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Volumn 9, Issue 42, 2010, Pages 7020-7025

Some applications of thermophiles and their enzymes for protein processing

Author keywords

Keratinases; Proteases; Thermophiles; Thermozymes

Indexed keywords

KERATINASE; MEMBRANE PROTEIN; MICROBIAL ENZYME; PRION PROTEIN; PROTEINASE; SERINE PROTEINASE; THERMOZYME; UNCLASSIFIED DRUG;

EID: 78049461379     PISSN: 16845315     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (35)

References (74)
  • 3
    • 13844298001 scopus 로고    scopus 로고
    • Enzymatic hydrolysis of atlantic cod (Gadus morhua) visceria
    • Aspamo SI, Horn SJ, Eijsink VGH (2005). Enzymatic hydrolysis of atlantic cod (Gadus morhua) visceria. Process Biochem. 40: 1957-1966.
    • (2005) Process Biochem , vol.40 , pp. 1957-1966
    • Aspamo, S.I.1    Horn, S.J.2    Eijsink, V.G.H.3
  • 5
    • 0032716420 scopus 로고    scopus 로고
    • Thermostable alkaline protease from Bacillus brevis and its characterization as a laundry additive
    • Banerjee V, Saani K, Azmi W, Soni R (1999). Thermostable alkaline protease from Bacillus brevis and its characterization as a laundry additive. Proc. Biochem. 35: 213-219.
    • (1999) Proc. Biochem , vol.35 , pp. 213-219
    • Banerjee, V.1    Saani, K.2    Azmi, W.3    Soni, R.4
  • 8
    • 78049454929 scopus 로고    scopus 로고
    • Characterization of a feather degrading by Bacillus amyloliquefaciens protease: A new strain
    • Cortezi M, Contiero J, De Lima CJB, Lovaglio RB, Monti R (2008). Characterization of a feather degrading by Bacillus amyloliquefaciens protease: A new strain. World J. Agric. Sci. 4: 648-656.
    • (2008) World J. Agric. Sci , vol.4 , pp. 648-656
    • Cortezi, M.1    Contiero, J.2    de Lima, C.J.B.3    Lovaglio, R.B.4    Monti, R.5
  • 9
    • 0021983374 scopus 로고
    • Thermophilic proteases: Properties and applications
    • Covan D, Daniel R, Morgan H (1985). Thermophilic proteases: properties and applications. Trends Biotechnol. 3: 68-72.
    • (1985) Trends Biotechnol , vol.3 , pp. 68-72
    • Covan, D.1    Daniel, R.2    Morgan, H.3
  • 10
    • 0031280508 scopus 로고    scopus 로고
    • Thermophilic proteins: Stability and function in aqueous and organic solvents
    • Covan DA (1997). Thermophilic proteins: stability and function in aqueous and organic solvents. Comp. Biochem. Physiol., Part A: Mol. Integr. Physiol. 118: 429-438.
    • (1997) Comp. Biochem. Physiol., Part A: Mol. Integr. Physiol , vol.118 , pp. 429-438
    • Covan, D.A.1
  • 12
    • 0035821309 scopus 로고    scopus 로고
    • High isolate yields in thermolysin catalyzed synthesis of Z-L-aspartyl-L-phenylalanine methyl ester in toluene at controlled water activity
    • De Martin L, Ebert C, Gardossi L, Linda P (2001). High isolate yields in thermolysin catalyzed synthesis of Z-L-aspartyl-L-phenylalanine methyl ester in toluene at controlled water activity. Tetrahedron Lett. 42: 3395-3397.
    • (2001) Tetrahedron Lett , vol.42 , pp. 3395-3397
    • de Martin, L.1    Ebert, C.2    Gardossi, L.3    Linda, P.4
  • 13
    • 0027974424 scopus 로고
    • A thermostable alkaline- active keratinolytic proteinases from Chryzosporium keratinophilum
    • Dozie INS, Okeke CN, Unaeze NC (1994). A thermostable alkaline- active keratinolytic proteinases from Chryzosporium keratinophilum. World J. Microbiol. Biotechnol. 10: 563-567.
