong (New York, NY: Marcel Dekker, Inc.), 303-330.
49. Guo, B., Chen, X. L., Sun, C. Y., Zhou, B. C., and Zhang, Y. Z. (2009). Gene cloning, expression and characterization of a new cold-active and salt-tolerant endo-beta-1, 4-xylanase from marine Glaciecola mesophila KMM 241. Appl. Microbiol. Biotechnol. 84, 1107-1115. doi: 10.1007/s00253-009-2056-y
50. Guo, B., Li, P. Y., Yue, Y. S., Zhao, H. L., Dong, S., Song, X. Y., et al. (2013). Gene cloning, expression and characterization of a novel xylanase from the marine bacterium, Glaciecola mesophila KMM241. Mar. Drugs 11, 1173-1187. doi: 10.3390/md11041173
51. Guo, M. (2009). Functional Foods: Principles and Technology. Cambridge: Woodhead Publishing. doi: 10.1533/9781845696078
52. Gupta, R. S., and Bhandari, V. (2011). Phylogeny and molecular signatures for the phylum Thermotogae and its subgroups. Antonie van Leeuwenhoek 100, 1-34. doi: 10.1007/s10482-011-9576-z
53. Gurumurthy, D. M., and Neelagund, S. E. (2012). Molecular characterization of industrially viable extreme thermostable novel a-amylase of Geobacillus sp. Iso5 Isolated from Geothermal Spring. J. Pure Appl. Microbiol. 6, 1759-1773. doi: 10.1007/s10989-012-9303-2
54. Han, W. J., Gu, J. Y., Liu, H. H., Li, F. C., Wu, Z. H., and Li, Y. Z. (2013). An extra peptide within the catalytic module of a ß-agarase affects the agarose degradation pattern. J. Biol. Chem. 288, 9519-9531. doi: 10.1074/jbc.M112.412247
55. Harris, A. D., and Ramalingam, C. (2010). Xylanases and its application in food industry: a review. J. Exp. Sci. 1, 1-11.
56. Hassairi, I., Amar, R. B., Nonus, M., and Gupta, B. B. (2001). Production and separation of a-agarase from Altermonas agarlyticus strain GJ1B. Bioresource Technol. 79, 47-51. doi: 10.1016/S0960-8524(01)00037-2
57. Hehemann, J. H., Correc, G., Thomas, F., Bernard, T., Barbeyron, T., Jam, M., et al. (2012). Biochemical and structural characterization of the complex agarolytic enzyme system from the marine bacterium Zobellia galactanivorans. J. Biol. Chem. 287, 30571-30584. doi: 10.1074/jbc.M112.377184
58. Helland, R., Larsen, R. L., and ásgeirsson, B. (2009). The 1.4 Å crystal structure of the large and cold-active Vibrio sp. alkaline phosphatase. Biochim. Biophys. Acta 1794, 297-308. doi: 10.1016/j.bbapap.2008.09.020
59. Henrissat, B. (1991). A classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J. 280, 309-316.
60. Hii, S. L., Tan, J. S., Ling, T. C., and Ariff, A. B. (2012). Pullulanase: role in starch hydrolysis and potential industrial applications. Enzyme Res. 2012, 921362. doi: 10.1155/2012/921362
61. Hu, Z., Lin, B.-K., Xu, Y., Zhong, M. Q., and Liu, G.-M. (2009). Production and purification of agarase from a marine agarolytic bacterium Agarivorans sp. HZ105. J. Appl. Microbiol. 106, 181-190. doi: 10.1111/j.1365-2672.2008.03990.x
62. Huang, X., Zhao, Y., Dai, Y., Wu, G., Shao, Z., Zeng, Q., et al. (2012). Cloning and biochemical characterization of a glucosidase from a marine bacterium Aeromonas sp. HC11e-3. World J. Microbiol. Biotechnol. 28, 3337-3344. doi: 10.1007/s11274-012-1145-8
63. Huston, A. L., Methe, B., and Deming, J. W. (2004). Purification, characterization, and sequencing of an extracellular cold-active aminopeptidase produced by marine psychrophile Colwellia psychrerythraea Strain 34H. Appl. Environ. Microbiol. 70, 3321-3328. doi: 10.1128/AEM.70.6.3321-3328.2004
