来自青霉属TS-622菌株的甘油氧化酶的纯化及特性分析。

Purification and characterization of a glycerol oxidase from Penicillium sp. TS-622.

作者信息

Lin S F, Chiou C M, Tsai Y C

机构信息

Department of Bioengineering, Tatung Institute of Technology, Taipei, Taiwan, Republic of China.

出版信息

Enzyme Microb Technol. 1996 Apr;18(5):383-7. doi: 10.1016/0141-0229(95)00154-9.

DOI:10.1016/0141-0229(95)00154-9

PMID:8882006

Abstract

A novel extracellular glycerol oxidase was purified 39-fold from wheat bran culture of a soil-isolated Penicillium strain TS-622 with an overall yield of 3%. The addition of Triton X-100 into the extraction buffer improved the extraction yield by 90 times, indicating that the enzyme is bound to the cell surface. The molecular weight of this enzyme was 400,000 as determined by size-exclusion high-performance liquid chromatography. The optimum pH was from 6 to 7 and the optimum temperature was 45 degrees C. This enzyme showed high specificity toward dihydroxyacetone and glycerol. It was inhibited by KCN, NaN3, and hydroxylamine.

摘要

从土壤分离的青霉菌株TS-622的麦麸培养物中纯化出一种新型细胞外甘油氧化酶，纯化倍数为39倍，总产率为3%。在提取缓冲液中添加Triton X-100可使提取产率提高90倍，表明该酶与细胞表面结合。通过尺寸排阻高效液相色谱法测定，该酶的分子量为400,000。最适pH为6至7，最适温度为45℃。该酶对二羟基丙酮和甘油具有高度特异性。它受到KCN、NaN3和羟胺的抑制。