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Volumn 22, Issue 5-6, 2004, Pages 299-305

Chemical modification of proteases for wool cuticle scale removal

Author keywords

Anti shrinkage; Bacillus lentus protease; Diffusion; Enzyme modification; Polyethylene glycol; Wool treatment

Indexed keywords

ENZYMES; FABRICS; FIBERS; MOLECULAR WEIGHT; POLYETHYLENE GLYCOLS; SHRINKPROOFING (TEXTILES);

EID: 15844378085     PISSN: 10242422     EISSN: None     Source Type: Journal    
DOI: 10.1080/10242420400025794     Document Type: Article
Times cited : (36)

References (28)
  • 1
    • 0017701219 scopus 로고
    • Alteration of immunological properties of bovine serum albumin by covalent attachment of polyethylene glycol
    • Abuchowski, A., van Es, T., Palczuk, N.C. and Davis, F.F. (1977) Alteration of immunological properties of bovine serum albumin by covalent attachment of polyethylene glycol, J. Biol. Chem. 252 3578.
    • (1977) J. Biol. Chem. , vol.252 , pp. 3578
    • Abuchowski, A.1    van Es, T.2    Palczuk, N.C.3    Davis, F.F.4
  • 2
    • 0028815614 scopus 로고
    • Chemical derivates of Pseudomonas aeruginosa elastase showing increased stability
    • Besson, C., Favre-Bovine, G., O'Fagain, C. and Wallach, J. (1995) Chemical derivates of Pseudomonas aeruginosa elastase showing increased stability, Enzyme Microb. Technol. 17, 877-881.
    • (1995) Enzyme Microb. Technol. , vol.17 , pp. 877-881
    • Besson, C.1    Favre-Bovine, G.2    O'Fagain, C.3    Wallach, J.4
  • 3
    • 0000937988 scopus 로고    scopus 로고
    • The use of proteolitic enzymes to reduce wool fibre stiffness and prickle
    • Bishop, D.P., Shen, J., Heine, E. and Hollfelder, B. (1998) The use of proteolitic enzymes to reduce wool fibre stiffness and prickle, J. Text. Inst. 89, 546-553.
    • (1998) J. Text. Inst. , vol.89 , pp. 546-553
    • Bishop, D.P.1    Shen, J.2    Heine, E.3    Hollfelder, B.4
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M.M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding, Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 0344665625 scopus 로고    scopus 로고
    • Application of transglutaminases in the modification of wool textiles
    • Cortez, J., Bonner, P.L.R. and Griffin, M. (2004) Application of transglutaminases in the modification of wool textiles, Enzyme Microb. Technol. 34, 64-72.
    • (2004) Enzyme Microb. Technol. , vol.34 , pp. 64-72
    • Cortez, J.1    Bonner, P.L.R.2    Griffin, M.3
  • 6
    • 0035845748 scopus 로고    scopus 로고
    • Poly(ethylene glycol)-human serum albumin-paclitaxel conjugates: Preparation, characterization and pharmacokinetics
    • Dosio, F., Apricco, S., Brusa, P., Stella, B. and Cattel, L. (2001) Poly(ethylene glycol)-human serum albumin-paclitaxel conjugates: preparation, characterization and pharmacokinetics, J. Contr. Rel. 76, 107-117.
    • (2001) J. Contr. Rel. , vol.76 , pp. 107-117
    • Dosio, F.1    Apricco, S.2    Brusa, P.3    Stella, B.4    Cattel, L.5
  • 7
    • 0034838636 scopus 로고    scopus 로고
    • Developing a zero-AOX shrink-resist process for wool. Part 1: Preliminary results
    • El-Sayed, H., Kantouch, A., Heine, E. and Höcker, H. (2001) Developing a zero-AOX shrink-resist process for wool. Part 1: Preliminary results, Color. Technol. 117, 234-238.
    • (2001) Color. Technol. , vol.117 , pp. 234-238
    • El-Sayed, H.1    Kantouch, A.2    Heine, E.3    Höcker, H.4
  • 8
    • 0037457502 scopus 로고    scopus 로고
    • Size-exclusion reaction chromatography (SERC): A new technique for protein PEGylation
    • Fee, C.J. (2003) Size-exclusion reaction chromatography (SERC): A new technique for protein PEGylation, Biotechnol. Bioeng. 82, 200-206.
    • (2003) Biotechnol. Bioeng. , vol.82 , pp. 200-206
    • Fee, C.J.1
  • 9
    • 0026816560 scopus 로고
    • Increased activity and stability of poly(ethylene glycol)-modified trypsin
    • Gaertner, H.F. and Puigserver, A.J. (1992) Increased activity and stability of poly(ethylene glycol)-modified trypsin, Enzyme Microb. Technol. 14, 150-155.
    • (1992) Enzyme Microb. Technol. , vol.14 , pp. 150-155
    • Gaertner, H.F.1    Puigserver, A.J.2
  • 10
    • 0013889689 scopus 로고
    • Determination of free amino groups in proteins by trinitrobenzensulfonic acid
    • Habeeb, A.F.S.A. (1966) Determination of free amino groups in proteins by trinitrobenzensulfonic acid, Anal. Biochem. 14, 328-336.
    • (1966) Anal. Biochem. , vol.14 , pp. 328-336
    • Habeeb, A.F.S.A.1
  • 11
    • 0029168601 scopus 로고
    • Enzyme treatments for wool and cotton
    • Heine, E. and Hocker, H. (1995) Enzyme treatments for wool and cotton, Rev. Prog. Coloration 25, 57-63.
