Cold and hot extremozymes: Industrial relevance and current trends

Frontiers in Bioengineering and Biotechnology

Volumn 3, Issue OCT, 2015, Pages

  Sarmiento, Felipe ^a   Peralta, Rocío ^b   Blamey, Jenny M ^a,b  

^a Swissaustral USA LLC   (United States)

^b Fundación Científica y Cultural Biociencia ^*  (Chile)

Author keywords

Cold adapted enzymes; Extremophiles; Extremozymes; Hyperthermophiles; Psychrophiles; Thermophiles

Indexed keywords

BIOCATALYSTS; CATALYSIS; MICROBIOLOGY; MICROORGANISMS;

COLD-ADAPTED ENZYMES; EXTREMOPHILES; EXTREMOZYMES; HYPERTHERMOPHILES; PSYCHROPHILES; THERMOPHILES;

ENZYMES;

EID: 84976381688     PISSN: None     EISSN: 22964185     Source Type: Journal    
DOI: 10.3389/fbioe.2015.00148     Document Type: Review

References (128)

1. Achenbach-Richter, L., Stetter, K. O., and Woese, C. R. (1987). A possible biochemical missing link among archaebacteria. Nature 327, 348-349. doi:10.1038/327348a0
2. Adapa, V., Ramya, L. N., Pulicherla, K. K., and Rao, K. R. (2014). Cold active pectinases: advancing the food industry to the next generation. Appl. Biochem. Biotechnol. 172, 2324-2337. doi:10.1007/s12010-013-0685-1
3. Adrio, J. L., and Demain, A. L. (2014). Microbial enzymes: tools for biotechnological processes. Biomolecules 4, 117-139. doi:10.3390/biom4010117
4. Alias, N., Ahmad Mazian, M., Salleh, A. B., Basri, M., and Rahman, R. N. (2014). Molecular cloning and optimization for high level expression of cold-adapted serine protease from antarctic yeast Glaciozyma antarctica PI12. Enzyme Res. 2014, 197938. doi:10.1155/2014/197938
5. Asenjo, J. A., Andrews, B. A., Acevedo, J. P., Parra, L., and Burzio, L. O. (2014a). Protein and DNA Sequence Encoding a Cold Adapted Xylanase. US Patent No 8679814 B2. United States Patent and Trademark Office.
6. Asenjo, J. A., Andrews, B. A., Acevedo, J. P., Reyes, F., and Burzio, L. O. (2014b). Protein and DNA Sequence Encoding a Cold Adapted Subtilisin-Like Activity. US Patent No 8759065 B2. United States Patent and Trademark Office.
7. Awazu, N., Shodai, T., Takakura, H., Kitagawa, M., Mukai, H., and Kato, I. (2011). Microorganism-Derived Psychrophilic Endonuclease. US Patent No 8034597 B2. United States Patent and Trademark Office.
8. Bachmann, B. O., Van Lanen, S. G., and Baltz, R. H. (2014). Microbial genome mining for accelerated natural products discovery: is a renaissance in the making? J. Ind. Microbiol. Biotechnol. 41, 175-184. doi:10.1007/s10295-013-1389-9
9. Bakermans, C., and Skidmore, M. L. (2011). Microbial metabolism in ice and brine at-5 degrees C. Environ. Microbiol. 13, 2269-2278. doi:10.1111/j.1462-2920.2011.02485.x
10. Baldrian, P. (2004). Purification and characterization of laccase from the white-rot fungus Daedalea quercina and decolorization of synthetic dyes by the enzyme. Appl. Microbiol. Biotechnol. 63, 560-563. doi:10.1007/s00253-003-1434-0
11. Beeder, J., Nilsen, R. K., Rosnes, J. T., Torsvik, T., and Lien, T. (1994). Archaeoglobus fulgidus isolated from hot North Sea oil field waters. Appl. Environ. Microbiol. 60, 1227-1231.
12. Beg, Q. K., Bhushan, B., Kapoor, M., and Hoondal, G. S. (2000). Enhanced production of a thermostable xylanase from Streptomyces sp. QG-11-3 and its application in biobleaching of Eucalyptus kraft pulp. Enzyme Microb. Technol. 27, 459-466. doi:10.1016/S0141-0229(00)00231-3
13. Bentley, I. S., and Williams, E. C. (1996). "Starch conversion," in Industrial Enzymology, ed. W. S. Godfrey (New York, NY: Stockton Press), 341-357.