64. Imhoff, J. F., Labes, A., and Wiese, J. (2011). Bio-mining the microbial treasures of the ocean: new natural products. Biotechnol. Adv. 29, 468-482. doi: 10.1016/j.biotechadv.2011.03.001
65. Jaeger, K. E., Dijkstra, B. W., and Reetz, M. T. (1999). Bacterial biocatalysts:molecular biology, three-dimensional structures, and biotechnological applications of lipases. Annu. Rev. Microbiol. 53, 315-351. doi: 10.1146/annurev.micro.53.1.315
66. Jeon, J. H., Kim, J. T., Lee, H. S., Kim, S.-J., Kang, S. G., Choi, S. H., et al. (2011). Novel lipolytic enzymes identified from metagenomic library of deep-sea sediment. Evid. Based Complement. Alternat. Med. 2011, 271419. doi: 10.1155/2011/271419
67. Jeon, J. H., Lee, H. S., Kim, J. T., Kim, S. J., Choi, S. H., Kang, S. G., et al. (2012). Identification of a new subfamily of salt-tolerant esterases from a metagenomic library of tidal flat sediment. Appl. Microbiol. Biotechnol. 93, 623-631. doi: 10.1007/s00253-011-3433-x
68. Jiang, X., Huo, Y., Cheng, H., Zhang, X., Zhu, X., and Wu, M. (2012b). Cloning, expression and characterization of a halotolerant esterase from a marine bacterium Pelagibacterium halotolerans B2T. Extremophiles 16, 427-435. doi: 10.1007/s00792-012-0442-3
69. Jiang, X., Xu, X., Huo, Y., Wu, Y., Zhu, X., Zhang, X., et al. (2012a). Identification and characterization of novel esterases from a deep-sea sediment metagenome. Arch. Microbiol. 194, 207-214. doi: 10.1007/s00203-011-0745-2
70. Jiang, Z., Le Bail, A., and Wu, A. (2008). Effect of the thermostable xylanase B (XynB) from Thermotoga maritima on the quality of frozen partially baked bread. J. Cereal Sci. 47, 172-179. doi: 10.1016/j.jcs.2007.03.013
71. Jonghee, K., and Hon, S.-K. (2012). Isolation and characterization of an agarase-producing bacterial strain, Alteromonas sp. GNUM-1, from the West Sea, Korea. J. Microbiol. Biotechnol. 22, 1621-1628. doi: 10.4014/jmb.1209.08087
72. Kang, W., Xu, Y., Qin, L., and Wang, Y. (2010). Effects of Different ß-D-Glycosidases on bound aroma compounds in muscat grape determined by HS-SPME and GC-MS. J. Inst. Brewing 116, 70-77. doi: 10.1002/j.2050-0416.2010.tb00400.x
73. Kango, N., and Jain, S. C. (2011). Production and properties of microbial inulinases: recent advances. Food Biotechnol. 25, 165-212. doi: 10.1080/08905436.2011.590763
74. Kennedy, J., Flemer, B., Jackson, S. A., Lejon, D. P. H., Morrissey, J. P., O'Gara, F., et al. (2010). Marine metagenomics: new tools for the study and exploitation of marine microbial metabolism. Mar. Drugs 8, 608-628. doi: 10.3390/md8030608
75. Kerkhoffs, P. L. (1981). Preparation of fructose. US patent 4277563.
76. Khan, S., Pozzo, T., Megyeri, M., Lindahl, S., Sundin, A., Turner, C., et al. (2011). Aglycone specificity of Thermotoga neapolitana ß-glucosidase 1A modified by mutagenesis, leading to increased catalytic efficiency in quercetin-3-glucoside hydrolysis. BMC Biochem. 12:11. doi: 10.1186/1471-2091-12-11
77. Klomklao, S. (2008). Digestive proteinases from marine organisms and their applications. Songklanakarin J. Sci. Technol. 30, 37-46.
78. Klotz, A., Brown, K. M., and Zaretsky, E. M. (2010). Microbial trypsin mutants having chymotrypsin activity and nucleic acids encoding same. US Patent Application 20100151515 A1.
