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Volumn 48, Issue 12, 2013, Pages 1952-1963

Biodegradation of feather keratin with a PEGylated protease of Chryseobacterium gleum

Author keywords

Covalent modification; Improved stability; Keratinolytic protease; Non immunogenic protein; Polyethylene glycol; Reusability

Indexed keywords

CHRYSEOBACTERIUM; COVALENT ATTACHMENT; COVALENT MODIFICATIONS; FEATHER DEGRADATION; KERATINOLYTIC PROTEASE; MODIFIED ENZYMES; SOLVENT STABILITY; UV-VIS SPECTROSCOPY;

EID: 84888199516     PISSN: 13595113     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.procbio.2013.09.011     Document Type: Article
Times cited : (12)

References (38)
  • 1
    • 76849100849 scopus 로고    scopus 로고
    • Biochemical features of microbial keratinases and their production and applications
    • A. Brandelli, D.J. Daroit, and A. Riffel Biochemical features of microbial keratinases and their production and applications Appl Microbiol Biotechnol 85 2010 1735 1750
    • (2010) Appl Microbiol Biotechnol , vol.85 , pp. 1735-1750
    • Brandelli, A.1    Daroit, D.J.2    Riffel, A.3
  • 2
    • 0037124473 scopus 로고    scopus 로고
    • Introduction and overview of peptide and protein pegylation
    • F.M. Veronese, and J.M. Harris Introduction and overview of peptide and protein pegylation Adv Drug Deliv Rev 54 4 2002 453 456
    • (2002) Adv Drug Deliv Rev , vol.54 , Issue.4 , pp. 453-456
    • Veronese, F.M.1    Harris, J.M.2
  • 3
    • 0017701219 scopus 로고
    • Alteration of immunological properties of bovine serum albumin by covalent attachment of polyethylene glycol
    • A. Abuchowski, T.V. Es, N.C. Palczuk, and F.F. Davis Alteration of immunological properties of bovine serum albumin by covalent attachment of polyethylene glycol J Biol Chem 252 1977 3578 3581
    • (1977) J Biol Chem , vol.252 , pp. 3578-3581
    • Abuchowski, A.1    Es, T.V.2    Palczuk, N.C.3    Davis, F.F.4
  • 5
    • 84870918540 scopus 로고    scopus 로고
    • PEGylation enhancement of pH stability of uricase via inhibitive tetramer dissociation
    • H. Tian, Y. Guo, X. Gao, and W. Yao PEGylation enhancement of pH stability of uricase via inhibitive tetramer dissociation J Pharm Pharmacol 65 2013 53 63
    • (2013) J Pharm Pharmacol , vol.65 , pp. 53-63
    • Tian, H.1    Guo, Y.2    Gao, X.3    Yao, W.4
  • 6
    • 84860012591 scopus 로고    scopus 로고
    • Predictable and tunable half-life extension of therapeutic agents by controlled chemical release from macromolecular conjugates
    • D.V. Santi, E.L. Schneider, R. Reid, L. Robinson, and G.W. Ashley Predictable and tunable half-life extension of therapeutic agents by controlled chemical release from macromolecular conjugates Proc Natl Acad Sci USA 109 16 2012 6211 6216
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.16 , pp. 6211-6216
    • Santi, D.V.1    Schneider, E.L.2    Reid, R.3    Robinson, L.4    Ashley, G.W.5
  • 7
    • 0037124506 scopus 로고    scopus 로고
    • Chemistry for peptide and protein PEGylation
    • M. Roberts, M. Bentley, and J. Harris Chemistry for peptide and protein PEGylation Adv Drug Deliv Rev 54 2002 459 476
    • (2002) Adv Drug Deliv Rev , vol.54 , pp. 459-476
    • Roberts, M.1    Bentley, M.2    Harris, J.3
  • 8
    • 84864145665 scopus 로고    scopus 로고