14. Berka, R. M., Schneider, P., Golightly, E. J., Brown, S. H., Madden, M., Brown, K. M., et al. (1997). Characterization of the gene encoding an extracellular laccase of Myceliophthora thermophila and analysis of the recombinant enzyme expressed in Aspergillus oryzae. Appl. Environ. Microbiol. 63, 3151-3157.
15. 2 on the growth of the hyperthermophilic archaeon Pyrococcus furiosus. Extremophiles 6, 161-166. doi:10.1007/s007920100244
16. Blochl, E., Rachel, R., Burggraf, S., Hafenbradl, D., Jannasch, H. W., and Stetter, K. O. (1997). Pyrolobus fumarii, gen. and sp. nov., represents a novel group of archaea, extending the upper temperature limit for life to 113 degrees C. Extremophiles 1, 14-21. doi:10.1007/s007920050010
17. Borchert, T. V., Svendsen, A., Andersen, C., Nielsen, B., Nissem, T. L., and Kjærulff, S. (2004). Exhibit Alterations in at Least One of the Following Properties Relative to Parent Alpha-Amylase: Improved pH Stability at pH 8-10.5, Improved Calcium Ion Stability at pH 8-10.5, Increased Specific Activity at 10-60 Degrees C. US Patent No 6673589 B2. United States Patent and Trademark Office.
18. Brock, T. D., Brock, K. M., Belly, R. T., and Weiss, R. L. (1972). Sulfolobus: a new genus of sulfur-oxidizing bacteria living at low pH and high temperature. Arch. Mikrobiol. 84, 54-68. doi:10.1007/BF00408082
19. Bult, C. J., White, O., Olsen, G. J., Zhou, L., Fleischmann, R. D., Sutton, G. G., et al. (1996). Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii. Science 273, 1058-1073. doi:10.1126/science.273.5278.1058
20. Calero-Rueda, O., Gutierrez, A., Del Rio, J. C., Prieto, A., Plou, F., Ballesteros, A., et al. (2004). Hydrolysis of sterol esters by an esterase from Ophiostoma piceae: application to pitch control in pulping of Eucalyptus globulus wood. Int. J. Biotechnol. 6, 367-375. doi:10.1504/IJBT.2004.005519
21. Canganella, F., and Wiegel, J. (2011). Extremophiles: from abyssal to terrestrial ecosystems and possibly beyond. Naturwissenschaften 98, 253-279. doi:10.1007/s00114-011-0775-2
22. Cavicchioli, R., Charlton, T., Ertan, H., Mohd Omar, S., Siddiqui, K. S., and Williams, T. J. (2011). Biotechnological uses of enzymes from psychrophiles. Microb. Biotechnol. 4, 449-460. doi:10.1111/j.1751-7915.2011.00258.x
23. Chen, C., Adolphson, R., Dean, J. F. D., Eriksson, K. L., Adams, M. W. W., and Westpheling, J. (1997). Release of lignin from kraft pulp by a hyperthermophilic xylanase from Thermatoga maritima. Enzyme Microb. Technol. 20, 39-45. doi:10.1016/S0141-0229(97)82192-8
24. Chen, M., Li, H., Chen, W., Diao, W., Liu, C., Yuan, M., et al. (2013a). [Isolation, identification and characterization of 68 protease-producing bacterial strains from the Arctic]. Wei Sheng Wu Xue Bao 53, 702-709.
25. Chen, S., Kaufman, M. G., Miazgowicz, K. L., Bagdasarian, M., and Walker, E. D. (2013b). Molecular characterization of a cold-active recombinant xylanase from Flavobacterium johnsoniae and its applicability in xylan hydrolysis. Bioresour. Technol. 128, 145-155. doi:10.1016/j.biortech.2012.10.087
26. Cheng, Y. Y., Qian, Y. K., Li, Z. F., Wu, Z. H., Liu, H., and Li, Y. Z. (2011). A novel cold-adapted lipase from Sorangium cellulosum strain So0157-2: gene cloning, expression, and enzymatic characterization. Int. J. Mol. Sci. 12, 6765-6780. doi:10.3390/ijms12106765
27. Chintalapati, S., Kiran, M. D., and Shivaji, S. (2004). Role of membrane lipid fatty acids in cold adaptation. Cell Mol. Biol. (Noisy-le-grand) 50, 631-642. doi:10.1170/T553
28. Collins, T., Gerday, C., and Feller, G. (2005). Xylanases, xylanase families and extremophilic xylanases. FEMS Microbiol. Rev. 29, 3-23. doi:10.1016/j.femsre.2004.06.005
29. Collins, T., Meuwis, M. A., Stals, I., Claeyssens, M., Feller, G., and Gerday, C. (2002). A novel family 8 xylanase, functional and physicochemical characterization. J. Biol. Chem. 277, 35133-35139. doi:10.1074/jbc.M204517200
30. Cowen, D. A. (2004). The upper temperature of life-where do we draw the line? Trends Microbiol. 12, 58-60. doi:10.1016/j.tim.2003.12.002
31. D'Amico, S., Collins, T., Marx, J. C., Feller, G., and Gerday, C. (2006). Psychrophilic microorganisms: challenges for life. EMBO Rep. 7, 385-389. doi:10.1038/sj.embor.7400662
32. de Souza, P. M., and de Oliveira Magalhaes, P. (2010). Application of microbial alpha-amylase in industry-a review. Braz. J. Microbiol. 41, 850-861. doi:10.1590/S1517-83822010000400004
33. Del-Cid, A., Ubilla, P., Ravanal, M. C., Medina, E., Vaca, I., Levican, G., et al. (2014). Cold-active xylanase produced by fungi associated with Antarctic marine sponges. Appl. Biochem. Biotechnol. 172, 524-532. doi:10.1007/s12010-013-0551-1