    • (1994) World J. Microbiol. Biotechnol , vol.10 , pp. 563-567
    • Dozie, I.N.S.1    Okeke, C.N.2    Unaeze, N.C.3
  • 14
    • 0034913744 scopus 로고    scopus 로고
    • Biotechnological uses of archaeal enzymes
    • Eichler J (2001). Biotechnological uses of archaeal enzymes. Biotechnol. Adv. 19: 261-278.
    • (2001) Biotechnol. Adv , vol.19 , pp. 261-278
    • Eichler, J.1
  • 15
    • 2542451914 scopus 로고    scopus 로고
    • Preferred amino acids and thermostability
    • Farias ST, Bonato MC (2003). Preferred amino acids and thermostability. Genet. Mol. Res. 2: 383-393.
    • (2003) Genet. Mol. Res , vol.2 , pp. 383-393
    • Farias, S.T.1    Bonato, M.C.2
  • 16
    • 0029948243 scopus 로고    scopus 로고
    • Thermostable alkaline protease of Bacillus licheniformis MIR 29, isolation, production and characterization
    • Ferrero M, Castro G, Abate M, Baigori M, Sinerz F (1996). Thermostable alkaline protease of Bacillus licheniformis MIR 29, isolation, production and characterization. Appl. Microbiol. Technol. 45: 327-332.
    • (1996) Appl. Microbiol. Technol , vol.45 , pp. 327-332
    • Ferrero, M.1    Castro, G.2    Abate, M.3    Baigori, M.4    Sinerz, F.5
  • 17
    • 0029659518 scopus 로고    scopus 로고
    • Keratin degradation by Fervidobacterium pennavorans, a novel thermophilic anaerobic species of the order Thermatogales
    • Fredrich A, Antrakian G (1996). Keratin degradation by Fervidobacterium pennavorans, a novel thermophilic anaerobic species of the order Thermatogales. Appl. Environ. Microbiol. 62: 2875-2882.
    • (1996) Appl. Environ. Microbiol , vol.62 , pp. 2875-2882
    • Fredrich, A.1    Antrakian, G.2
  • 18
    • 0036968065 scopus 로고    scopus 로고
    • Extremophiles: Developments of their specialxfunctions and potential resources
    • Fujiwara S (2002). Extremophiles: Developments of their specialxfunctions and potential resources. J. Biosci. Bioeng. 94: 518-525.
    • (2002) J. Biosci. Bioeng , vol.94 , pp. 518-525
    • Fujiwara, S.1
  • 19
    • 0035876479 scopus 로고    scopus 로고
    • Protein surface amino acid compositions distinctively differ between thermophilic and mesophilic bacteria
    • Fukuchi S Nishikawa K (2001). Protein surface amino acid compositions distinctively differ between thermophilic and mesophilic bacteria. J. Mol. Biol. 309: 835-843.
    • (2001) J. Mol. Biol , vol.309 , pp. 835-843
    • Fukuchi, S.1    Nishikawa, K.2
  • 23
    • 33745202363 scopus 로고    scopus 로고
    • A protease stable in organic solvents from solvent tolerant strain Pseudomonas aeruginosa
    • Gupta A, Khare SK (2006). A protease stable in organic solvents from solvent tolerant strain Pseudomonas aeruginosa. Bioresour. Technol. 97: 1788-1793.
    • (2006) Bioresour. Technol , vol.97 , pp. 1788-1793
    • Gupta, A.1    Khare, S.K.2
  • 24
    • 0001785135 scopus 로고
    • Thermostabilization of proteins
    • Gupta MN (1991). Thermostabilization of proteins. Biotechnol. Appl. Biochem. 14:1-11.
    • (1991) Biotechnol. Appl. Biochem , vol.14 , pp. 1-11
    • Gupta, M.N.1
  • 25
    • 32644435175 scopus 로고    scopus 로고
    • Microbial keratinases and their perspective applications
    • Gupta R, Ramnani P (2006). Microbial keratinases and their perspective applications. Appl. Microbiol. Biotechnol. 70: 21-33.