    • PEGylation of antibody fragments for half-life extension
    • G. Proetzel, H. Ebersbach, Humana Press New York, USA
    • S. Jevsevar, M. Kusterle, and M. Keing PEGylation of antibody fragments for half-life extension G. Proetzel, H. Ebersbach, Antibody methods and protocols. Methods in molecular biology vol. 901 2012 Humana Press New York, USA 233 246
    • (2012) Antibody Methods and Protocols. Methods in Molecular Biology , vol.901 , pp. 233-246
    • Jevsevar, S.1    Kusterle, M.2    Keing, M.3
  • 9
    • 80051753313 scopus 로고    scopus 로고
    • FDA-approved poly(ethylene glycol)-protein conjugate drugs
    • S.N.S. Alconcel, A.S. Baas, and H.D. Maynard FDA-approved poly(ethylene glycol)-protein conjugate drugs Polym Chem 2 2011 1442 1448
    • (2011) Polym Chem , vol.2 , pp. 1442-1448
    • Alconcel, S.N.S.1    Baas, A.S.2    Maynard, H.D.3
  • 10
    • 0033572187 scopus 로고    scopus 로고
    • Microbial alkaline proteases: From a bioindustrial viewpoint
    • C.G. Kumar, and H. Takagi Microbial alkaline proteases: from a bioindustrial viewpoint Biotechnol Adv 17 1999 561 594
    • (1999) Biotechnol Adv , vol.17 , pp. 561-594
    • Kumar, C.G.1    Takagi, H.2
  • 11
    • 0029805302 scopus 로고    scopus 로고
    • Hydrolysis of feather keratin by immobilized keratinase
    • X. Lin, J.C.H. Shih, and E.H. Swaisgood Hydrolysis of feather keratin by immobilized keratinase Appl Environ Microbiol 62 1996 4273 4275
    • (1996) Appl Environ Microbiol , vol.62 , pp. 4273-4275
    • Lin, X.1    Shih, J.C.H.2    Swaisgood, E.H.3
  • 12
    • 67649188397 scopus 로고    scopus 로고
    • Polymer-assisted iron oxide magnetic nanoparticle immobilized keratinase
    • R. Konwarh, N. Karak, S. Rai, and A. Mukherjee Polymer-assisted iron oxide magnetic nanoparticle immobilized keratinase Nanotechnology 20 22 2009 5107
    • (2009) Nanotechnology , vol.20 , Issue.22 , pp. 5107
    • Konwarh, R.1    Karak, N.2    Rai, S.3    Mukherjee, A.4
  • 14
    • 77952239414 scopus 로고    scopus 로고
    • Cholesterol biotransformation to androsta-1,4-diene-3,17-dione by growing cells of Chryseobacterium gleum
    • P.N. Chaudhari, B.L. Chaudhari, and S.B. Chincholkar Cholesterol biotransformation to androsta-1,4-diene-3,17-dione by growing cells of Chryseobacterium gleum Biotechnol Lett 32 2010 695 699
    • (2010) Biotechnol Lett , vol.32 , pp. 695-699
    • Chaudhari, P.N.1    Chaudhari, B.L.2    Chincholkar, S.B.3
  • 15
    • 34247348535 scopus 로고    scopus 로고
    • The influence of enzymatic treatment on wool fibre properties using PEG-modified proteases
    • S. Jus, M. Schroeder, G.M. Guebitz, E. Heine, and V. Kokol The influence of enzymatic treatment on wool fibre properties using PEG-modified proteases Enzyme Microb Technol 40 2007 1705 1711
    • (2007) Enzyme Microb Technol , vol.40 , pp. 1705-1711
    • Jus, S.1    Schroeder, M.2    Guebitz, G.M.3    Heine, E.4    Kokol, V.5
  • 16
    • 84861316086 scopus 로고    scopus 로고
    • Immobilization of keratinolytic metalloprotease from Chryseobacterium sp strain kr6 on glutaraldehyde-activated chitosan
    • S.T. Silveira, S. Gemelli, J. Segalin, and A. Brandelli Immobilization of keratinolytic metalloprotease from Chryseobacterium sp. strain kr6 on glutaraldehyde-activated chitosan J Microbiol Biotechnol 22 6 2012 818 825