34. Dewan, S. S. (2014). Global Markets for Enzymes in Industrial Applications. Wellesley, MA: BCC Research.
35. Di Giulio, M. (2005). A comparison of proteins from Pyrococcus furiosus and Pyrococcus abyssi: barophily in the physicochemical properties of amino acids and in the genetic code. Gene 346, 1-6. doi:10.1016/j.gene.2004.10.008
36. Dominguez, A., Sanroman, A., Fucinos, P., Rua, M. L., Pastrana, L., and Longo, M. A. (2004). Quantification of intra-and extra-cellular thermophilic lipase/esterase production by Thermus sp. Biotechnol. Lett. 26, 705-708. doi:10.1023/B:BILE.0000024092.27943.75
37. Donadio, S., Monciardini, P., and Sosio, M. (2009). Chapter 1. Approaches to discovering novel antibacterial and antifungal agents. Methods Enzymol. 458, 3-28. doi:10.1016/S0076-6879(09)04801-0
38. Dornez, E., Verjans, P., Arnaut, F., Delcour, J. A., and Courtin, C. M. (2011). Use of psychrophilic xylanases provides insight into the xylanase functionality in bread making. J. Agric. Food Chem. 59, 9553-9562. doi:10.1021/jf201752g
39. Du, B. B., Hao, S., Li, Y. M., Yue, L. L., and Jiao, Q. H. (2006). [Expression of a thermostable a-amylase mutant into Escherichia coli and Pichia pastoris]. Wei Sheng Wu Xue Bao 46, 827-830.
40. Feller, G. (2010). Protein stability and enzyme activity at extreme biological temperatures. J. Phys. Condens. Matter 22, 323101. doi:10.1088/0953-8984/22/32/323101
41. Feller, G. (2013). Psychrophilic enzymes: from folding to function and biotechnology. Scientifica (Cairo) 2013, 512840. doi:10.1155/2013/512840
42. Feller, G., Le Bussy, O., and Gerday, C. (1998). Expression of psychrophilic genes in mesophilic hosts: assessment of the folding state of a recombinant α-amylase. Appl. Environ. Microbiol. 64, 1163-1165.
43. Friedrich, C. G. (1998). Physiology and genetics of sulfur-oxidizing bacteria. Adv. Microb. Physiol. 39, 235-289. doi:10.1016/S0065-2911(08)60018-1
44. Fucinos, P., Abadin, C. M., Sanroman, A., Longo, M. A., Pastrana, L., and Rua, M. L. (2005a). Identification of extracellular lipases/esterases produced by Thermus thermophilus HB27: partial purification and preliminary biochemical characterisation. J. Biotechnol. 117, 233-241. doi:10.1016/j.jbiotec.2005.01.019
45. Fucinos, P., Dominguez, A., Sanroman, M. A., Longo, M. A., Rua, M. L., and Pastrana, L. (2005b). Production of thermostable lipolytic activity by thermus species. Biotechnol. Prog. 21, 1198-1205. doi:10.1021/bp050080g
46. Georlette, D., Jonsson, Z. O., Van Petegem, F., Chessa, J., Van Beeumen, J., Hubscher, U., et al. (2000). A DNA ligase from the psychrophile Pseudoalteromonas haloplanktis gives insights into the adaptation of proteins to low temperatures. Eur. J. Biochem. 267, 3502-3512. doi:10.1046/j.1432-1327.2000.01377.x
47. Ghosh, M., Pulicherla, K. K., Rekha, V. P., Raja, P. K., and Sambasiva Rao, K. R. (2012). Cold active beta-galactosidase from Thalassospira sp. 3SC-21 to use in milk lactose hydrolysis: a novel source from deep waters of Bay-of-Bengal. World J. Microbiol. Biotechnol. 28, 2859-2869. doi:10.1007/s11274-012-1097-z
48. Glaser, R., and Venus, J. (2014). Screening of Bacillus coagulans strains in lignin supplemented minimal medium with high throughput turbidity measurements. Biotechnol. Rep. 4, 60-65. doi:10.1016/j.btre.2014.08.001
49. Graham, J. E., Clark, M. E., Nadler, D. C., Huffer, S., Chokhawala, H. A., Rowland, S. E., et al. (2011). Identification and characterization of a multidomain hyperthermophilic cellulase from an archaeal enrichment. Nat. Commun. 2, 375. doi:10.1038/ncomms1373