    • (2006) Appl. Microbiol. Biotechnol , vol.70 , pp. 21-33
    • Gupta, R.1    Ramnani, P.2
  • 26
    • 0037411739 scopus 로고    scopus 로고
    • Developments in industrially important thermostable enzymes
    • Haaki GD, Rakshit SK (2003). Developments in industrially important thermostable enzymes. Bioresour. Technol. 89: 17-23.
    • (2003) Bioresour. Technol , vol.89 , pp. 17-23
    • Haaki, G.D.1    Rakshit, S.K.2
  • 27
    • 0000620268 scopus 로고    scopus 로고
    • An extremely thermostable serine protease from hyperthermophilic archaeum Desulfurococcus strain, isolated from deep sea hydrothermal vent
    • Hanazawa S, Hoaki T, Jannasch H, Maruyama T (1996). An extremely thermostable serine protease from hyperthermophilic archaeum Desulfurococcus strain, isolated from deep sea hydrothermal vent. J. Mar. Biotechnol. 4: 121-126.
    • (1996) J. Mar. Biotechnol , vol.4 , pp. 121-126
    • Hanazawa, S.1    Hoaki, T.2    Jannasch, H.3    Maruyama, T.4
  • 28
    • 0344061526 scopus 로고    scopus 로고
    • Hyperthermophiles and their possible potential in biotechnology
    • Huber H, Stetter KO (1998). Hyperthermophiles and their possible potential in biotechnology. J. Biotechnol. 64: 39-52.
    • (1998) J. Biotechnol , vol.64 , pp. 39-52
    • Huber, H.1    Stetter, K.O.2
  • 30
    • 24944561061 scopus 로고    scopus 로고
    • Prion diseases
    • Johnson RT (2005). Prion diseases. Lancet Neurol. 4: 635-642.
    • (2005) Lancet Neurol , vol.4 , pp. 635-642
    • Johnson, R.T.1
  • 31
    • 0026028265 scopus 로고
    • Properties of extremely thermostable proteases from anaerobic hyperthermophilic bacteria
    • Klingberg M, Hashawa F Antranikian G (1991). Properties of extremely thermostable proteases from anaerobic hyperthermophilic bacteria. Appl. Microbiol. Biotechnol. 34: 715-719.
    • (1991) Appl. Microbiol. Biotechnol , vol.34 , pp. 715-719
    • Klingberg, M.1    Hashawa, F.2    Antranikian, G.3
  • 32
    • 69449091329 scopus 로고    scopus 로고
    • Desulfurococcus kamchatkensis sp.nov. a novel hyperthermophilic protein-degrading archaeon isolated from Kamchatka hot spring
    • Kublanov IV, Bidjeva SK, Mardanov AV, Bonch-Osmolovskaya EA (2009). Desulfurococcus kamchatkensis sp.nov. a novel hyperthermophilic protein-degrading archaeon isolated from Kamchatka hot spring. Int. J. Syst. Evol. Microbiol. 59: 1743-1747.
    • (2009) Int. J. Syst. Evol. Microbiol , vol.59 , pp. 1743-1747
    • Kublanov, I.V.1    Bidjeva, S.K.2    Mardanov, A.V.3    Bonch-Osmolovskaya, E.A.4
  • 33
    • 0034855858 scopus 로고    scopus 로고
    • How do thermophilic proteins deal with heat
    • Kumar S, Nussinov R (2001). How do thermophilic proteins deal with heat. Cell Mol. Life Sci. 58: 1216-1233.
    • (2001) Cell Mol. Life Sci , vol.58 , pp. 1216-1233
    • Kumar, S.1    Nussinov, R.2
  • 34
    • 0028526562 scopus 로고
    • Enzymatic production of protein hydrolysates for food use
    • Lahl WJ, Braun SD (1994). Enzymatic production of protein hydrolysates for food use. Food Technol. 48: 68-71.
    • (1994) Food Technol , vol.48 , pp. 68-71
    • Lahl, W.J.1    Braun, S.D.2
  • 35
    • 0346882925 scopus 로고    scopus 로고
    • Enzymatic degradation of prion protein in brain steam from infected cattle and sheep
    • Langeveld JP, Wang JJ, Van De Wiel DF, Shih JC (2003). Enzymatic degradation of prion protein in brain steam from infected cattle and sheep. J. Infect. Dis. 188: 1782-1789.
