메뉴 건너뛰기




Volumn 47, Issue 3, 2010, Pages 105-111

Covalent bonding of protease to different sized enteric polymers and their potential use in wool processing

Author keywords

Enteric polymer; Enzyme; Modified protease; Protease; Shrink resistance; Wool

Indexed keywords

ACTIVITY LEVELS; CARBODIIMIDES; CHEMICAL STRUCTURE; CHEMICALLY MODIFIED; COVALENT BONDING; ENTERIC POLYMER; ENZYME ATTACK; FIBRE DAMAGE; GEL FILTRATION; MODIFIED ENZYMES; NATIVE ENZYMES; PENETRATION ABILITY; POLYMERIC MOLECULES; WEIGHT LOSS;

EID: 77954656420     PISSN: 01410229     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2010.05.011     Document Type: Article
Times cited : (26)

References (26)
  • 1
    • 84902217827 scopus 로고    scopus 로고
    • Wool finishing and development of novel finishes
    • Woodhead Publishing, Cambridge, N.A.G. Johnson, I.M. Russell (Eds.)
    • Shen J. Wool finishing and development of novel finishes. Advances in wool technology 2009, 147-182. Woodhead Publishing, Cambridge. N.A.G. Johnson, I.M. Russell (Eds.).
    • (2009) Advances in wool technology , pp. 147-182
    • Shen, J.1
  • 2
    • 0029672282 scopus 로고    scopus 로고
    • Effects of proteolytic and lipolytic enzymes on untreated and shrink-resist treated wool
    • Nolte H., Bishop D.P., Höcker H. Effects of proteolytic and lipolytic enzymes on untreated and shrink-resist treated wool. J Text Inst 1996, 87:212-226.
    • (1996) J Text Inst , vol.87 , pp. 212-226
    • Nolte, H.1    Bishop, D.P.2    Höcker, H.3
  • 3
    • 0002858849 scopus 로고    scopus 로고
    • Some factors affecting the control of proteolytic enzyme reactions on wool
    • Shen J., Bishop D., Heine E., Hollfelder B. Some factors affecting the control of proteolytic enzyme reactions on wool. J Text Inst 1999, 90:404-411.
    • (1999) J Text Inst , vol.90 , pp. 404-411
    • Shen, J.1    Bishop, D.2    Heine, E.3    Hollfelder, B.4
  • 5
    • 77954659937 scopus 로고    scopus 로고
    • Treatment of animal hair fibres with modified proteases.
    • Cavaco-Paulo A, Silva CJSM. Treatment of animal hair fibres with modified proteases. WO03097927; 2003.
    • (2003)
    • Cavaco-Paulo, A.1    Silva, C.J.S.M.2
  • 7
    • 31444440561 scopus 로고    scopus 로고
    • Optimisation of a serine protease coupling to Eudragit S-100 by experimental design techniques
    • Silva C.J.S.M., Gübitz G., Cavaco-Paulo A. Optimisation of a serine protease coupling to Eudragit S-100 by experimental design techniques. J Chem Technol Biotechnol 2006, 81:8-16.
    • (2006) J Chem Technol Biotechnol , vol.81 , pp. 8-16
    • Silva, C.J.S.M.1    Gübitz, G.2    Cavaco-Paulo, A.3
  • 8
    • 33745213794 scopus 로고    scopus 로고
    • Immobilization of proteases with a water soluble-insoluble reversible polymer for the treatment of wool
    • Silva C.J.S.M., Zhang Q., Shen J., Cavaco-Paulo A. Immobilization of proteases with a water soluble-insoluble reversible polymer for the treatment of wool. Enzyme Microb Technol 2006, 39:634-640.
    • (2006) Enzyme Microb Technol , vol.39 , pp. 634-640
    • Silva, C.J.S.M.1    Zhang, Q.2    Shen, J.3    Cavaco-Paulo, A.4
  • 9
    • 54049129684 scopus 로고    scopus 로고
    • Modification of Esperase by covalent bonding to Eudragit polymers L100 and S100 for wool fibre surface treatment