50. Gurung, N., Ray, S., Bose, S., and Rai, V. (2013). A broader view: microbial enzymes and their relevance in industries, medicine, and beyond. Biomed Res. Int. 2013, 329121. doi:10.1155/2013/329121
51. Gutierrez, A., del Rio, J. C., and Martinez, A. T. (2009). Microbial and enzymatic control of pitch in the pulp and paper industry. Appl. Microbiol. Biotechnol. 82, 1005-1018. doi:10.1007/s00253-009-1905-z
52. Hmidet, N., Ali, N. E. H., Haddar, A., Kanoun, S., Alya, S. K., and Nasri, M. (2009). Alkaline proteases and thermostable α-amylase co-produced by Bacillus licheniformis NH1: characterization and potential application as detergent additive. Biochem. Eng. J. 47, 71-79. doi:10.1016/j.bej.2009.07.005
53. Horikoshi, K. (1999). Alkaliphiles: some applications of their products for biotechnology. Microbiol. Mol. Biol. Rev. 63, 735-750.
54. Horner, T. W., Dunn, M. L., Eggett, D. L., and Ogden, L. V. (2011). beta-galactosidase activity of commercial lactase samples in raw and pasteurized milk at refrigerated temperatures. J. Dairy Sci. 94, 3242-3249. doi:10.3168/jds.2010-3742
55. Huber, H., and Stetter, K. O. (1998). Hyperthermophiles and their possible potential in biotechnology. J. Biotechnol. 64, 39-52. doi:10.1016/S0168-1656(98)00102-3
56. Ji, X., Chen, G., Zhang, Q., Lin, L., and Wei, Y. (2015). Purification and characterization of an extracellular cold-adapted alkaline lipase produced by psychrotrophic bacterium Yersinia enterocolitica strain KM1. J. Basic Microbiol. 55, 718-728. doi:10.1002/jobm.201400730
57. Jiang, Z. Q., Li, X. T., Yang, S. Q., Li, L. T., Li, Y., and Feng, W. Y. (2006). Biobleach boosting effect of recombinant xylanase B from the hyperthermophilic Thermotoga maritima on wheat straw pulp. Appl. Microbiol. Biotechnol. 70, 65-71. doi:10.1007/s00253-005-0036-4
58. Jiewei, T., Zuchao, L., Peng, Q., Lei, W., and Yongqiang, T. (2014). Purification and characterization of a cold-adapted lipase from oceanobacillus strain PT-11. PLoS ONE 9:e101343. doi:10.1371/journal.pone.0101343
59. Joshi, S., and Satyanarayana, T. (2013). Biotechnology of cold-active proteases. Biology (Basel) 2, 755-783. doi:10.3390/biology2020755
60. Karan, R., Capes, M. D., and Dassarma, S. (2012). Function and biotechnology of extremophilic enzymes in low water activity. Aquat. Biosyst. 8, 4. doi:10.1186/2046-9063-8-4
61. Karlsson, E. N., Holst, O., and Tocaj, A. (1999). Efficient production of truncated thermostable xylanases from Rhodothermus marinus in Escherichia coli fed-batch cultures. J. Biosci. Bioeng. 87, 598-606. doi:10.1016/S1389-1723(99)80121-2
62. Kasana, R. C., and Gulati, A. (2011). Cellulases from psychrophilic microorganisms: a review. J. Basic Microbiol. 51, 572-579. doi:10.1002/jobm.201000385
63. Kim, K. W., and Lee, S. B. (2003). Inhibitory effect of Maillard reaction products on growth of the aerobic marine hyperthermophilic archaeon Aeropyrum pernix. Appl. Environ. Microbiol. 69, 4325-4328. doi:10.1128/AEM.69.7.4325-4328.2003
64. King, O. N., Li, X. S., Sakurai, M., Kawamura, A., Rose, N. R., Ng, S. S., et al. (2010). Quantitative high-throughput screening identifies 8-hydroxyquinolines as cell-active histone demethylase inhibitors. PLoS ONE 5:e15535. doi:10.1371/journal.pone.0015535
65. Kishishita, S., Fujii, T., and Ishikawa, K. (2015). Heterologous expression of hyperthermophilic cellulases of archaea Pyrococcus sp. by fungus Talaromyces cellulolyticus. J. Ind. Microbiol. Biotechnol. 42, 137-141. doi:10.1007/s10295-014-1532-2
66. Kitamoto, N., Yamagata, H., Kato, T., Tsukagoshi, N., and Udaka, S. (1988). Cloning and sequencing of the gene encoding thermophilic beta-amylase of Clostridium thermosulfurogenes. J. Bacteriol. 170, 5848-5854.