    • (2003) J. Infect. Dis , vol.188 , pp. 1782-1789
    • Langeveld, J.P.1    Wang, J.J.2    van de Wiel, D.F.3    Shih, J.C.4
  • 36
    • 0343854374 scopus 로고
    • Thermophilic enzymes and their biotechnological potential
    • Lasa I, Berenguer J (1993). Thermophilic enzymes and their biotechnological potential. Microbiologia SEM, 9: 77-89.
    • (1993) Microbiologia SEM , vol.9 , pp. 77-89
    • Lasa, I.1    Berenguer, J.2
  • 39
    • 62949235842 scopus 로고    scopus 로고
    • Sustainable and practical degradation of intact chicken feathers by cultivating a newly isolated thermophilic Meiothermus ruber H328
    • Matsui T, Yamada Y, Mitsuya H, Shigeri Y, Yoshida Y, Saito Y, Matsui H, Watanabe K (2009). Sustainable and practical degradation of intact chicken feathers by cultivating a newly isolated thermophilic Meiothermus ruber H328. Appl. Microbiol. Biotechnol. 82: 941-950.
    • (2009) Appl. Microbiol. Biotechnol , vol.82 , pp. 941-950
    • Matsui, T.1    Yamada, Y.2    Mitsuya, H.3    Shigeri, Y.4    Yoshida, Y.5    Saito, Y.6    Matsui, H.7    Watanabe, K.8
  • 40
    • 20644433074 scopus 로고    scopus 로고
    • Two oligopeptidase-like Pz peptidases produced by a collagen-degrading thermophile Geobacillus collagenovorans MO-1
    • Miytake R, Shigeri Y, Tatsu Y, Yumoto N, Umekawa M, Tsujimoto Y, Matsui H, Watanabe K (2005). Two oligopeptidase-like Pz peptidases produced by a collagen-degrading thermophile Geobacillus collagenovorans MO-1. J. Bacteriol. 187: 4140-4148.
    • (2005) J. Bacteriol , vol.187 , pp. 4140-4148
    • Miytake, R.1    Shigeri, Y.2    Tatsu, Y.3    Yumoto, N.4    Umekawa, M.5    Tsujimoto, Y.6    Matsui, H.7    Watanabe, K.8
  • 41
    • 26244468929 scopus 로고    scopus 로고
    • Fractionation and enzymatic hydrolysis of soluble proteins present in waste from soy processing
    • Moure A, Dominiguez H, Parajo C (2005). Fractionation and enzymatic hydrolysis of soluble proteins present in waste from soy processing. J. Agric. Food Chem. 53: 7600-7608.
    • (2005) J. Agric. Food Chem , vol.53 , pp. 7600-7608
    • Moure, A.1    Dominiguez, H.2    Parajo, C.3
  • 42
    • 0027572338 scopus 로고
    • Mechanism-based strategies for protein thermostabilization
    • Mozhaev V (1993). Mechanism-based strategies for protein thermostabilization. Trends Biotechnol. 11: 88-95.
    • (1993) Trends Biotechnol , vol.11 , pp. 88-95
    • Mozhaev, V.1
  • 43
  • 45
    • 0032499796 scopus 로고    scopus 로고
    • Collagen-binding growth factors: Production and characterization of functional fusion proteins having a collagen-binding domain
    • Nishi N, Matsushita O, Yuube K, Miyanaka H, Okabe A, Wada F (1998). Collagen-binding growth factors: production and characterization of functional fusion proteins having a collagen-binding domain. Proc. Natl. Acad. Sci. USA, 95: 7018-7023.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 7018-7023
    • Nishi, N.1    Matsushita, O.2    Yuube, K.3    Miyanaka, H.4    Okabe, A.5    Wada, F.6
  • 46
    • 0034789606 scopus 로고    scopus 로고
    • A thermostable collagenolytic protease with a very large molecular mass produced by thermophilic Bacillus sp. strain MO-1
    • Okamoto M, Yonejima Y, Tsujimoto Y, Suzuki Y, Watanabe K (2001). A thermostable collagenolytic protease with a very large molecular mass produced by thermophilic Bacillus sp. strain MO-1. Appl. Microbiol. Biotechnol. 57: 103-108.