79. Korhonen, H. (2009). Milk-derived bioactive peptides: from science to applications. J. Funct. Foods 1, 177-187. doi: 10.1016/j.jff.2009.01.007
80. Kumar, P. S., Ghosh, M., Pulicherla, K. K., and Rao, K. R. S. S. (2011). Cold active enzymes from the marine psychrophiles: biotechnological perspective. Adv. Biotech. 10, 16-20.
81. Leary, D., Vierros, M., Hamon, G., Arico, S., and Monagle, C. (2009). Marine genetic resources: a review of scientific and commercial interest. Mar. Policy 33, 183-194. doi: 10.1016/j.marpol.2008.05.010
82. Lee, Y. H., Jun, S. E., and Shin, H. D. (2005). Low molecular weight agarose-specific alpha-agarase from agarolytic marine microorganism Pseudoalteromonas sp. BL-3 which hydrolyzes alpha-1, 3-glycoside bond of agar or agarose to produce agarobiose and agarotetraose. Patent KR2005079035-A.
83. Lee, Y., Oh, C., De Zoysa, M., Kim, H., Wickramaarachchi, W. D. N., Whang, I., et al. (2013). molecular cloning, overexpression, and enzymatic characterization of glycosyl hydrolase family 16 ß-agarase from marine bacterium Saccharophagus sp. AG21 in Escherichia coli. J. Microbiol. Biotechnol. 23, 913-922. doi: 10.4014/jmb.1209.09009
84. Li, A.-X., Guo, L.-Z., and Lu, W.-D. (2012). Alkaline inulinase production by a newly isolated bacterium Marinimicrobium sp. LS-A18 and inulin hydrolysis by the enzyme. World J. Microbiol. Biotechnol. 28, 81-89. doi: 10.1007/s11274-011-0794-3
85. Li, H., Chi, Z., Duan, X., Wang, L., Sheng, J., and Wu, L. (2007). Glucoamylase production by the marine yeast Aureobasidium pullulans N13d and hydrolysis of potato starch granules by the enzyme. Process Biochem. 42, 462-465. doi: 10.1016/j.procbio.2006.09.012
86. Li, P. Y., Ji, P., Li, C. Y., Zhang, Y., Wang, G. L., and Zhang, X. Y. (2014). Structural basis for dimerization and catalysis of a novel esterase from the GTSAG motif subfamily of the bacterial hormone-sensitive lipase family. J. Biol. Chem. 289, 19031-19041. doi: 10.1074/jbc.M114.574913
87. Li, X., Chi, Z., Liu, Z., Yan, K., and Li, H. (2008). Phytase production by a marine yeast Kodamea ohmeri BG3. Appl. Biochem. Biotechnol. 149, 183-193. doi: 10.1007/s12010-007-8099-6
88. Liang, Q. (2005). "Understanding starches and their roles in foods, " in Food Carbohydrates Chemistry, Physical Properties, and Applications, ed S. W. Cui (Boca Raton, FL: CRC Press), 309-355.
89. Lima, D. M., Fernandes, P., Nascimento, D. S., Ribeiro, R. C. L. F., and de Assis, S. A. A. (2011). Fructose syrup: a biotechnology asset. Food Technol. Biotechnol. 49, 424-434.
90. Longo, M. A., and Sanromán, M. A. (2006). Production of food aroma compounds: microbial and enzymatic methodologies. Food Technol. Biotechnol. 44, 335-353.
91. Lu, W.-D., Li, A.-X., and Guo, Q.-L. (2014). Production of novel alkalitolerant and thermostable inulinase from marine actinomycete Nocardiopsis sp. DN-K15 and inulin hydrolysis by the enzyme. Ann. Microbiol. 64, 441-449. doi: 10.1007/s13213-013-0674-1
92. Lundemo, P., Adlercreutz, P., and Karlsson, E. N. (2013). Improved transferase/hydrolase ratio through rational design of a family 1 ß-glucosidase from Thermotoga neapolitana. Appl. Environ. Microbiol. 79, 3400-3405. doi: 10.1128/AEM.00359-13
93. Mao, X., Hong, Y., Shao, Z., Zhao, Y., and Liu, Z. (2010). A novel cold-active and alkali-stable ß-glucosidase gene isolated from the marine bacterium Martelella mediterranea. Appl. Biochem. Biotechnol. 162, 2136-2148. doi: 10.1007/s12010-010-8988-y
94. Meenakshi, S., Umayaparvathi, S., Manivasagan, P., Arumugam, M., and Balasubramanian, T. (2013). Purification and characterization of inulinase from marine bacterium Bacillus cereus MU-31. Indian J.Geo-Marine Sci. 42, 510-515.