67. Klenk, H. P., Clayton, R. A., Tomb, J. F., White, O., Nelson, K. E., Ketchum, K. A., et al. (1997). The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus. Nature 390, 364-370. doi:10.1038/37052
68. Klenk, H. P., Spitzer, M., Ochsenreiter, T., and Fuellen, G. (2004). Phylogenomics of hyperthermophilic archaea and bacteria. Biochem. Soc. Trans. 32(Pt 2), 175-178. doi:10.1042/bst0320175
69. Kletzin, A., Urich, T., Muller, F., Bandeiras, T. M., and Gomes, C. M. (2004). Dissimilatory oxidation and reduction of elemental sulfur in thermophilic archaea. J. Bioenerg. Biomembr. 36, 77-91. doi:10.1023/B:JOBB.0000019600.36757.8c
70. Kluskens, L. D., Zeilstra, J., Geerling, A. C., de Vos, W. M., and van der Oost, J. (2010). Molecular characterization of the glucose isomerase from the thermophilic bacterium Fervidobacterium gondwanense. Environ. Technol. 31, 1083-1090. doi:10.1080/09593330903486673
71. Kobori, H., Sullivan, C. W., and Shizuya, H. (1984). Heat-labile alkaline phosphatase from Antarctic bacteria: Rapid 5' end-labeling of nucleic acids. Proc. Natl. Acad. Sci. U.S.A. 81, 6691-6695. doi:10.1073/pnas.81.21.6691
72. Koutsioulis, D., Wang, E., Tzanodaskalaki, M., Nikiforaki, D., Deli, A., Feller, G., et al. (2008). Directed evolution on the cold adapted properties of TAB5 alkaline phosphatase. Protein Eng. Des. Sel. 21, 319-327. doi:10.1093/protein/gzn009
73. Kristjansson, J. K. (1989). Thermophilic organisms as sources of thermostable enzymes. Trends Biotechnol. 7, 395-401. doi:10.1016/0167-7799(89)90035-8
74. Kuddus, M., Roohi, Saima, and Ahmad, I. Z. (2012). Cold-active extracellular a-amylase production from novel bacteria Microbacterium foliorum GA2 and Bacillus cereus GA6 isolated from Gangotri glacier, Western Himalaya. J. Genet. Eng. Biotechnol. 10, 151-159. doi:10.1016/j.jgeb.2012.03.002
75. Kuhad, R. C., Gupta, R., and Singh, A. (2011). Microbial cellulases and their industrial applications. Enzyme Res. 2011, 280696. doi:10.4061/2011/280696
76. Kühne, W. (1877). über das Verhalten verschiedener organisirter und sog. ungeformter Fermente. Verhandlungen des naturhistorisch-medicinischen Vereins zu Heidelberg 1, 190-193.
77. Kumar, S., and Nussinov, R. (2001). How do thermophilic proteins deal with heat? Cell. Mol. Life Sci. 58, 1216-1233. doi:10.1007/PL00000935
78. Ladenstein, R., and Antranikian, G. (1998). Proteins from hyperthermophiles: stability and enzymatic catalysis close to the boiling point of water. Adv. Biochem. Eng. Biotechnol. 61, 37-85.
79. Lanes, O., Leiros, I., Smalas, A. O., and Willassen, N. P. (2002). Identification, cloning, and expression of uracil-DNA glycosylase from Atlantic cod (Gadus morhua): characterization and homology modeling of the cold-active catalytic domain. Extremophiles 6, 73-86. doi:10.1007/s007920100225
80. Larsson, L., Olsson, G., Holst, O., and Karlsson, H. T. (1990). Pyrite oxidation by thermophilic archaebacteria. Appl. Environ. Microbiol. 56, 697-701.