    • (2001) Appl. Microbiol. Biotechnol , vol.57 , pp. 103-108
    • Okamoto, M.1    Yonejima, Y.2    Tsujimoto, Y.3    Suzuki, Y.4    Watanabe, K.5
  • 48
    • 0031657562 scopus 로고    scopus 로고
    • Hard α-keratin intermediate filament chains: Substructure of the N- and C-terminal domains and the predicted structure and function of the C-terminal domains of type I and type II chains
    • Parry DAD, North ACT (1998). Hard α-keratin intermediate filament chains: substructure of the N- and C-terminal domains and the predicted structure and function of the C-terminal domains of type I and type II chains. J. Struct. Biol. 122: 279-290.
    • (1998) J. Struct. Biol , vol.122 , pp. 279-290
    • Parry, D.A.D.1    North, A.C.T.2
  • 49
    • 0034943846 scopus 로고    scopus 로고
    • Prion protein diversity and disease in the transmissible spongiform encephalopathies
    • Priola SA (2001). Prion protein diversity and disease in the transmissible spongiform encephalopathies. Adv. Protein Chem. 57: 1-27.
    • (2001) Adv. Protein Chem , vol.57 , pp. 1-27
    • Priola, S.A.1
  • 50
    • 0028353748 scopus 로고
    • Purification and characterization of a heat stable protease from Bacillus stearothermophilus F-1
    • Rahman R, Razak C, Ampon K, Basri M,Yunus W, Salleh A (1994). Purification and characterization of a heat stable protease from Bacillus stearothermophilus F-1. Appl. Microbiol. Biotechnol. 40: 822-827.
    • (1994) Appl. Microbiol. Biotechnol , vol.40 , pp. 822-827
    • Rahman, R.1    Razak, C.2    Ampon, K.3    Basri, M.4    Yunus, W.5    Salleh, A.6
  • 51
    • 0642373729 scopus 로고    scopus 로고
    • Exopeptidases and their application to reduce bitterness in food: A review
    • Raksakulthai R, Haard NF (2003). Exopeptidases and their application to reduce bitterness in food: a review. Crit. Rev. Food Sci. Nutr. 43: 401-445.
    • (2003) Crit. Rev. Food Sci. Nutr , vol.43 , pp. 401-445
    • Raksakulthai, R.1    Haard, N.F.2
  • 52
    • 0031686839 scopus 로고    scopus 로고
    • Molecular and biotechnological aspects of microbial proteases. Microbiol
    • Rao MB, Tanksale AM, Ghatge MS, Deshpande VV (1998). Molecular and biotechnological aspects of microbial proteases. Microbiol. Mol. Biol. Rev. 62: 597-635.
    • (1998) Mol. Biol. Rev , vol.62 , pp. 597-635
    • Rao, M.B.1    Tanksale, A.M.2    Ghatge, M.S.3    Deshpande, V.V.4
  • 53
    • 0035748508 scopus 로고    scopus 로고
    • Isolation of Thermoanaerobacter keratinophilus sp. nov., a novel thermophilic, anaerobic bacterium with keratinolytic activity
    • Riessen S, Antranikian G (2001). Isolation of Thermoanaerobacter keratinophilus sp. nov., a novel thermophilic, anaerobic bacterium with keratinolytic activity. Extremophile, 5: 399-408.
    • (2001) Extremophile , vol.5 , pp. 399-408
    • Riessen, S.1    Antranikian, G.2
  • 55
    • 0035931866 scopus 로고    scopus 로고
    • Life in extreme environments
    • Rothschild L, Manicineli R (2001). Life in extreme environments. Nature, 409: 1092-1101.
    • (2001) Nature , vol.409 , pp. 1092-1101
    • Rothschild, L.1    Manicineli, R.2
  • 56
    • 0037021413 scopus 로고    scopus 로고
    • Thermostability of membrane protein helix-helix interaction elucidated by statistical analysis
    • Schneider D, Liu Y, Gerstein M, Engelmann DM (2002). Thermostability of membrane protein helix-helix interaction elucidated by statistical analysis. FEBS Lett. 532: 231-236.
