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Volumn 22, Issue 6, 2012, Pages 818-825

Immobilization of keratinolytic metalloprotease from Chryseobacterium sp. strain kr6 on glutaraldehyde-activated chitosan

Author keywords

Casein hydrolysis; Chitosan; Enzyme; Immobilization; Protease

Indexed keywords

ACETIC ACID; CHITOSAN; GLUTARALDEHYDE; METALLOPROTEINASE;

EID: 84861316086     PISSN: 10177825     EISSN: 17388872     Source Type: Journal    
DOI: 10.4014/jmb.1111.11048     Document Type: Article
Times cited : (15)

References (35)
  • 1
    • 0028883655 scopus 로고
    • Characterization of a keratinolytic serine proteinase from Streptomyces pactum DSM 40530
    • Böckle, B., B. Galunsky, and R. Müller. 1995. Characterization of a keratinolytic serine proteinase from Streptomyces pactum DSM 40530. Appl. Environ. Microbiol. 61: 3705-3710.
    • (1995) Appl. Environ. Microbiol , vol.61 , pp. 3705-3710
    • Böckle, B.1    Galunsky, B.2    Müller, R.3
  • 2
    • 77956170052 scopus 로고    scopus 로고
    • Heterofunctional supports for one-step purification, immobilization and stabilization of large-multimeric enzymes: Amino-glyoxyl versus amino-epoxy supports
    • Bolivar, J. M., C. Mateo, V. Grazu, A. V. Carrascosa, B. C. Pessela, and J. M. Guisan. 2010. Heterofunctional supports for one-step purification, immobilization and stabilization of large-multimeric enzymes: Amino-glyoxyl versus amino-epoxy supports. Process Biochem. 45: 1692 -1698.
    • (2010) Process Biochem , vol.45 , pp. 1692-1698
    • Bolivar, J.M.1    Mateo, C.2    Grazu, V.3    Carrascosa, A.V.4    Pessela, B.C.5    Guisan, J.M.6
  • 4
    • 17144381303 scopus 로고    scopus 로고
    • Hydrolysis of native proteins by a keratinolytic protease of Chryseobacterium sp
    • Brandelli, A. 2005. Hydrolysis of native proteins by a keratinolytic protease of Chryseobacterium sp. Ann. Microbiol. 55: 47-50.
    • (2005) Ann. Microbiol , vol.55 , pp. 47-50
    • Brandelli, A.1
  • 5
    • 48349145890 scopus 로고    scopus 로고
    • Bacterial keratinases: Useful enzymes for bioprocessing agricultural wastes and beyond
    • Brandelli, A. 2008. Bacterial keratinases: Useful enzymes for bioprocessing agricultural wastes and beyond. Food Bioprocess Technol. 1: 105-116.
    • (2008) Food Bioprocess Technol , vol.1 , pp. 105-116
    • Brandelli, A.1
  • 6
    • 76849100849 scopus 로고    scopus 로고
    • Biochemical features of microbial keratinases and their production and applications
    • Brandelli, A., D. J. Daroit, and A. Riffel. 2010. Biochemical features of microbial keratinases and their production and applications. Appl. Microbiol. Biotechnol. 85: 1735-1750.
    • (2010) Appl. Microbiol. Biotechnol , vol.85 , pp. 1735-1750
    • Brandelli, A.1    Daroit, D.J.2    Riffel, A.3
  • 8
    • 20444432723 scopus 로고    scopus 로고
    • Competitive ion-exchange adsorption of proteins: Competitive isotheims with controlled competitor concentration
    • Cano, T., N. D. Offringa, and L. D. Willson. 2005. Competitive ion-exchange adsorption of proteins: Competitive isotheims with controlled competitor concentration. J. Chromatogr. A 1079: 116-126.
    • (2005) J. Chromatogr. A , vol.1079 , pp. 116-126
    • Cano, T.1    Offringa, N.D.2    Willson, L.D.3
  • 9
    • 16244405562 scopus 로고    scopus 로고
    • Immobilised enzymes: Science or art
    • Cao, L. 2005. Immobilised enzymes: Science or art? Curr. Opin. Chem. Biol. 9: 217-226.
    • (2005) Curr. Opin. Chem. Biol , vol.9 , pp. 217-226
    • Cao, L.1
  • 10
    • 76849113294 scopus 로고    scopus 로고
    • Use of poultry byproduct for production of keratinolytic enzymes
