메뉴 건너뛰기




Volumn 40, Issue 7, 2007, Pages 1794-1800

An evaluation of the action of thioesterases on the surface of wool

Author keywords

Esterases; Lipases; Palmitoyl protein thioesterase; Surface modification; Wool

Indexed keywords

ESTERASES; PALMITOYL PROTEIN THIOESTERASE; THIOESTERASES;

EID: 34247356863     PISSN: 01410229     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2007.01.016     Document Type: Article
Times cited : (21)

References (26)
  • 2
    • 0031171547 scopus 로고    scopus 로고
    • Cleavage of integral surface lipids of wool by aminolysis
    • Evans D.J., and Lanczki M. Cleavage of integral surface lipids of wool by aminolysis. Text Res J 67 (1997) 435-444
    • (1997) Text Res J , vol.67 , pp. 435-444
    • Evans, D.J.1    Lanczki, M.2
  • 4
    • 0025957385 scopus 로고
    • Structural lipids of the wool fibre
    • Rivett D.E. Structural lipids of the wool fibre. Wool Sci Rev 67 (1991) 1-25
    • (1991) Wool Sci Rev , vol.67 , pp. 1-25
    • Rivett, D.E.1
  • 5
    • 0023809217 scopus 로고
    • Integral lipids of human hair
    • Wertz P.W., and Downing D.T. Integral lipids of human hair. Lipids 23 (1988) 878-881
    • (1988) Lipids , vol.23 , pp. 878-881
    • Wertz, P.W.1    Downing, D.T.2
  • 7
    • 0001562785 scopus 로고
    • The nature of the covalently bound fatty acids in wool fibres
    • Negri A.P., Cornell H.J., and Rivett D.E. The nature of the covalently bound fatty acids in wool fibres. Aust J Agric Res 42 (1991) 1285-1292
    • (1991) Aust J Agric Res , vol.42 , pp. 1285-1292
    • Negri, A.P.1    Cornell, H.J.2    Rivett, D.E.3
  • 8
    • 0027542578 scopus 로고
    • A model for the surface of keratin fibres
    • Negri A.P., Cornell H.J., and Rivett D.E. A model for the surface of keratin fibres. Text Res J 63 (1993) 109-115
    • (1993) Text Res J , vol.63 , pp. 109-115
    • Negri, A.P.1    Cornell, H.J.2    Rivett, D.E.3
  • 10
    • 33751239105 scopus 로고    scopus 로고
    • Considerations on the occurrence of Loricrin and Involucrin in the cell envelope of wool cuticle cells
    • Zahn H., and Wortmann F.J. Considerations on the occurrence of Loricrin and Involucrin in the cell envelope of wool cuticle cells. Int J Sheep Wool Sci 53 (2005) 23-36
    • (2005) Int J Sheep Wool Sci , vol.53 , pp. 23-36
    • Zahn, H.1    Wortmann, F.J.2
  • 11
    • 0027542578 scopus 로고
    • The modification of the surface diffusion barrier of wool
    • Negri A.P., Cornell H.J., and Rivett D.E. The modification of the surface diffusion barrier of wool. J Soc Dyers Colour 63 (1993) 109-115
    • (1993) J Soc Dyers Colour , vol.63 , pp. 109-115
    • Negri, A.P.1    Cornell, H.J.2    Rivett, D.E.3
  • 12
    • 0001441710 scopus 로고    scopus 로고
    • Time-of-flight secondary-ion-mass spectometric (ToF-SIMS) and X-ray photoelectron spectroscopic (XPS) analyses of the surface lipids of wool
    • Shao J., Jones D.C., Mitchell R., Vickerman J.C., and Carr C.M. Time-of-flight secondary-ion-mass spectometric (ToF-SIMS) and X-ray photoelectron spectroscopic (XPS) analyses of the surface lipids of wool. J Text Inst 88 (1997) 317-324
    • (1997) J Text Inst , vol.88 , pp. 317-324
    • Shao, J.1    Jones, D.C.2    Mitchell, R.3    Vickerman, J.C.4    Carr, C.M.5
  • 13
    • 84942087397 scopus 로고    scopus 로고
    • Process engineering and industrial enzyme applications
    • Cavaco-Paulo A., and Gubiz G.M. (Eds), Woodhead Publishing Limited, Cambridge
    • Nierstrasz V.A., and Warmoeskerken M.M.C.G. Process engineering and industrial enzyme applications. In: Cavaco-Paulo A., and Gubiz G.M. (Eds). Textile processing with enzymes (2003), Woodhead Publishing Limited, Cambridge 120-157
    • (2003) Textile processing with enzymes , pp. 120-157
    • Nierstrasz, V.A.1    Warmoeskerken, M.M.C.G.2
  • 14