    • (2012) J Microbiol Biotechnol , vol.22 , Issue.6 , pp. 818-825
    • Silveira, S.T.1    Gemelli, S.2    Segalin, J.3    Brandelli, A.4
  • 17
    • 84874114318 scopus 로고    scopus 로고
    • Iron containing keratinolytic metallo-protease produced by Chryseobacterium gleum
    • P.N. Chaudhari, B.L. Chaudhari, and S.B. Chincholkar Iron containing keratinolytic metallo-protease produced by Chryseobacterium gleum Process Biochem 48 2013 144 151
    • (2013) Process Biochem , vol.48 , pp. 144-151
    • Chaudhari, P.N.1    Chaudhari, B.L.2    Chincholkar, S.B.3
  • 18
    • 71849104860 scopus 로고
    • Protein measurement with the folin phenol reagent
    • O.H. Lowry, N.J. Rosenberg, A.L. Farr, and F. Smith Protein measurement with the folin phenol reagent J Biol Chem 193 1951 265 275
    • (1951) J Biol Chem , vol.193 , pp. 265-275
    • Lowry, O.H.1    Rosenberg, N.J.2    Farr, A.L.3    Smith, F.4
  • 19
    • 0242500381 scopus 로고    scopus 로고
    • Characterization of a new keratinolytic bacterium that completely degrades native feather keratin
    • A. Riffel, F. Lucas, P. Heeb, and A. Brandelli Characterization of a new keratinolytic bacterium that completely degrades native feather keratin Arch Microbiol 179 2003 258 265
    • (2003) Arch Microbiol , vol.179 , pp. 258-265
    • Riffel, A.1    Lucas, F.2    Heeb, P.3    Brandelli, A.4
  • 20
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 21
    • 33947442158 scopus 로고
    • Effects of ions on Mohr method for chloride determination
    • R.T. Sheen, and H.L. Kahler Effects of ions on Mohr method for chloride determination Ind Eng Chem Anal Ed 10 11 1938 628 629
    • (1938) Ind Eng Chem Anal Ed , vol.10 , Issue.11 , pp. 628-629
    • Sheen, R.T.1    Kahler, H.L.2
  • 22
    • 29744466425 scopus 로고
    • Determination of serum proteins by means of the biuret reaction
    • A.G. Gornall, C.J. Bardawill, and M.M. David Determination of serum proteins by means of the biuret reaction J Biol Chem 177 1949 751 766
    • (1949) J Biol Chem , vol.177 , pp. 751-766
    • Gornall, A.G.1    Bardawill, C.J.2    David, M.M.3
  • 24
    • 49749221698 scopus 로고
    • Modified ninhydrin colorimetric analysis for amino acids
    • H.A. Rosen Modified ninhydrin colorimetric analysis for amino acids Arch Biochem Biophys 67 1957 10 15
    • (1957) Arch Biochem Biophys , vol.67 , pp. 10-15
    • Rosen, H.A.1
  • 25
    • 0037362655 scopus 로고    scopus 로고
    • Effect of PEGylation on pharmaceuticals
    • J.M. Harris, and R.B. Chess Effect of PEGylation on pharmaceuticals Nat Rev Drug Discov 2 2003 214 221
    • (2003) Nat Rev Drug Discov , vol.2 , pp. 214-221
    • Harris, J.M.1    Chess, R.B.2
  • 29
    • 0033911947 scopus 로고    scopus 로고
    • Kinetic study of thermal inactivation for native and methoxypoly-ethylene glycol modified trypsin
    • Z. He, Z. Zhang, and M. He Kinetic study of thermal inactivation for native and methoxypoly-ethylene glycol modified trypsin Process Biochem 35 2000 1235 1240
    • (2000) Process Biochem , vol.35 , pp. 1235-1240
    • He, Z.1    Zhang, Z.2    He, M.3
  • 30
    • 0036225062 scopus 로고    scopus 로고
    • Production, purification, and characterization of an extracellular keratinase from Lysobacter NCIMB 9497