    • Smith E., Zhang Q., Shen J., Schroeder M., Silva C. Modification of Esperase by covalent bonding to Eudragit polymers L100 and S100 for wool fibre surface treatment. Biocatal Biotransform 2008, 26:391-398.
    • (2008) Biocatal Biotransform , vol.26 , pp. 391-398
    • Smith, E.1    Zhang, Q.2    Shen, J.3    Schroeder, M.4    Silva, C.5
  • 10
    • 26844576835 scopus 로고    scopus 로고
    • Amide formation and peptide coupling
    • Montalbetti C.A.G.N., Falque V. Amide formation and peptide coupling. Tetrahedron 2005, 61:10827-10852.
    • (2005) Tetrahedron , vol.61 , pp. 10827-10852
    • Montalbetti, C.A.G.N.1    Falque, V.2
  • 11
    • 0034255864 scopus 로고    scopus 로고
    • Reversibly soluble biocatalyst: optimization of tripsyn coupling to Eudragit S-100 and biocatalyst activity in soluble and precipitated forms
    • Arasaratnam V., Galaev I.Y., Mattiasson B. Reversibly soluble biocatalyst: optimization of tripsyn coupling to Eudragit S-100 and biocatalyst activity in soluble and precipitated forms. Enzyme Microb Technol 2000, 27:254-263.
    • (2000) Enzyme Microb Technol , vol.27 , pp. 254-263
    • Arasaratnam, V.1    Galaev, I.Y.2    Mattiasson, B.3
  • 12
    • 12144260774 scopus 로고    scopus 로고
    • Enteric film coating of soft gelatine capsules
    • Felton L.A., McGinity J.W. Enteric film coating of soft gelatine capsules. Drug Deliv Technol 2003, 3(6):34-39.
    • (2003) Drug Deliv Technol , vol.3 , Issue.6 , pp. 34-39
    • Felton, L.A.1    McGinity, J.W.2
  • 14
    • 0033997903 scopus 로고    scopus 로고
    • Ion-exclusion controlled size exclusion chromatography of methacrylic acid-methyl methacrylate copolymers
    • Porsch B., Hillang I., Karlsson A., Sundelöf L.-O. Ion-exclusion controlled size exclusion chromatography of methacrylic acid-methyl methacrylate copolymers. J Chromatogr A 2000, 872:91-99.
    • (2000) J Chromatogr A , vol.872 , pp. 91-99
    • Porsch, B.1    Hillang, I.2    Karlsson, A.3    Sundelöf, L.-O.4
  • 16
    • 0348025526 scopus 로고    scopus 로고
    • Pharmaceutical Press, London, R.C. Rowe, P.J. Sheskey, P.J. Weller (Eds.)
    • Handbook of pharmaceutical excipients 2003, Pharmaceutical Press, London. 4th ed. R.C. Rowe, P.J. Sheskey, P.J. Weller (Eds.).
    • (2003) Handbook of pharmaceutical excipients
  • 17
    • 2942668680 scopus 로고    scopus 로고
    • Molecular weight determination of hypromellose phthalate (HPMCP) using size exclusion chromatography with a multi-angle laser light scattering detector
    • Fukasawa M., Obara S. Molecular weight determination of hypromellose phthalate (HPMCP) using size exclusion chromatography with a multi-angle laser light scattering detector. Chem Pharm Bull 2003, 51:1304-1306.
    • (2003) Chem Pharm Bull , vol.51 , pp. 1304-1306
    • Fukasawa, M.1    Obara, S.2
  • 18
    • 0036604788 scopus 로고    scopus 로고
    • Distribution analysis of cellulose acetate phthalate by ion-exclusion-moderated size exclusion chromatography
    • Porsch B., Hillang I., Karlsson A., Sundelöf L.-O. Distribution analysis of cellulose acetate phthalate by ion-exclusion-moderated size exclusion chromatography. Carbohydr Polym 2002, 48:379-384.
    • (2002) Carbohydr Polym , vol.48 , pp. 379-384
    • Porsch, B.1    Hillang, I.2    Karlsson, A.3    Sundelöf, L.-O.4
  • 19
    • 0032524177 scopus 로고    scopus 로고