    • 0029168601 scopus 로고
    • Enzyme treatments for wool and cotton
    • Heine E., and Höcker H. Enzyme treatments for wool and cotton. Rev Prog Color 25 (1995) 57-63
    • (1995) Rev Prog Color , vol.25 , pp. 57-63
    • Heine, E.1    Höcker, H.2
  • 15
    • 34247386871 scopus 로고    scopus 로고
    • Heine E. Fundamental research on the action of enzymes on wool. PhD Thesis. Reinisch-Westfaelish Technischen Hochschule; 1991.
  • 20
    • 34247371977 scopus 로고    scopus 로고
    • Surface chemical analysis of lipase enzyme treatments on wool and mohair
    • Mall J.K., Sims P., and Carr C.M. Surface chemical analysis of lipase enzyme treatments on wool and mohair. J Text Inst, Part 1 93 (2002) 43-51
    • (2002) J Text Inst, Part 1 , vol.93 , pp. 43-51
    • Mall, J.K.1    Sims, P.2    Carr, C.M.3
  • 21
    • 0242329835 scopus 로고    scopus 로고
    • Enzyme catalysed hydrolysis of 18-methyleicosanoic acid-cysteine thioester
    • Ganske F., Meyer H.H., Deutz H., and Bornscheuer U. Enzyme catalysed hydrolysis of 18-methyleicosanoic acid-cysteine thioester. Eur J Lipid Sci Technol 105 (2003) 627-632
    • (2003) Eur J Lipid Sci Technol , vol.105 , pp. 627-632
    • Ganske, F.1    Meyer, H.H.2    Deutz, H.3    Bornscheuer, U.4
  • 22
    • 0037047595 scopus 로고    scopus 로고
    • Chemical synthesis of poliovirus cDNA: generation of infectious virus in absence of natural template
    • Cello J., Paul A.V., and Wimmer E. Chemical synthesis of poliovirus cDNA: generation of infectious virus in absence of natural template. Science 297 (2002) 1016-1018
    • (2002) Science , vol.297 , pp. 1016-1018
    • Cello, J.1    Paul, A.V.2    Wimmer, E.3
  • 23
    • 0034712969 scopus 로고    scopus 로고
    • The crystal structure of palmitoyl protein thioesterase 1 and the molecular basis of infantile neuronal ceroid lipofuscinosis
    • Bellizzi III J.J., Widom J., Kemp C., Lu J.-Y., Das A.K., Hofmann S.L., et al. The crystal structure of palmitoyl protein thioesterase 1 and the molecular basis of infantile neuronal ceroid lipofuscinosis. Proc Nat Acad Sci 97 (2000) 4573-4578
    • (2000) Proc Nat Acad Sci , vol.97 , pp. 4573-4578
    • Bellizzi III, J.J.1    Widom, J.2    Kemp, C.3    Lu, J.-Y.4    Das, A.K.5    Hofmann, S.L.6
  • 24
    • 0141621057 scopus 로고    scopus 로고
    • The crystal structure of palmitoyl protein thioesterase-2 (PPT2) reveals the basis for divergent substrate specificities of the two lysosomal thioesterases. PPT1 and PPT2
    • Calero G., Gupta P., Nonato M.C., Tandel S., Biehl E.R., Hofmann S.L., et al. The crystal structure of palmitoyl protein thioesterase-2 (PPT2) reveals the basis for divergent substrate specificities of the two lysosomal thioesterases. PPT1 and PPT2. J Biol Chem 278 (2003) 37957-37964
    • (2003) J Biol Chem , vol.278 , pp. 37957-37964
    • Calero, G.1    Gupta, P.2    Nonato, M.C.3    Tandel, S.4    Biehl, E.R.5    Hofmann, S.L.6
  • 25
    • 0019346202 scopus 로고
    • Medium-chain fatty acyl-S-4′-phosphopantetheine-fatty acid synthase thioester hydrolase from lactating rabbit and goat mammary glands
    • Knudsen J., Grunnet I., and Dils R. Medium-chain fatty acyl-S-4′-phosphopantetheine-fatty acid synthase thioester hydrolase from lactating rabbit and goat mammary glands. Methods Enzymol 71 (1981) 200-229
    • (1981) Methods Enzymol , vol.71 , pp. 200-229
    • Knudsen, J.1    Grunnet, I.2    Dils, R.3
  • 26
    • 0035852885 scopus 로고    scopus 로고
    • How do lipases and esterases work: the electrostatic contribution
    • Petersen M.T.N., and Petersen S.B. How do lipases and esterases work: the electrostatic contribution. J Biotechnol 85 (2001) 115-147
    • (2001) J Biotechnol , vol.85 , pp. 115-147
    • Petersen, M.T.N.1    Petersen, S.B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.