81. Lee, D. H., Choi, S. L., Rha, E., Kim, S., Yeom, S. J., Moon, J. H., et al. (2015). A novel psychrophilic alkaline phosphatase from the metagenome of tidal flat sediments. BMC Biotechnol. 15:1. doi:10.1186/s12896-015-0115-2
82. Lee, M. S., Kim, G. A., Seo, M. S., Lee, J. H., and Kwon, S. T. (2009). Characterization of heat-labile uracil-DNA glycosylase from Psychrobacter sp. HJ147 and its application to the polymerase chain reaction. Biotechnol. Appl. Biochem. 52(Pt 2), 167-175. doi:10.1042/BA20080028
83. Leis, B., Angelov, A., and Liebl, W. (2013). Screening and expression of genes from metagenomes. Adv. Appl. Microbiol. 83, 1-68. doi:10.1016/B978-0-12-407678-5.00001-5
84. Li, X. L., Zhang, W. H., Wang, Y. D., Dai, Y. J., Zhang, H. T., Wang, Y., et al. (2014). A high-detergent-performance, cold-adapted lipase from Pseudomonas stutzeri PS59 suitable for detergent formulation. J. Mol. Catal. B. Enzym. 102, 16-24. doi:10.1016/j.molcatb.2014.01.006
85. Ling, L. L., Schneider, T., Peoples, A. J., Spoering, A. L., Engels, I., Conlon, B. P., et al. (2015). A new antibiotic kills pathogens without detectable resistance. Nature 517, 455-459. doi:10.1038/nature14098
86. Litantra, R., Lobionda, S., Yim, J. H., and Kim, H. K. (2013). Expression and biochemical characterization of cold-adapted lipases from Antarctic Bacillus pumilus strains. J. Microbiol. Biotechnol. 23, 1221-1228. doi:10.4014/jmb.1305.05006
87. Madigan, M. T., and Marrs, B. L. (1997). Extremophiles. Sci. Am. 276, 82-87. doi:10.1038/scientificamerican0497-82
88. Maras, B., Valiante, S., Chiaraluce, R., Consalvi, V., Politi, L., De Rosa, M., et al. (1994). The amino acid sequence of glutamate dehydrogenase from Pyrococcus furiosus, a hyperthermophilic archaebacterium. J. Protein Chem. 13, 253-259. doi:10.1007/BF01891983
89. Marx, J. C., Collins, T., D'Amico, S., Feller, G., and Gerday, C. (2007). Cold-adapted enzymes from marine Antarctic microorganisms. Mar. Biotechnol. 9, 293-304. doi:10.1007/s10126-006-6103-8
90. Mateo, C., Monti, R., Pessela, B. C., Fuentes, M., Torres, R., Guisan, J. M., et al. (2004). Immobilization of lactase from Kluyveromyces lactis greatly reduces the inhibition promoted by glucose. Full hydrolysis of lactose in milk. Biotechnol. Prog. 20, 1259-1262. doi:10.1021/bp049957m
91. Milagres, A. M. F., Santos, E., Piovan, T., and Roberto, I. C. (2004). Production of xylanase by Thermoascus aurantiacus from sugar cane bagasse in an aerated growth fermentor. Process Biochem. 39, 1387-1391. doi:10.1016/S0032-9592(03)00272-3
92. Mykytczuk, N. C., Foote, S. J., Omelon, C. R., Southam, G., Greer, C. W., and Whyte, L. G. (2013). Bacterial growth at-15 degrees C; molecular insights from the permafrost bacterium planococcus halocryophilus Or1. ISME J. 7, 1211-1226. doi:10.1038/ismej.2013.8
93. Niehaus, F., Bertoldo, C., Kahler, M., and Antranikian, G. (1999). Extremophiles as a source of novel enzymes for industrial application. Appl. Microbiol. Biotechnol. 51, 711-729. doi:10.1007/s002530051456
94. Nisha, M., and Satyanarayana, T. (2013). Recombinant bacterial amylopullulanases: developments and perspectives. Bioengineered 4, 388-400. doi:10.4161/bioe.24629
95. Paloheimo, M., Puranen, T., Valtakari, L., Kruus, K., Kallio, J., Maentylae, A., et al. (2006). Novel Laccase Enzymes and Their Uses. US Patent No 77321784 B2. United States Patent and Trademark Office.
96. Park, I. H., Kim, S. H., Lee, Y. S., Lee, S. C., Zhou, Y., Kim, C. M., et al. (2009). Gene cloning, purification, and characterization of a cold-adapted lipase produced by Acinetobacter baumannii BD5. J. Microbiol. Biotechnol. 19, 128-135. doi:10.4014/jmb.0802.130
97. Payen, A., and Persoz, J. F. (1833). Memoir on diastase, the principal products of its reactions, and their applications to the industrial arts. Ann. Chim. Phys. 53, 73-92.