    • Casarin, F., F. Cladera-Olivera, and A. Brandelli. 2008. Use of poultry byproduct for production of keratinolytic enzymes. Food Bioprocess Technol. 1: 301-305.
    • (2008) Food Bioprocess Technol , vol.1 , pp. 301-305
    • Casarin, F.1    Cladera-Olivera, F.2    Brandelli, A.3
  • 11
    • 0034071719 scopus 로고    scopus 로고
    • Immobilization of catalase on chitosan film
    • çetinus, S. A. and H. N. Oztop. 2000. Immobilization of catalase on chitosan film. Enzyme Microb. Technol. 26: 497-501
    • (2000) Enzyme Microb. Technol , vol.26 , pp. 497-501
    • Çetinus, S.A.1    Oztop, H.N.2
  • 12
    • 9944250922 scopus 로고    scopus 로고
    • Activities, stabilities, and reaction kinetics of three free and chitosan-clay composite immobilized enzymes
    • Chang, M. Y. and R. S. Juang. 2005. Activities, stabilities, and reaction kinetics of three free and chitosan-clay composite immobilized enzymes. Enzyme Microb. Technol. 36: 75-82.
    • (2005) Enzyme Microb. Technol , vol.36 , pp. 75-82
    • Chang, M.Y.1    Juang, R.S.2
  • 13
    • 3142688134 scopus 로고    scopus 로고
    • Bacteriocin production by Bacillus licheniformis strain P40 in cheese whey using response surface methodology
    • Cladera-Olivera, F., G R. Caron, and A. Brandelli. 2004. Bacteriocin production by Bacillus licheniformis strain P40 in cheese whey using response surface methodology. Biochem. Eng. J. 21: 53-58.
    • (2004) Biochem. Eng. J , vol.21 , pp. 53-58
    • Cladera-Olivera, F.1    Caron, G.R.2    Brandelli, A.3
  • 14
    • 63749119165 scopus 로고    scopus 로고
    • Optimal immobilization of β-galactosidase from Pea (PsBGAL) onto Sephadex and chitosan beads using surface methodology and its application
    • Dwevedi, A. and A. M. Kayastha. 2009. Optimal immobilization of β-galactosidase from Pea (PsBGAL) onto Sephadex and chitosan beads using surface methodology and its application. Bioresour. Technol. 100: 2667-2675.
    • (2009) Bioresour. Technol , vol.100 , pp. 2667-2675
    • Dwevedi, A.1    Kayastha, A.M.2
  • 15
    • 0347683371 scopus 로고    scopus 로고
    • Purification, characterization and immobilization of a keratinase from Aspergillus oryzae
    • Farag, A. M. and M. A. Hassan. 2004. Purification, characterization and immobilization of a keratinase from Aspergillus oryzae. Enzyme Microb. Technol. 34: 85-93.
    • (2004) Enzyme Microb. Technol , vol.34 , pp. 85-93
    • Farag, A.M.1    Hassan, M.A.2
  • 16
    • 78650818528 scopus 로고    scopus 로고
    • Control of protein immobilization: Coupling immobilization and site-directed mutagenesis to improve biocatalysis and biosensor perfoimance
    • Hernandez, K. and R. Fernandez-Lafuente. 2011. Control of protein immobilization: Coupling immobilization and site-directed mutagenesis to improve biocatalysis and biosensor perfoimance. Enzyme Microb. Technol. 48: 107-122.
    • (2011) Enzyme Microb. Technol , vol.48 , pp. 107-122
    • Hernandez, K.1    Fernandez-Lafuente, R.2
  • 17
    • 0035252643 scopus 로고    scopus 로고
    • Enzyme immobilization on nylon-optimization and the steps used to prevent enzyme leakage from the support
    • Isgrove, S. H., R. J. H. Williams, G W. Niven, and A. T. Andrews. 2001. Enzyme immobilization on nylon-optimization and the steps used to prevent enzyme leakage from the support. Enzme Microb. Technol. 28: 225 -232.
    • (2001) Enzme Microb. Technol , vol.28 , pp. 225-232
    • Isgrove, S.H.1    Williams, R.J.H.2    Niven, G.W.3    Andrews, A.T.4
  • 18
    • 0028384710 scopus 로고
    • Lipoprotein lipase immobilization onto porous chitosan beads