    • (2002) FEBS Lett , vol.532 , pp. 231-236
    • Schneider, D.1    Liu, Y.2    Gerstein, M.3    Engelmann, D.M.4
  • 57
    • 0033199021 scopus 로고    scopus 로고
    • Biocatalysis in organic media using enzymes from extremophiles
    • Sellek GA, Chaudhuri JB (1998). Biocatalysis in organic media using enzymes from extremophiles. Enzymes Microb. Technol. 25: 471-482.
    • (1998) Enzymes Microb. Technol , vol.25 , pp. 471-482
    • Sellek, G.A.1    Chaudhuri, J.B.2
  • 58
    • 0035681828 scopus 로고    scopus 로고
    • Conformational stability of a hyperthermophilic proteins in various conditions for denaturation
    • Shiraki K, Fujiwara S, Imanaka T, Takagi M (2001). Conformational stability of a hyperthermophilic proteins in various conditions for denaturation. Electrochemistry, 69: 949-952.
    • (2001) Electrochemistry , vol.69 , pp. 949-952
    • Shiraki, K.1    Fujiwara, S.2    Imanaka, T.3    Takagi, M.4
  • 59
    • 0034825542 scopus 로고    scopus 로고
    • Comparative analyses of the conformational stability of a hyperthermophilic protein and its mesophilic counterparts
    • Shiraki K, Nishikori S, Fujiwara S, Hashimoto H, Kai Y, Takagi M, Imanaka T (2001). Comparative analyses of the conformational stability of a hyperthermophilic protein and its mesophilic counterparts. Eur. J. Biochem. 268: 4144-4150.
    • (2001) Eur. J. Biochem , vol.268 , pp. 4144-4150
    • Shiraki, K.1    Nishikori, S.2    Fujiwara, S.3    Hashimoto, H.4    Kai, Y.5    Takagi, M.6    Imanaka, T.7
  • 60
    • 0033066726 scopus 로고    scopus 로고
    • Extremophiles and their adaptation to hot environments
    • Stetter K (1999). Extremophiles and their adaptation to hot environments. FEBS Lett. 452: 22-25.
    • (1999) FEBS Lett , vol.452 , pp. 22-25
    • Stetter, K.1
  • 61
    • 33749245479 scopus 로고    scopus 로고
    • Decomposition of extremely hard-to-degrade animal proteins by thermophilic bacteria
    • Suzuki Y, Tsujimoto Y, Matsui H, Watanabe K (2006). Decomposition of extremely hard-to-degrade animal proteins by thermophilic bacteria. J. Biosci. Bioeng. 102: 73-81.
    • (2006) J. Biosci. Bioeng , vol.102 , pp. 73-81
    • Suzuki, Y.1    Tsujimoto, Y.2    Matsui, H.3    Watanabe, K.4
  • 62
    • 80053477170 scopus 로고    scopus 로고
    • Thermostable enzymes in food processing
    • Enzymes as Additives or Processing Aids, Research Signpost, Kerala
    • Synowiecki J (2008). Thermostable enzymes in food processing, in Recent Research Developments in Food Biotechnology. Enzymes as Additives or Processing Aids, Research Signpost, Kerala.
    • (2008) Recent Research Developments In Food Biotechnology
    • Synowiecki, J.1
  • 63
    • 0001322051 scopus 로고
    • Degradation of human hair by a thermostable alkaline protease from alkalophilic Bacillus sp. No. AH-101
    • Takami H, Nakamura S, Aono R, Horikoshi K (1992). Degradation of human hair by a thermostable alkaline protease from alkalophilic Bacillus sp. No. AH-101. Biosci. Biotechnol. Biochem. 56: 1667-1669.
    • (1992) Biosci. Biotechnol. Biochem , vol.56 , pp. 1667-1669
    • Takami, H.1    Nakamura, S.2    Aono, R.3    Horikoshi, K.4
  • 64
    • 0033538553 scopus 로고    scopus 로고
    • Transproteomic evidence of a loop- deletion mechanism for enhancing protein thermostability
    • Thompson MJ, Eisenberg D (1999). Transproteomic evidence of a loop- deletion mechanism for enhancing protein thermostability. J. Mol. Biol. 290: 595-604.