95. Miguel, A. S. M., Martins-Meyer, T. S., Figueiredo, E. V. C., Lobo, V. W. P., and Dellamora-Ortiz, G. M. (2013). "Enzymes in bakery: current and future trends, " in Food Industry, ed I. Muzzalupo (e-book, InTech). Available onlineat: http://www.intechopen.com/books/food-industry/enzymes-in-bakery-current-and-future-trends
96. Mikkelson, A., Maaheimo, H., and Hakala, T. (2013). Hydrolysis of konjac glucomannan by Trichoderma reesei mannanase and endoglucanases Cel7B and Cel5A for the production of glucomannooligosaccharides. Carbohydrate Res. 372, 60-68. doi: 10.1016/j.carres.2013.02.012
97. Minegishi, H., Shimane, Y., Echigo, A., Ohta, Y., Hatada, Y., Kamekura, M., et al. (2013). Thermophilic and halophilic ß-agarase from a halophilic archaeon Halococcus sp. 197A. Extremophiles 17, 931-939. doi: 10.1007/s00792-013-0575-z
98. Mittal, A., Gupta, V., Singh, G., Yadav, A., and Aggarwal, N. K. (2013). Phytase: a boom in food industry. Octa J. Biosci. 1, 158-169.
99. Mohankumar, A., and Ranjitha, P. (2010). Purification and characterization of esterase from marine Vibrio fischeri isolated from squid. Indian J. Mar. Sci. 39, 262-269.
100. Mojsov, K. (2013). Use of enzymes in wine making: a review. Int. J. Market. Technol. 3, 112-127.
101. Molkabadi, E. Z., Hamidi-Esfahani, Z., Sahari, M. A., and Hosein Azizi, M. (2013). A new native source of tannase producer, Penicillium sp. EZ-ZH190: characterization of the enzyme. Iran. J. Biotechnol. 11, 244-250. doi: 10.5812/ijb.11848
102. Nakaya, K., Ohtara, K., Okamoto, T., Yamada, N., and Kaga, C. (2010). Low-protein food and manufacturing method for same. Patent application US20100316762 A1.
103. Nedwin, G., Sharma, V., and Shetty, J. (2011). a-Amylase blend for starch processing and use thereof Patent application. WO 2011017093 A1.
104. Ni, X., Yue, L., Chi, Z., Li, J., Wang, X., and Madzak, C. (2009). Alkaline protease gene cloning from the marine yeast Aureobasidium pullulans HN2-3 and the protease surface display on Yarrowia lipolytica for bioactive peptide production. Mar. Biotechnol. 11, 81-89. doi: 10.1007/s10126-008-9122-9
105. Nielsen, M. K., and Nielsen, H. H. (2012). "Seafood enzymes, " in Food Biochemistry and Food Processing, eds L. Simpson, F. Nollet, B. Soottawat, P. Gopinadhan, and Y. Hui (Ames, IA: Wiley-Blackwell), 247-262.
106. Ohta, Y., Hatada, Y., Miyazaki, M., Nogi, Y., Ito, S., and Horikoshi, K. (2005). Purification and characterization of a Novel a-agarase from a Thalassomonas sp. Curr. Microbiol. 50, 212-216. doi: 10.1007/s00284-004-4435-z
107. Palanisami, S., Kannan, K., and Lakshmanan, U. (2012). Tannase activity from the marine cyanobacterium Phormidium valderianum BDU140441. J. Appl. Phycol. 24, 1093-1098. doi: 10.1007/s10811-011-9738-4
108. Pancha, I., Jain, D., Shrivastav, A., Mishra, S. K., Shethia, B., Mishra, S., et al. (2010). A thermoactive a-amylase from a Bacillus sp. isolated from CSMCRI salt farm. Int. J. Biol. Macromol. 47, 288-291. doi: 10.1016/j.ijbiomac.2010.04.006
109. Panda, T., and Gowrishankar, B. S. (2005). Production and applications of esterases. Appl. Microbiol. Biotechnol. 67, 160-169. doi: 10.1007/s00253-004-1840-y
110. Paravidino, M., Böhm, P., Gröger, H., and Hanefeld, U. (2012). "Hydrolysis and formation of carboxylic acid esters, " in Enzyme Catalysis in Organic Synthesis: A Comprehensive Handbook, eds K. Drauz, H. Gröger, and O. May (Weinheim: Wiley-VCH Verlag and Co KGaA), 249-361.
