转谷氨酰胺酶的纯化及酶学性质的分析研究论文.doc

摘　　要 转谷氨酰胺酶通过硫酸铵分级沉淀，超滤脱盐，聚乙二醇浓缩， Sephadex G-100凝胶过滤柱层析进行纯化，上述提纯步骤得到酶活回收率为27.30%，纯化倍数为10.42。经SDS检验蛋白纯度，得到单一区带，并得出转谷氨酰胺酶的相对分子质量为3.8?104。 对转谷氨酰胺酶酶学性质进行研究，得到该酶的最适反应温度为40℃，最适pH为6.0，该酶的温度稳定范围在35℃～45℃，pH稳定范围在5.0～7.0，Ca2+、Mg2+、Ba2+对转谷氨酰胺酶的活性几乎没有影响，而Fe3+、Cu2+、Zn2+ 抑制转谷氨酰胺酶的活性。 关键词：转谷氨酰胺酶；分离纯化； 酶学性质 Abstract The transgulaminase was purified using saturation of ammonium sulfate, ultrafiltering, PEG-2000 concentrating and Sephadex G-100, the resuluts showed that a 10.42 fold purification of alliinase was obtained, and recovery was 27.30% .The apparent purity was examined by SDSand the molecular mass of MTG was 3.8?104. The properties of the transgulaminase were studied. The optimal temperature and pH were 40℃ and 6.0 ,respectively. The transgulaminase was stable below 45℃ and within pH 5.0～7.0 .Metal ions of Ca2+、Mg2+and Ba2+ had little effect on the activity of MTG, but Fe3+ 、Cu2+ and Zn2+ Key Words：transgulaminase；purification；properties 目 录 TOC \o 1-3 \h \z \u HYPERLINK \l _Toc264145388 摘　　要 PAGEREF _Toc264145388 \h I HYPERLINK \l _Toc264145389 Abstract PAGEREF _Toc264145389 \h II HYPERLINK \l _Toc264145390 1 绪 论 PAGEREF _Toc264145390 \h 1 HYPERLINK \l _Toc264145391 1.1 转谷氨酰胺酶概述 PAGEREF _Toc264145391 \h 1 HYPERLINK \l _Toc264145392 1.1.1 转谷氨酰胺酶性能及分类 PAGEREF _Toc264145392 \h 1 HYPERLINK \l _Toc264145393 1.1.2 转谷氨酰胺酶的研究现状 PAGEREF _Toc264145393 \h 2 HYPERLINK \l _Toc264145394 1.1.3 转谷氨酰胺酶的生产状况 PAGEREF _Toc264145394 \h 3 HYPERLINK \l _Toc264145395 1.2 转谷氨酰胺酶的在食品上的应用 PAGEREF _Toc264145395 \h 4 HYPERLINK \l _Toc264145396 1.2.1 转谷氨酰胺酶在肉制品加工中的应用 PAGEREF _Toc264145396 \h 4 HYPERLINK \l _Toc264145397 1.2.2 转谷氨酰胺酶在乳品加工中的应用 PAGEREF _Toc264145397 \h 4 HYPERLINK \l _Toc264145398 1.2.3 转谷氨酰胺酶在水产品加工中的应用 PAGEREF _Toc264145398 \h 5 HYPERLINK \l _Toc264145399 1.2.4 转谷氨酰胺酶在大豆产品加工中的应用 PAGEREF _Toc264145399 \h 5 HYPERLINK \l _Toc264145400 1.2.5 转谷氨酰胺酶在人造产品加工中的应用 PAGEREF _Toc264145400 \h 5 HYPERLINK \l _Toc264145401 1.3 本课题的来源及研究的意义 PAGEREF _Toc264145401