    • Reversible immobilization of chitinase via coupling to reversibly soluble polymer
    • Wang S., Chio S. Reversible immobilization of chitinase via coupling to reversibly soluble polymer. Enzyme Microb Technol 1998, 22:634-640.
    • (1998) Enzyme Microb Technol , vol.22 , pp. 634-640
    • Wang, S.1    Chio, S.2
  • 20
    • 0034237456 scopus 로고    scopus 로고
    • Protease produced by Pseudomonas aeruginosa K-187 and its application in the deproteinization of shrimp and crab shell wastes
    • Oh Y., Shih I., Tzeng Y., Wang S. Protease produced by Pseudomonas aeruginosa K-187 and its application in the deproteinization of shrimp and crab shell wastes. Enzyme Microb Technol 2000, 27:3-10.
    • (2000) Enzyme Microb Technol , vol.27 , pp. 3-10
    • Oh, Y.1    Shih, I.2    Tzeng, Y.3    Wang, S.4
  • 21
    • 0041880324 scopus 로고    scopus 로고
    • Reversible immobilization of lysozyme via coupling to reversibly soluble polymer
    • Chen S., Yen Y., Wang C., Wang S. Reversible immobilization of lysozyme via coupling to reversibly soluble polymer. Enzyme Microb Technol 2003, 33:643-649.
    • (2003) Enzyme Microb Technol , vol.33 , pp. 643-649
    • Chen, S.1    Yen, Y.2    Wang, C.3    Wang, S.4
  • 22
    • 0029124443 scopus 로고
    • Preparation and properties of an immobilized soluble-insoluble pectinlyase
    • Dinella C., Lanzarini G., Ercolessi P. Preparation and properties of an immobilized soluble-insoluble pectinlyase. Process Biochem 1995, 30:151-157.
    • (1995) Process Biochem , vol.30 , pp. 151-157
    • Dinella, C.1    Lanzarini, G.2    Ercolessi, P.3
  • 23
    • 0023331854 scopus 로고
    • Preparation and properties of soluble-insoluble immobilized proteases
    • Fujimura M., Mori T., Tosa T. Preparation and properties of soluble-insoluble immobilized proteases. Biotechnol Bioeng 1987, 29:747-752.
    • (1987) Biotechnol Bioeng , vol.29 , pp. 747-752
    • Fujimura, M.1    Mori, T.2    Tosa, T.3
  • 24
    • 0025890983 scopus 로고
    • Application of reversibly soluble polymers in bioprocessing
    • Fujii M., Taniguchi M. Application of reversibly soluble polymers in bioprocessing. Trends Biotechnol 1991, 9:191-196.
    • (1991) Trends Biotechnol , vol.9 , pp. 191-196
    • Fujii, M.1    Taniguchi, M.2
  • 25
    • 0029973959 scopus 로고    scopus 로고
    • Repeated utilization of β-glucsidase immobilized on a reversibly soluble insoluble polymer for hydrolysis of phloridzin as a model reaction producing a water-insoluble product
    • Hoshino K., Taniguchi M., Ueko H., Ohkuwa M., Chida C., Morohashi S., et al. Repeated utilization of β-glucsidase immobilized on a reversibly soluble insoluble polymer for hydrolysis of phloridzin as a model reaction producing a water-insoluble product. J Ferment Bioeng 1996, 82:253-258.
    • (1996) J Ferment Bioeng , vol.82 , pp. 253-258
    • Hoshino, K.1    Taniguchi, M.2    Ueko, H.3    Ohkuwa, M.4    Chida, C.5    Morohashi, S.6
  • 26
    • 0000402303 scopus 로고    scopus 로고
    • The efficiency of an enzyme treatment in reducing wool shrinkage
    • Jovančić P., Jocić D., Dumić J. The efficiency of an enzyme treatment in reducing wool shrinkage. J Text Inst 1998, 89(2):390-400.
    • (1998) J Text Inst , vol.89 , Issue.2 , pp. 390-400
    • Jovančić, P.1    Jocić, D.2    Dumić, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.