111. Parker, K., Salas, M., and Nwosu, V. C. (2010). High fructose corn syrup: production, uses and public health concerns. Biotechnol. Mol. Biol. Rev. 5, 71-78
112. Peng, Q., Wang, X., Shang, M., Huang, J., Guan, G., Li, Y., et al. (2014). Isolation of a novel alkaline-stable lipase from a metagenomic library and its specific application for milkfat flavor production. Microb. Cell Fact. 13, 1-9. doi: 10.1186/1475-2859-13-1
113. Potin, P., Richard, C., Rochas, C., and Kloareg, B. (1993). Purification and characterization of the a-agarase from Alteromonas agarlyticus (Cataldi) comb. nov., strain GJ1B. Eur. J. Biochem. 214, 599-607. doi: 10.1111/j.1432-1033.1993.tb17959.x
114. Pozzo, T., Pasten, J. L., Karlsson, E. N., and Logan, D. T. (2010). Structural and functional analyses of beta-glucosidase 3B from Thermotoga neapolitana: a thermostable three-domain representative of glycoside hydrolase 3. J. Mol. Biol. 397, 724-739. doi: 10.1016/j.jmb.2010.01.072
115. Ramnani, P., Chitarrari, R., Tuohy, K., Grant, J., Hotchkiss, S., Philp, K., et al. (2012). In vitro fermentation and prebiotic potential of novel low molecular weight polysaccharides derived from agar and alginate seaweeds. Anaerobe 18, 1-6. doi: 10.1016/j.anaerobe.2011.08.003
116. Ran, L. Y., Su, H. N., Zhao, G. Y., Gao, X., Zhou, M. Y., Wang, P., et al. (2013). Structural and mechanistic insights into collagen degradation by a bacterial collagenolytic serine protease in the subtilisin family. Mol. Microbiol. 90, 997-1010. doi: 10.1111/mmi.12412
117. Ran, L. Y., Su, H. N., Zhou, M. Y., Wang, L., Chen, X. L., Xie, B. B., et al. (2014). Characterization of a novel subtilisin-like protease myroicolsin from deep sea bacterium Myroides profundi D25 and molecular insight into its collagenolytic mechanism. J. Biol. Chem. 289, 6041-6053. doi: 10.1074/jbc.M113.513861
118. Ricca, E., Calabr, ò, V., Curcio, S., and Iorio, G. (2007). The state of the art in the production of fructose from inulin enzymatic hydrolysis. Crit. Rev. Biotechnol. 27, 129-145. doi: 10.1080/07388550701503477
119. Sawant, R., and Nagendran, S. (2014). Protease: an enzyme with multiple industrial applications. World J. Pharm. Pharm. Sci. 3, 568-579.
120. Schwerdtfeger, R. M., Chiaraluce, R., Consalvi, V., Scandurra, R., and Antranikian, G. (1999). Stability, refolding and Ca2+ binding of pullulanase from the hyperthermophilic archaeon Pyrococcus woesei. Eur. J. Biochem. 264, 479-487. doi: 10.1046/j.1432-1327.1999.00640.x
121. Seok, J. H., Kim, H.-S., Hatada, Y., Nam, S.-W., and Kim, Y.-H. (2012). Construction of an expression system for the secretory production of recombinant a-agarase in yeast. Biotechnol. Lett. 34, 1041-1049. doi: 10.1007/s10529-012-0864-0
122. Sharma, M., and Kumar, A. (2013). Xylanases: an overview. Br. Biotechnol. J. 3, 1-28. doi: 10.9734/BBJ/2013/1784
123. Sriram, N., Priyadharshini, M., and Sivasakthi, S. (2012). Production and characterization of amino peptidase from marine aspergillus flavus. Int. J. Microbiol. Res. 3, 221-226. doi: 10.5829/idosi.ijmr.2012.3.3.66171
124. Singh, A., Das, M., Bal, S., and Banerjee, R. (2014). "Rice processing, " in Engineering Aspects of Cereal and Cereal-Based Products, eds R. P. F. Guiné and P. M. R. Correia (Boca Raton, FL: CRC Press), 71-95.