98. Phadtare, S. (2004). Recent developments in bacterial cold-shock response. Curr. Issues Mol. Biol. 6, 125-136.
99. Pulicherla, K. K., Kumar, P. S., Manideep, K., Rekha, V. P., Ghosh, M., and Sambasiva Rao, K. R. (2013). Statistical approach for the enhanced production of cold-active beta-galactosidase from Thalassospira frigidphilosprofundus: a novel marine psychrophile from deep waters of Bay of Bengal. Prep. Biochem. Biotechnol. 43, 766-780. doi:10.1080/10826068.2013.773341
100. Pulicherla, K. K., Mrinmoy, G., Kumar, S., and Sambasiva Rao, K. R. (2011). Psychrozymes-the next generation industrial enzymes. J. Mar. Sci. Res. Dev. 1, 102. doi:10.4172/2155-9910.1000102
101. Qin, Y., Huang, Z., and Liu, Z. (2014). A novel cold-active and salt-tolerant alpha-amylase from marine bacterium Zunongwangia profunda: molecular cloning, heterologous expression and biochemical characterization. Extremophiles 18, 271-281. doi:10.1007/s00792-013-0614-9
102. Reed, C. J., Lewis, H., Trejo, E., Winston, V., and Evilia, C. (2013). Protein adaptations in archaeal extremophiles. Archaea 2013, 373275. doi:10.1155/2013/373275
103. Reid, I. I., and Ricard, M. (2000). Pectinase in papermaking: solving retention problems in mechanical pulps bleached with hydrogen peroxide. Enzyme Microb. Technol. 26, 115-123. doi:10.1016/S0141-0229(99)00131-3
104. Rice, D. W., Yip, K. S., Stillman, T. J., Britton, K. L., Fuentes, A., Connerton, I., et al. (1996). Insights into the molecular basis of thermal stability from the structure determination of Pyrococcus furiosus glutamate dehydrogenase. FEMS Microbiol. Rev. 18, 105-117. doi:10.1111/j.1574-6976.1996.tb00230.x
105. Rina, M., Pozidis, C., Mavromatis, K., Tzanodaskalaki, M., Kokkinidis, M., and Bouriotis, V. (2000). Alkaline phosphatase from the Antarctic strain TAB5. Properties and psychrophilic adaptations. Eur. J. Biochem. 267, 1230-1238. doi:10.1046/j.1432-1327.2000.01127.x
106. Roohi, R., Kuddus, M., and Saima, S. (2013). Cold-active detergent-stable extracellular a-amylase from Bacillus cereus GA6: biochemical characteristics and its perspectives in laundry detergent formulation. J. Biochem. Technol. 4, 636-644.
107. Rothschild, L. J., and Mancinelli, R. L. (2001). Life in extreme environments. Nature 409, 1092-1101. doi:10.1038/35059215
108. Roychoudhury, A. N. (2004). Sulphate metabolism among thermophiles and hyperthermophiles in natural aquatic systems. Biochem. Soc. Trans. 32(Pt 2), 172-174. doi:10.1042/bst0320172
109. Rozzell, J. D. (1999). Commercial scale biocatalysis: myths and realities. Bioorg. Med. Chem. 7, 2253-2261. doi:10.1016/S0968-0896(99)00159-5
110. Rua, M. L., Atomi, H., Schmidt-Dannert, C., and Schmid, R. D. (1998). High-level expression of the thermoalkalophilic lipase from Bacillus thermocatenulatus in Escherichia coli. Appl. Microbiol. Biotechnol. 49, 405-410. doi:10.1007/s002530051190
111. Russell, N. J. (1997). Psychrophilic bacteria-molecular adaptations of membrane lipids. Comp. Biochem. Physiol. A Physiol. 118, 489-493. doi:10.1016/S0300-9629(97)87354-9
112. Satyanarayana, T., Noorwez, S. M., Kumar, S., Rao, J. L., Ezhilvannan, M., and Kaur, P. (2004). Development of an ideal starch saccharification process using amylolytic enzymes from thermophiles. Biochem. Soc. Trans. 32(Pt 2), 276-278. doi:10.1042/bst0320276
113. Shi, H., Zhang, Y., Li, X., Huang, Y., Wang, L., Wang, Y., et al. (2013). A novel highly thermostable xylanase stimulated by Ca2+ from Thermotoga thermarum: cloning, expression and characterization. Biotechnol. Biofuels 6, 26. doi:10.1186/1754-6834-6-26
114. Siddiqui, K. S., and Cavicchioli, R. (2006). Cold-adapted enzymes. Annu. Rev. Biochem. 75, 403-433. doi:10.1146/annurev.biochem.75.103004.142723
115. Stougaard, P., and Schmidt, M. (2010). Cold-Active Beta-Galactosidase, a Method of Producing Same and Use of Such Enzyme. Canadian Patent No 2751957 A1. Canadian Intellectual Property Office.