    • J.D. Allpress, G. Mountain, and P.C. Gowland Production, purification, and characterization of an extracellular keratinase from Lysobacter NCIMB 9497 Lett Appl Microbiol 34 2002 337 342
    • (2002) Lett Appl Microbiol , vol.34 , pp. 337-342
    • Allpress, J.D.1    Mountain, G.2    Gowland, P.C.3
  • 31
    • 10044290786 scopus 로고    scopus 로고
    • Biosynthetic hydrogel scaffolds made from fibrinogen and polyethylene glycol for 3D cell cultures
    • L. Almany, and D. Seliktar Biosynthetic hydrogel scaffolds made from fibrinogen and polyethylene glycol for 3D cell cultures Biomaterials 26 2005 2467 2477
    • (2005) Biomaterials , vol.26 , pp. 2467-2477
    • Almany, L.1    Seliktar, D.2
  • 32
    • 33748747129 scopus 로고    scopus 로고
    • An organic solvent-stable alkaline protease from Pseudomonas aeruginosa strain K: Enzyme purification and characterization
    • R.N.Z.A. Rahman, L.P. Geok, M. Basri, and A.B. Salleh An organic solvent-stable alkaline protease from Pseudomonas aeruginosa strain K: enzyme purification and characterization Enzyme Microb Technol 39 2006 1484 1491
    • (2006) Enzyme Microb Technol , vol.39 , pp. 1484-1491
    • Rahman, R.N.Z.A.1    Geok, L.P.2    Basri, M.3    Salleh, A.B.4
  • 33
    • 34548094323 scopus 로고    scopus 로고
    • Fourier transform infrared spectroscopic analysis of protein secondary structures
    • J. Kong, and S. Yu Fourier transform infrared spectroscopic analysis of protein secondary structures Acta Biochim Biophys Sin 39 2007 549 559
    • (2007) Acta Biochim Biophys Sin , vol.39 , pp. 549-559
    • Kong, J.1    Yu, S.2
  • 35
    • 33846115676 scopus 로고    scopus 로고
    • PEGylated dendritic architecture for development of a prolonged drug delivery system for an antitubercular drug
    • P. Vijayaraj Kumar, H. Agashe, T. Dutta, and N. Jain PEGylated dendritic architecture for development of a prolonged drug delivery system for an antitubercular drug Curr Drug Deliv 4 2007 11 19
    • (2007) Curr Drug Deliv , vol.4 , pp. 11-19
    • Vijayaraj Kumar, P.1    Agashe, H.2    Dutta, T.3    Jain, N.4
  • 36
    • 0001629452 scopus 로고
    • Conformation of poly(ethylene oxide) in the solid state, melt and solution measured by Raman scattering
    • J. Maxfield, and I.W. Shepherd Conformation of poly(ethylene oxide) in the solid state, melt and solution measured by Raman scattering Polymer 16 1975 505 509
    • (1975) Polymer , vol.16 , pp. 505-509
    • Maxfield, J.1    Shepherd, I.W.2
  • 37
    • 0035312586 scopus 로고    scopus 로고
    • Interactions between prion protein isoforms: The kiss of death
    • B. Caughey Interactions between prion protein isoforms: the kiss of death Trends Biochem Sci 26 2001 235 242
    • (2001) Trends Biochem Sci , vol.26 , pp. 235-242
    • Caughey, B.1
  • 38
    • 0346882925 scopus 로고    scopus 로고
    • Enzymatic degradation of prion protein in brain stem from infected cattle and sheep
    • J. Langeveld, J. Wang, D. van de Wiel, G. Shih, G. Garssen, and A. Bossers Enzymatic degradation of prion protein in brain stem from infected cattle and sheep J Infect Dis 188 2003 1782 1789
    • (2003) J Infect Dis , vol.188 , pp. 1782-1789
    • Langeveld, J.1    Wang, J.2    Van De Wiel, D.3    Shih, G.4    Garssen, G.5    Bossers, A.6


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