125. Steen, A. D., and Arnosti, C. (2013). Extracellular peptidase and carbohydrate hydrolase activities in an Arctic fjord (Smeerenburgfjord, Svalbard). Aquat. Microb. Ecol. 69, 93-99. doi: 10.3354/ame01625
126. Struvay, C., and Feller, G. (2012). Optimization to low temperature activity in psychrophilic enzymes. Int. J. Mol. Sci. 13, 11643-11665. doi: 10.3390/ijms130911643
127. Su, E., Xia, T., Gao, L., Dai, O., and Zhang, Z. (2010). Immobilization of ß glucosidase and its aromaincreasing effect on tea beverage. Food Bioproducts Proc. 88, 83-89. doi: 10.1016/j.fbp.2009.04.001
128. Sun, H., Xue, Y., and Lin, Y. (2014). Enhanced catalytic efficiency in Quercetin-4'-glucoside Hydrolysis of Thermotoga maritima ß-Glucosidase a by site-directed mutagenesis. J. Agric. Food Chem. 62, 6763-6770. doi: 10.1021/jf501932v
129. Takagi, H., Kondou, M., Tomoaki, H., Nakamori, S., Tsai, Y.-C. H., and Yamasaki, M. (1992). Effects of an alkaline elastase from an alkalophilic Bacillus strain on the tenderization of beef meat. J. Agric. Food Chem. 40, 2364-2368. doi: 10.1021/jf00024a008
130. Temuujin, U., Chi, W. J., Chang, Y. K., and Hong, S. K. (2012). Identification and biochemical characterization of Sco3487 from Streptomyces coelicolor A3(2), an exo-and endo-type ß-agarase-producing neoagarobiose. J. Bacteriol. 194, 142-149. doi: 10.1128/JB.05978-11
131. Tramice, A., Andreotti, G., and Trincone, A. (2011). Hydrosoluble antioxidants by enzymatic glucosylation of a vitamin E derivative using marine a-D-Glucosidase from Aplysia fasciata. Mar. Biotechnol. 13, 773-781. doi: 10.1007/s10126-010-9339-2
132. Trincone, A. (2011). Marine biocatalysts: enzymatic features and applications. Mar. Drugs 9, 478-499. doi: 10.3390/md9040478
133. Trincone, A. (2013a). Biocatalytic processes using marine biocatalysts: ten cases in point. Curr. Org. Chem. 17, 1058-1066.
134. Trincone, A. (2013b). Angling for uniqueness in enzymatic preparation of glycosides. Biomolecules 3, 334-350. doi: 10.3390/biom3020334
135. Turner, P., Svensson, D., Adlercreutz, P., and Karlsson, E. N. (2007). A novel variant of Thermotoga neapolitana ß-glucosidase B is an eficiente catalyst for the synthesis of alkyl glucosides by transglycosylation. J. Biotechnol. 130, 67-74. doi: 10.1016/j.jbiotec.2007.02.016
136. Uchiyama, T., Kawamura, M., Sashida, R., Ueda, M., Ohba, S., and Ohkishi, H. (2005). Method of manufacturing inulotriose and/or inulotetrose using an exo-type hydrolase capable of hydrolyzinga fructan only every 3 or 4 sugar units from a terminal fructose. US patent 5122460.
137. Uzyol, K. S., Sariyar-Akbulut, B., Denizci, A. A., and Kazan, D. (2012). Thermostable a-amylase from moderately halophilic Halomonas sp. AAD21. Turk. J. Biol. 36, 327-338. doi: 10.3906/biy-1106-7
138. Veltman, O. R., Vriend, G., Berendsen, H. J. C., Van den Burg, B., Venema, G., and Eijsink, V. G. H. (1998). A single calcium binding site is crucial for the calcium-dependent thermal stability of thermolysin-like proteases. Biochemistry 37, 5312-5319. doi: 10.1021/bi9725879
139. Vijayaraghavan, R., and Rajendran, S. (2012). Identification of a novel agarolytic ?-proteobacterium Microbulbifer maritimus and characterization of its agarase. J. Basic Microbiol. 52, 705-712. doi: 10.1002/jobm.201100315
140. Visser, J., Hinz, S., Verij, J., Visser, J., Joosten, V., Koetsier, M., et al. (2012). Novel fungal esterases. WIPO Patent Application WO/2012/078741 A2.