    • Itoyama, K., S. Tokura, and T. Hayashi. 1994. Lipoprotein lipase immobilization onto porous chitosan beads. Biotechnol. Progr. 10: 225 -229.
    • (1994) Biotechnol. Progr , vol.10 , pp. 225-229
    • Itoyama, K.1    Tokura, S.2    Hayashi, T.3
  • 19
    • 56049111888 scopus 로고    scopus 로고
    • Immobilization of alkaline serine endopeptidase from Bacillus licheniformis on SBA-15 and MCF by surface covalent binding
    • Kannan, K. and R. V. Jasra. 2009. Immobilization of alkaline serine endopeptidase from Bacillus licheniformis on SBA-15 and MCF by surface covalent binding. J. Mol. Catal. B Enzym. 56: 34-40.
    • (2009) J. Mol. Catal. B Enzym , vol.56 , pp. 34-40
    • Kannan, K.1    Jasra, R.V.2
  • 20
    • 67649188397 scopus 로고    scopus 로고
    • Polymer-assisted iron oxide magnetic nanoparticle immobilized keratinase
    • 225107
    • Konwarh, R., N. Karak, S. K. Rai, and A. K. Mukherjee. 2009. Polymer-assisted iron oxide magnetic nanoparticle immobilized keratinase. Nanotechnology 20: 225107.
    • (2009) Nanotechnology , vol.20
    • Konwarh, R.1    Karak, N.2    Rai, S.K.3    Mukherjee, A.K.4
  • 21
    • 3142763845 scopus 로고    scopus 로고
    • Applications of chitin- and chitosan-based materials for enzyme immobilizations: A review
    • Krajewska, B. 2004. Applications of chitin- and chitosan-based materials for enzyme immobilizations: A review. Enzyme Microb. Technol. 35: 126-139.
    • (2004) Enzyme Microb. Technol , vol.35 , pp. 126-139
    • Krajewska, B.1
  • 22
    • 63249111145 scopus 로고    scopus 로고
    • Immobilization of soybean (Glycine max) urease on alginate and chitosan beads showing improved stability: Analytical applications
    • Kumar, S., A. Dwevedi, and A. M. Kayastha. 2008. Immobilization of soybean (Glycine max) urease on alginate and chitosan beads showing improved stability: Analytical applications. J. Mol. Catal. B Enzym. 58: 138-145.
    • (2008) J. Mol. Catal. B Enzym , vol.58 , pp. 138-145
    • Kumar, S.1    Dwevedi, A.2    Kayastha, A.M.3
  • 25
    • 79952198974 scopus 로고    scopus 로고
    • Introduction to the field of enzyme immobilization and stabilization
    • Moehlenbrock, M. J. and S. D. Minteer. 2011. Introduction to the field of enzyme immobilization and stabilization. Methods Mol. Biol. 679: 1-7.
    • (2011) Methods Mol. Biol , vol.679 , pp. 1-7
    • Moehlenbrock, M.J.1    Minteer, S.D.2
  • 26
    • 34247866397 scopus 로고    scopus 로고
    • Lectin-immobilization strategies for affinity purification and separation of glycoconjugates
    • Monzo, A., G K. Bonn, and A. Guttman. 2007. Lectin-immobilization strategies for affinity purification and separation of glycoconjugates. Trends Anal. Chem. 26: 423-432.
    • (2007) Trends Anal. Chem , vol.26 , pp. 423-432
    • Monzo, A.1    Bonn, G.K.2    Guttman, A.3
  • 27
    • 0242500381 scopus 로고    scopus 로고
    • Characterization of a new keratinolytic bacterium that completely degrades native feather keratin
    • Riffel, A., F. S. Lucas, P. Heeb, and A. Brandelli. 2003. Characterization of a new keratinolytic bacterium that completely degrades native feather keratin. Arch. Microbiol. 179: 258-265.
    • (2003) Arch. Microbiol , vol.179 , pp. 258-265
    • Riffel, A.1    Lucas, F.S.2    Heeb, P.3    Brandelli, A.4
  • 28
    • 33846431239 scopus 로고    scopus 로고
    • Purification and characterization of a keratinolytic metalloprotease from Chryseobacterium sp. kr6
    • Riffel, A., A. Brandelli, C. M. Bellato, G H. M. F. Souza, M. N. Eberlin, and F. C. A. Tavares. 2007. Purification and characterization of a keratinolytic metalloprotease from Chryseobacterium sp. kr6. J. Biotechnol. 128: 693-703.