    • (1999) J. Mol. Biol , vol.290 , pp. 595-604
    • Thompson, M.J.1    Eisenberg, D.2
  • 65
    • 38149128080 scopus 로고    scopus 로고
    • Protein thermostability in archaea and eubacteria
    • Trivedi S, Gehlot HS, Rao SR (2006). Protein thermostability in archaea and eubacteria. Genet. Mol. Res. 5: 816-827.
    • (2006) Genet. Mol. Res , vol.5 , pp. 816-827
    • Trivedi, S.1    Gehlot, H.S.2    Rao, S.R.3
  • 68
    • 0035098779 scopus 로고    scopus 로고
    • Hyperthermophilic enzymes: Sources, uses, and molecular mechanisms for thermostability
    • Vieille C, Zeikus GJ (2001). Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability. Microbiol. Mol. Biol. Rev. 65: 1-43.
    • (2001) Microbiol. Mol. Biol. Rev , vol.65 , pp. 1-43
    • Vieille, C.1    Zeikus, G.J.2
  • 69
    • 0031580199 scopus 로고    scopus 로고
    • Protein thermal stability, hydrogen bonds, and ion-pairs
    • Voght G, Woell S, Argos P (1997). Protein thermal stability, hydrogen bonds, and ion-pairs. J. Mol. Biol. 269: 631-643.
    • (1997) J. Mol. Biol , vol.269 , pp. 631-643
    • Voght, G.1    Woell, S.2    Argos, P.3
  • 70
    • 33646567763 scopus 로고    scopus 로고
    • Production of a surfactans-and solvent-stable alkaliphilic protease by bioconversion of shrimp shell wastes fermented by Bacillus subtilis
    • Wang SI, Yeh PY (2006). Production of a surfactans-and solvent-stable alkaliphilic protease by bioconversion of shrimp shell wastes fermented by Bacillus subtilis. Process Biochem. 41: 1545-1552.
    • (2006) Process Biochem , vol.41 , pp. 1545-1552
    • Wang, S.I.1    Yeh, P.Y.2
  • 71
    • 1242292972 scopus 로고    scopus 로고
    • Collagenolytic proteases from bacteria
    • Watanabe K (2004). Collagenolytic proteases from bacteria. Appl. Microbiol. Biotechnol. 63: 520-526.
    • (2004) Appl. Microbiol. Biotechnol , vol.63 , pp. 520-526
    • Watanabe, K.1
  • 72
    • 70349504348 scopus 로고    scopus 로고
    • Isolation and characterization of a new keratinolytic bacterium that exhibits significant feather-degrading capability
    • Xu B, Zhong Q, Tang X, Yang Y, Huang Z (2009). Isolation and characterization of a new keratinolytic bacterium that exhibits significant feather-degrading capability. Afr. J. Biotechnol. 8: 4590-4596.
    • (2009) Afr. J. Biotechnol , vol.8 , pp. 4590-4596
    • Xu, B.1    Zhong, Q.2    Tang, X.3    Yang, Y.4    Huang, Z.5
  • 73
    • 0032142867 scopus 로고    scopus 로고
    • Thermozymes: Biotechnology and structure-function relationships
    • Zeikus GJ, Vieille C, Savchenko A (1998). Thermozymes: biotechnology and structure-function relationships. Extremophiles, 2: 179-183.
    • (1998) Extremophiles , vol.2 , pp. 179-183
    • Zeikus, G.J.1    Vieille, C.2    Savchenko, A.3
  • 74
    • 67649659822 scopus 로고    scopus 로고
    • Isolation and purification of alkaline keratinase from Bacillus sp. 50-3
    • Zhang B, Sun Z, Jiang DD, Niu TG (2009). Isolation and purification of alkaline keratinase from Bacillus sp. 50-3. Afr. J. Biotechnol. 8: 2598-2603.
    • (2009) Afr. J. Biotechnol , vol.8 , pp. 2598-2603
    • Zhang, B.1    Sun, Z.2    Jiang, D.D.3    Niu, T.G.4


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