116. Sukumar, M. S., Jeyaseelan, A., Sivasankaran, T., Mohanraj, P., Mani, P., Sudhakar, G., et al. (2013). Production and partial characterization of extracellular glucose isomerase using thermophilic Bacillus sp. isolated from agricultural land. Biocatal. Agric. Biotechnol. 2, 45-49. doi:10.1016/j.bcab.2012.10.003
117. Swamy, M. V., Sai Ram, M., and Seenayya, G. (1994). β-amylase from Clostridium thermocellum SS8-a thermophilic, anaerobic, cellulolytic bacterium. Lett. Appl. Microbiol. 18, 301-304. doi:10.1111/j.1472-765X.1994.tb00875.x
118. Takai, K., Nakamura, K., Toki, T., Tsunogai, U., Miyazaki, M., Miyazaki, J., et al. (2008). Cell proliferation at 122 degrees C and isotopically heavy CH4 production by a hyperthermophilic methanogen under high-pressure cultivation. Proc. Natl. Acad. Sci. U.S.A. 105, 10949-10954. doi:10.1073/pnas.0712334105
119. Van de Voorde, I., Goiris, K., Syryn, E., Van den Bussche, C., and Aerts, G. (2014). Evaluation of the cold-active Pseudoalteromonas haloplanktis β-galactosidase enzyme for lactose hydrolysis in whey permeate as primary step of d-tagatose production. Process Biochem. 49, 2134-2140. doi:10.1016/j.procbio.2014.09.010
120. Vieille, C., Hess, J. M., Kelly, R. M., and Zeikus, J. G. (1995). xylA cloning and sequencing and biochemical characterization of xylose isomerase from Thermotoga neapolitana. Appl. Environ. Microbiol. 61, 1867-1875.
121. Virk, A. P., Sharma, P., and Capalash, N. (2012). Use of laccase in pulp and paper industry. Biotechnol. Prog. 28, 21-32. doi:10.1002/btpr.727
122. Wagner, M., Roger, A. J., Flax, J. L., Brusseau, G. A., and Stahl, D. A. (1998). Phylogeny of dissimilatory sulfite reductases supports an early origin of sulfate respiration. J. Bacteriol. 180, 2975-2982.
123. Wang, S. Y., Hu, W., Lin, X. Y., Wu, Z. H., and Li, Y. Z. (2012). A novel cold-active xylanase from the cellulolytic myxobacterium Sorangium cellulosum So9733-1: gene cloning, expression, and enzymatic characterization. Appl. Microbiol. Biotechnol. 93, 1503-1512. doi:10.1007/s00253-011-3480-3
124. Xu, F., Shin, W., Brown, S. H., Wahleithner, J. A., Sundaram, U. M., and Solomon, E. I. (1996). A study of a series of recombinant fungal laccases and bilirubin oxidase that exhibit significant differences in redox potential, substrate specificity, and stability. Biochim. Biophys. Acta. 1292, 303-311. doi:10.1016/0167-4838(95)00210-3
125. Xuezheng, L., Shuoshuo, C., Guoying, X., Shuai, W., and Ning, D. J. (2010). Cloning and heterologous expression of two cold-active lipases from the Antarctic bacterium psychrobacter sp. G. Polar Res. 29, 421-429. doi:10.1111/j.1751-8369.2010.00189.x
126. Zhang, S., Yang, J., Li, J., Mai, Z., Tian, X., and Yin, H. (2013). Marine Bacteria Cold-Adapted Protease and Encoded Gene and Application Thereof. International Patent No WO2013177834 A1.
127. Zheng, Z., Li, H., Li, L., and Shao, W. (2012). Biobleaching of wheat straw pulp with recombinant laccase from the hyperthermophilic Thermus thermophilus. Biotechnol. Lett. 34, 541-547. doi:10.1007/s10529-011-0796-0
128. Zhu, Y., Zhang, Z., Zhang, M., Mais, D. E., and Wang, M. W. (2010). High-throughput screening for bioactive components from traditional Chinese medicine. Comb. Chem. High Throughput Screen. 13, 837-848. doi:10.2174/138620710793360257