    • (1995) Rev. Prog. Coloration , vol.25 , pp. 57-63
    • Heine, E.1    Hocker, H.2
  • 12
    • 0343471966 scopus 로고    scopus 로고
    • Influence of the nature of modifier in the enzymatic acvtivity of chemical modified semipurified lipase from Candia rugosa
    • Hernáiz, M.J., Sánchez-Montero, J.M. and Sinisterra, J.V. (1996) Influence of the nature of modifier in the enzymatic acvtivity of chemical modified semipurified lipase from Candia rugosa, Biotechnol. Bioeng. 55, 252-260.
    • (1996) Biotechnol. Bioeng. , vol.55 , pp. 252-260
    • Hernáiz, M.J.1    Sánchez-Montero, J.M.2    Sinisterra, J.V.3
  • 16
    • 0032887991 scopus 로고    scopus 로고
    • Effect of chemical modification on the activity of lipases in organic solvents
    • Koops, B.C., Verheij, H.M., Slotboom, A.J. and Egmond, M.R. (1999) Effect of chemical modification on the activity of lipases in organic solvents, Enzyme Microb. Technol. 25, 622-631.
    • (1999) Enzyme Microb. Technol. , vol.25 , pp. 622-631
    • Koops, B.C.1    Verheij, H.M.2    Slotboom, A.J.3    Egmond, M.R.4
  • 17
    • 0000026335 scopus 로고    scopus 로고
    • Catalytic activity and conformation of chemically modified subtilisin carlsberg in organic media
    • Kwon, O.H., Imanishi, Y. and Ito, Y. (1999) Catalytic activity and conformation of chemically modified subtilisin carlsberg in organic media, Biotechnol. Bioeng. 66, 265-270.
    • (1999) Biotechnol. Bioeng. , vol.66 , pp. 265-270
    • Kwon, O.H.1    Imanishi, Y.2    Ito, Y.3
  • 18
    • 71849104860 scopus 로고
    • Protein measurement with the folin phenol reagent
    • Lowry, O.H. (1950) Protein measurement with the folin phenol reagent, J. Biol. Chem. 193, 265-275.
    • (1950) J. Biol. Chem. , vol.193 , pp. 265-275
    • Lowry, O.H.1
  • 19
    • 0029888825 scopus 로고    scopus 로고
    • A Colorimetric assay for estimation of polethylene glycol and polyethylene glycolated protein using ammonium ferrothiocyanate
    • Nag, A., Mitra, G. and Ghosh, P.C. (1996) A Colorimetric assay for estimation of polethylene glycol and polyethylene glycolated protein using ammonium ferrothiocyanate, Anal. Biochem. 237, 224-231.
    • (1996) Anal. Biochem. , vol.237 , pp. 224-231
    • Nag, A.1    Mitra, G.2    Ghosh, P.C.3
  • 20
    • 0027507002 scopus 로고
    • The role of an enzyme in reducing wool shrinkage
    • Riva, A., Cegarra, J. and Prieto, R. (1993) The role of an enzyme in reducing wool shrinkage, J. Soc. Dyers. Colour. 109 210-213.
    • (1993) J. Soc. Dyers. Colour , vol.109 , pp. 210-213
    • Riva, A.1    Cegarra, J.2    Prieto, R.3
  • 22
    • 5244293803 scopus 로고    scopus 로고
    • Protein derivate in der Wollveredlung
    • Schäfer, K. and Höcker, H. (1996) Protein derivate in der Wollveredlung, Melliand Texilber. 77, 402-406.
    • (1996) Melliand Texilber. , vol.77 , pp. 402-406
    • Schäfer, K.1    Höcker, H.2
  • 23
    • 0035940087 scopus 로고    scopus 로고
    • Extremozymes for improving wool properties
    • Schumacher, K., Heine, E. and Höcker, H. (2001) Extremozymes for improving wool properties, J. Biotechnol. 89 281-288.
    • (2001) J. Biotechnol. , vol.89 , pp. 281-288
    • Schumacher, K.1    Heine, E.2    Höcker, H.3
  • 24
    • 0002858849 scopus 로고    scopus 로고
    • Factors affecting the control of proteolitic enzyme reactions on wool
    • Shen, J., Bishop, D.P., Heine, E. and Hollfelder, B. (1999) Factors affecting the control of proteolitic enzyme reactions on wool, J. Textile Inst. 90, 404-411.
    • (1999) J. Textile Inst. , vol.90 , pp. 404-411
    • Shen, J.1    Bishop, D.P.2    Heine, E.3    Hollfelder, B.4
  • 25
    • 0016636179 scopus 로고
    • An improved 2,4,6-trinitrobenzenesulfonic acid method for the determination of amines
    • Snyder, S.L. and Sobocinski, P.Z. (1975) An improved 2,4,6-trinitrobenzenesulfonic acid method for the determination of amines, Anal. Biochem. 64, 284-288.
    • (1975) Anal. Biochem. , vol.64 , pp. 284-288
    • Snyder, S.L.1    Sobocinski, P.Z.2
  • 26
    • 0004026796 scopus 로고
    • Enzyme - Biokatalysatoren in der Textilverarbeitung
    • Stöhr, R. (1995) Enzyme - Biokatalysatoren in der Textilverarbeitung, Melliand Textilber. 1010-1013.
    • (1995) Melliand Textilber. , pp. 1010-1013
    • Stöhr, R.1
  • 27
    • 0035284411 scopus 로고    scopus 로고
    • Peptide and protein PEGylation: A review of problems and solutions
    • Veronese, F.M. (2001) Peptide and protein PEGylation: a review of problems and solutions, Biomaterials 22, 405-417.
    • (2001) Biomaterials , vol.22 , pp. 405-417
    • Veronese, F.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.