    • (2007) J. Biotechnol , vol.128 , pp. 693-703
    • Riffel, A.1    Brandelli, A.2    Bellato, C.M.3    Souza, G.H.M.F.4    Eberlin, M.N.5    Tavares, F.C.A.6
  • 29
    • 79551490917 scopus 로고    scopus 로고
    • Nutritional regulation of protease production by the feather-degrading bacterium Chryseobacterium sp. kr6
    • Riffel, A., D. J. Daroit, and A. Brandelli. 2010. Nutritional regulation of protease production by the feather-degrading bacterium Chryseobacterium sp. kr6. New Biotechnol. 28: 153-157.
    • (2010) New Biotechnol , vol.28 , pp. 153-157
    • Riffel, A.1    Daroit, D.J.2    Brandelli, A.3
  • 30
    • 77952876667 scopus 로고    scopus 로고
    • Thermodynamics and kinetics of thermal inactivation of a keratinase from Chryseobacterium sp. strain kr6
    • Silveira, S. T., F. Casarin, S. Gemelli, and A. Brandelli. 2010. Thermodynamics and kinetics of thermal inactivation of a keratinase from Chryseobacterium sp. strain kr6. Appl. Biochem. Biotechnol. 162: 548-560.
    • (2010) Appl. Biochem. Biotechnol , vol.162 , pp. 548-560
    • Silveira, S.T.1    Casarin, F.2    Gemelli, S.3    Brandelli, A.4
  • 31
    • 79957982614 scopus 로고    scopus 로고
    • Glutaraldehyde-activated chitosan matrix for immobilization of a novel cysteine protease, Procerain B
    • Singh, A. N., S. Singh, N. Suthar, and C. K. Dubey. 2011. Glutaraldehyde-activated chitosan matrix for immobilization of a novel cysteine protease, Procerain B. J. Agric. Food Chem. 59: 6256-6262.
    • (2011) J. Agric. Food Chem , vol.59 , pp. 6256-6262
    • Singh, A.N.1    Singh, S.2    Suthar, N.3    Dubey, C.K.4
  • 32
    • 33645231083 scopus 로고    scopus 로고
    • Characterizations of immobilized neutral proteinase on chitosan nano-particles
    • Tang, Z. X., J. Q. Qian, and L. E. Shi. 2006. Characterizations of immobilized neutral proteinase on chitosan nano-particles. Process Biochem. 41: 1193-1197.
    • (2006) Process Biochem , vol.41 , pp. 1193-1197
    • Tang, Z.X.1    Qian, J.Q.2    Shi, L.E.3
  • 33
    • 0038058903 scopus 로고    scopus 로고
    • Production and characterization of bio-immobilized keratinase in proteolysis and keratinolysis
    • Wang, J. J., H. E. Swaisgood, and J. C. H. Shih. 2003. Production and characterization of bio-immobilized keratinase in proteolysis and keratinolysis. Enzyme Microb. Technol. 32: 812-819.
    • (2003) Enzyme Microb. Technol , vol.32 , pp. 812-819
    • Wang, J.J.1    Swaisgood, H.E.2    Shih, J.C.H.3
  • 34
    • 43049085901 scopus 로고    scopus 로고
    • Purification and characterization of three novel keratinolytic metalloproteases from Chryseobacterium indologenes TKU014 in a shrimp shell powder medium
    • Wang, S. L., W. T. Hsu, T. W. Liang, Y. H. Yen, and C. L. Wang. 2008. Purification and characterization of three novel keratinolytic metalloproteases from Chryseobacterium indologenes TKU014 in a shrimp shell powder medium. Bioresour Technol. 99: 5679-5686.
    • (2008) Bioresour Technol , vol.99 , pp. 5679-5686
    • Wang, S.L.1    Hsu, W.T.2    Liang, T.W.3    Yen, Y.H.4    Wang, C.L.5
  • 35
    • 77957958242 scopus 로고    scopus 로고
    • Control of protein immobilization: Coupling immobilization and site-directed mutagenesis to improve biocatalysis and biosensor perfoimance
    • Wang, M., W. Qi, Q. Yu, R. Su, and Z. He. 2010. Control of protein immobilization: Coupling immobilization and site-directed mutagenesis to improve biocatalysis and biosensor perfoimance. Biochem. Eng. J. 52: 168-174.
    • (2010) Biochem. Eng. J , vol.52 , pp. 168-174
    • Wang, M.1    Qi, W.2    Yu, Q.3    Su, R.4    He, Z.5


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