[1]蒲一涛.突变株U-616葡萄糖异构酶及其固定化研究[J].深圳大学学报理工版,1997,14(4):76-80.
 Pu Yitao.Studies on D-Glucose Isomerase and Its Immobilized Enzyme of Flavobacterium Araborescens Mutant Strain U-616[J].Journal of Shenzhen University Science and Engineering,1997,14(4):76-80.
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突变株U-616葡萄糖异构酶及其固定化研究()
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《深圳大学学报理工版》[ISSN:1000-2618/CN:44-1401/N]

卷:
第14卷
期数:
1997年4期
页码:
76-80
栏目:
电子与信息科学
出版日期:
1997-12-30

文章信息/Info

Title:
Studies on D-Glucose Isomerase and Its Immobilized Enzyme of Flavobacterium Araborescens Mutant Strain U-616
作者:
蒲一涛
深圳大学应用化学系 深圳   518060
Author(s):
Pu Yitao
Dept. of Applied Chemistry Shenzhen University, Shenzhen 518060, P .R .China
关键词:
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分类号:
Q 558.9
摘要:
树状黄杆菌NRRL 11022的诱变株U-616所产葡萄糖异构酶在60~80℃范围有较高活性,最适pH7.5-8.5对其固定化异构酶的理化性质进行了实验性探索。实验结果表明:固定化酶保留了83%的游离酶的活力,在55~85℃范围有较高活性,最适pH7.0-8.060℃,底物pH值为8.0及含有1.0*10-4mol/L 钴、镁离子时,固定化异构酶的酶活达到最高。此异构酶及其固定化酶均对金属离子耐受性较强,Co2+Mg2+有激活作用,对Ca2+不敏感,热稳定性较好。树状黄杆菌变株U-616所产葡萄糖异构酶及其固定化异构酶具有较大的工业应用价值。
Abstract:
The D-glucose I so merase(GI) from flavobacterium araborescens mutant strain U-616 showed a hi gh activity at 60~80 ℃,the optimum pH was 7.5-8. 5. The immobilized enzyme showed a high activity at 55~85℃,the optimum pH was 7.0~8.0. The activity of immobilized enzyme was 83% of that of soluble enzyme. When the temperature was 60 and the pH was 8, the immobilized enzyme activity showed the highest activity in the presence of 10-4mol/L of Co2+ and Mg2+. Both Co2+  and Mg2+ enhanced enzyme activity of the soluble enzyme and the immobilied enzyme, while other metal ions, e.g. Ca2+had less inhibiting effect on activity of enzyme. Both the soluble enzyme and the immobilized enzyme had high ther-mostability.

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更新日期/Last Update: 2016-03-15