141. Wang, Y., Zhang, C., Li, J., and Xu, Y. (2013). Different in?uences of ß-glucosidases on volatile compounds and anthocyanins of Cabernet Gernischt and possible reason. Food Chem. 140, 245-254. doi: 10.1016/j.foodchem.2013.02.044
142. Ward, O. P., Rao, M. B., and Kulkarni, A. (2009). "Proteases, " in Encyclopedia of Microbiology, Vol. 1, ed M. Schaechter (Oxford: Elsevier), 495-511.
143. Wu, S.-J., and Chen, J. (2014). Preparation of maltotriose from fermentation broth by hydrolysis of pullulan using pullulanase. Carbohydrate Pol. 107, 94-97. doi: 10.1016/j.carbpol.2014.02.050
144. Xie, W., Lin, B., Zhou, Z., Lu, G., Lun, J., Xia, C., et al. (2013). Characterization of a novel ß-agarase from an agar-degrading bacterium Catenovulum sp. X3. Appl. Microbiol. Biotechnol. 97, 4907-4915. doi: 10.1007/s00253-012-4385-5
145. Xu, J.-L., Lu, M.-S., Wang, S.-J., Li, H. Z., Sun, Y.-Y., and Fang, Y.-W. (2009). Production and characterization of pullulanase from hyperthermophilic archaeon Thermococcus sp.HJ21. J. Food Sci. Biotechnol. 2, 243-249.
146. Ye, M., Yu, C.-Y., Li, N., and Zong, M.-H. (2011). Highly regioselective glucosylation of 2'-deoxynucleosides by using the crude ß-glycosidase from bovine liver. J. Biotechnol. 155, 203-208. doi: 10.1016/j.jbiotec.2011.06.031
147. Yuan, D., Lan, D., Xin, R., Yang, B., and Wang, Y. (2014). Biochemical properties of a new cold-active mono-and diacylglycerol lipase from marine member Janibacter sp. strain HTCC2649. Int. J. Mol. Sci. 15, 10554-10566. doi: 10.3390/ijms150610554
148. Zhang, C., and Kim, S.-K. (2010). Research and application of marine microbial enzymes: status and prospects. Mar. Drugs 8, 1920-1934. doi: 10.3390/md8061920
149. Zhang, Z., Marquardt, R. R., Wang, G., Guenter, W., Crow, G. H., Han, Z., et al. (1996). A simple model for predicting the response of chicks to dietary enzyme supplementation. J. Anim. Sci. 74, 394-402.
150. Zhao, G. Y., Zhou, M. Y., Zhao, H. L., Chen, X. L., Xie, B. B., Zhang, X. Y., et al. (2012a). Tenderization effect of cold-adapted collagenolytic protease MCP-01 on beef meat at low temperature and its mechanism. Food Chem. 134, 1738-1744. doi: 10.1016/j.foodchem.2012.03.118
151. Zhao, H. L., Chen, X. L., Xie, B. B., Zhou, M. Y., Gao, X., and Zhang, X. Y. (2012b). Elastolytic mechanism of a novel M23 metalloprotease pseudoalterin from deep-sea Pseudoalteromonas sp. CF6-2: cleaving not only glycyl bonds in the hydrophobic regions but also peptide bonds in the hydrophilic regions involved in cross-linking. J. Biol. Chem. 287, 39710-39720. doi: 10.1074/jbc.M112.405076
152. Zhao, L., Budge, S. M., Ghaly, A. E., Brooks, M. S., and Dave, D. (2011). Extraction, purification and characterization of fish pepsin: a critical review. Food Process. Technol. 2, 1-14. doi: 10.4172/2157-7110.1000126
153. Zheng, H., Guo, B., Chen, X. L., Fan, S. J., and Zhang, Y. Z. (2011). Improvement of the quality of wheat bread by addition of glycoside hydrolase family 10 xylanases. Appl. Microbiol. Biotechnol. 90, 509-515. doi: 10.1007/s00253-011-3088-7