摘要
酯酶(esterase,EC3.1.1.1)在食品工业应用广泛。裂褶菌(Schizophyllum commune)ZM37.8的发酵液经85%饱和度的硫酸氨沉淀、DEAE Cellulose52处理后分离纯化得到一种酯酶,该酶分子量大小约为41.2ku;最适反应温度为50℃,70℃保温30min酶活保留70%,有较好的热稳定性;最适作用pH为6.4,pH在5.4～7.4之间较稳定,有较好的耐酸性;Co2+、Cu2+、Zn2+、Li+、Hg2+对酯酶有强烈的抑制作用,而Mn2+、Ca2+和Fe3+对其的促进作用明显;该酯酶属于无底物特异性的非特异性酯酶。酶学性质研究表明该酯酶在食品工业有良好的应用前景。
Esterase （esterase,EC3.1.1.1） are of great commercial importance due to their usage in food industry. A esterase was separated from Schizophyllum commun ZM37,8 after steps of electrophoretic homogeneity by successive ammonium sulfate with 85 % saturation precipitation, DEAE Cellulose 52 ion-exchange chromatography.Based on SDS-PAGE analysis, the molecular weight of the purified esterase was calculated to be approxi mately 41.2 ku in monomeric form. The pure enzyme had an optimum pH of 6.4, it was stable between pH 5.4-7.4; The esterase had an optimum temperature of 50 ℃,about 70 % of the enzyme activity was retained at 70 ℃ for 30min ;Esterase activity was strongly inhibited by Co^2＋, Cu^2＋, Zn^2＋, Li^＋and Hg^2＋, activity was increased by Mn^2＋,Ca^2＋ and Fe^3＋. The enzyme was not a specificity of the hydrolysis substrates of esterase.Initial characterization of the purified enzyme suggested that it is a potential candidate for food industry.
出处
《食品研究与开发》
CAS
北大核心
2007年第8期29-32,共4页
Food Research and Development
关键词
酯酶
裂褶菌
酶纯化
酶学特性
esterase
Schizophyllum commune
purification of enzyme
enzyme properties
