酿酒酵母可溶性转化酶与细胞壁转化酶稳定性的比较研究

Aleksandra Margetić, Z. Vujčić
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引用次数: 13

摘要

酿酒酵母是酵素转化酶最重要的来源。它主要用作食品工业中的可溶性或固定化酶。在酵母菌中,最多的转化酶位于质周间隙。本研究从酵母酿酒酵母细胞中分离出可溶性酶和细胞壁转化酶(CWI)两种酶。两种形式的酶表现出相同的最适温度(60℃)、最适pH值和动力学参数。这些生物催化剂在热稳定性、尿素稳定性和甲醇稳定性方面存在显著差异。60°C时,CWI的半衰期是可溶性酶的1.7倍,70°C时,CWI的半衰期是可溶性酶的8.7倍。在8 M尿素溶液中孵育2小时后,可溶性转化酶和CWI分别保持其初始活性的10%和60%。两种酶在30%和40%甲醇中孵育22小时,可溶性转化酶完全失活,而CWI在实验误差范围内改变了其活性。因此,可溶性转化酶和CWI并没有表现出实质性的差异,但CWI在一些典型的蛋白质变性剂中表现出更好的热稳定性和稳定性。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Comparative study of stability of soluble and cell wall invertase from Saccharomyces cerevisiae
ABSTRACT Yeast Saccharomyces cerevisiae is the most significant source of enzyme invertase. It is mainly used in the food industry as a soluble or immobilized enzyme. The greatest amount of invertase is located in the periplasmic space in yeast. In this work, it was isolated into two forms of enzyme from yeast S. cerevisiae cell, soluble and cell wall invertase (CWI). Both forms of enzyme showed same temperature optimum (60°C), similar pH optimum, and kinetic parameters. The significant difference between these biocatalysts was observed in their thermal stability, stability in urea and methanol solution. At 60°C, CWI had 1.7 times longer half-life than soluble enzyme, while at 70°C CWI showed 8.7 times longer half-life than soluble enzyme. After 2-hr of incubation in 8 M urea solution, soluble invertase and CWI retained 10 and 60% of its initial activity, respectively. During 22 hr of incubation of both enzymes in 30 and 40% methanol, soluble invertase was completely inactivated, while CWI changed its activity within the experimental error. Therefore, soluble invertase and CWI have not shown any substantial difference, but CWI showed better thermal stability and stability in some of the typical protein-denaturing agents.
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