期刊文献+

角质酶的研究进展 被引量:10

Advances in cutinase research
原文传递
导出
摘要 角质酶(EC3.1.1.74)是一种可以降解角质并产生大量脂肪酸单体的水解酶。角质酶是一种多功能酶,可水解可溶性酯、不溶性甘油三酯和各种聚酯,同时还能催化酸与醇的酯化、脂肪酸盐与醇的转酯化反应,因此在食品工业、化工工业等诸多领域都具有广泛的应用。近年来研究发现,角质酶可实现棉纤维的生物精练和合成纤维的生物改性,是推动纺织工业清洁生产的关键酶制剂。 Cutinase (EC 3.1.1.74) is a kind of hydrolase capable of catalyzing the cleavage of ester bonds of cutin to release fatty acids.Cutinase displayed hydrolytic activity not only toward cutin but also a variety of soluble synthetic esters,insoluble triglycerides and polyesters.Besides its hydrolytic activity,cutinase also showed synthetic activity and transester activity.Therefore,cutinase was evaluated as a versatile lipolytic enzyme used in food and chemical industry.Recently,it is found that cutinase has potential use in cotton bio-scouring and syiathetic fibers modification. Cutinase is the most important enzyme in clean production of textile industry.
出处 《生物工程学报》 CAS CSCD 北大核心 2009年第12期1829-1837,共9页 Chinese Journal of Biotechnology
基金 国家杰出青年基金(No.20625619) 教育部新世纪优秀人才支持计划(No.NCET-05-0488) 国家高技术研究发展计划(863计划)(No.2009AA02Z204) 江苏省科技支撑计划(No.SBE200900022)资助~~
关键词 角质酶 角质 棉纤维的生物精练 cutinase cutin cotton bio-scouring
  • 相关文献

参考文献71

  • 1Nardini M, Dijkstra BW. Alpha/beta hydrolase fold enzymes: the family keeps growing. Curr Opin Struct Biol, 1999, 9(6): 732-737.
  • 2Holmquist M. Alpha/Beta-hydrolase fold enzymes: structures, functions and mechanisms. Curr Protein Pept Sci, 2000, 1(2): 209-235.
  • 3Kolattukudy PE, Purdy RE, Maiti lB. Cutinases from fungi and pollen. Methods Enzymol, 1981, 71: 652-664.
  • 4Purdy RE, Kolattukudy PE. Hydrolysis of plant cuticle by plant pathogens. Properties of cutinase I, cutinase II, and a nonspecific esterase isolated from Fusarium solani pisi. Biochemistry, 1975, 14(13): 2832-2840.
  • 5Maiti IB, Kolattukudy PE. Prevention of fungal infection of plants by specific inhibition of cutinase. Science, 1979, 205(4405): 507-508.
  • 6Shaykh M, Soliday C, Kolattukudy PE. Proof for the production of cutinase by Fusarium solani f pisi during penetration into its host, Pisum sativum. Plant Physiol, 1977, 60(1): 170-172.
  • 7Shayk M, Kolattukudy PE. Production of a novel extracellular cutinase by the pollen and the chemical composition and ultrastructure of the stigma cuticle of Nasturtium (Tropaeolum majus). Plant Physiol, 1977, 60(6): 907-915.
  • 8Heslop-Harrison J. The physiology of the pollen grain surface. Proc R Soc Lond B Biol Sci, 1975, 190(1100): 275-299.
  • 9Pio TF, Macedo GA. Cutinase production by Fusarium oxysporum in liquid medium using central composite design. J lnd Microbiol Biotechnol, 2008, 35(1): 59-67.
  • 10Wang GY, Michailides TJ, Hammock BD, et al. Molecular cloning, characterization, and expression of a redox-responsive cutinase from Monilinia fructicola (Wint.) honey. Fungal Genet Biol, 2002, 35(3): 261-276.

二级参考文献44

  • 1毕凤珍,师俊玲,李寅,陈坚.Thermobifida fusca产角质酶摇瓶发酵条件研究[J].应用与环境生物学报,2005,11(5):608-610. 被引量:10
  • 2张守亮,陈坚,华兆哲,堵国成.角质酶产生菌Thermobifida fusca WSH03-11诱变及高产突变株发酵条件优化[J].化工进展,2006,25(5):533-537. 被引量:12
  • 3江昌俊.油菜花药中酯酶和柱头中角质酶的提纯[J].安徽农业大学学报,1996,23(1):90-93. 被引量:3
  • 4J N Etters. Cotton Preparation with Alkaline Pectinase: an Environmental Advance [J]. Textile Chem Color & Am Dyest Rep, 1999(3): 33-36.
  • 5D K Durden, J N Etters, A K Sarkar, et al. Advances in Commercial Biopreparation of Cotton with Alkaline Pectinase [J]. AATCC Review, 2001 (8): 28-30.
  • 6M M Hartzell, Y L Hsieh. Enzymatic Scouring to Improve Cotton-Fabric Wettability [J]. Textile Research Journal, 1998, 68 (4) :233- 241.
  • 7R B Waddell. Bioscouring of Cotton: Commercial Applications of Alkaline Stable Pectinase [J]. AATCC Review, 2002 (4): 28-30.
  • 8Y Li, I R Hardin. Enzymatic Scouring of Cotton: Effects on Structure and Properties [J]. Textile Chemist Colorist, 1997, 29 (8):71-76.
  • 9K Moussa Traore, G Buschle Diller. Environmentally Friendly Scouring Processes [J]. Textile Chem Color & Am Dyest Rep,2000, 32 (12): 40-43.
  • 10Usa Sangwatanaroj, Kingkamol Choonukulpong. Cotton Scouring with Pectinase and Lipase/protease/cellulase [J]. AATCC Review,2003 (3): 17-20.

共引文献27

同被引文献83

引证文献10

二级引证文献26

相关作者

内容加载中请稍等...

相关机构

内容加载中请稍等...

相关主题

内容加载中请稍等...

浏览历史

内容加载中请稍等...
;
使用帮助 返回顶部