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Characterization of immobilized tyrosinase - an enzyme that is stable in organic solvent at 100 degrees C

文献类型： 外文期刊

作者： Wu, Lidong 1 ; Rathi, Brijesh 2 ; Chen, Yi 2 ; Wu, Xiuhong 2 ; Liu, Huan 1 ; Li, Jincheng 1 ; Ming, Anjie 3 ; Han, Gang 1 ;

作者机构： 1.Chinese Acad Fishery Sci, Minist Agr, Key Lab Control Qual & Safety Aquat Prod, Beijing 100141, Peoples R China

2.MIT, Dept Chem, Cambridge, MA 02139 USA

3.Chinese Acad Sci, Inst Microelect, Smart Sensing R&D Ctr, Beijing 100029, Peoples R China

4.Univ Delhi, Hansraj Coll, Lab Translat Chem & Drug Discovery, Dept Chem, Delhi 110007, India

期刊名称：RSC ADVANCES （ 影响因子：3.361； 五年影响因子：3.39 ）

ISSN： 2046-2069

年卷期： 2018 年 8 卷 69 期

页码：

收录情况： SCI

摘要： Tyrosinase is a copper-containing enzyme present in plant and animal tissues, which catalyzes the production of melanin and other pigments. In organic solvent, tyrosinase can convert N-acetyl-l-tyrosine ethyl ester (insoluble in aqueous) to a derivative of l-dopamine (a drug used for the treatment of Parkinson's disease). Thus, the performances of tyrosinase in organic solvent have attracted scientific attention since 1980. In this work, we investigated the stability of immobilized tyrosinase at high temperature in anhydrous organic solvent. Triethylaminoethyl cellulose (TEAE-Cellulose) performed the best out of six immobilization platforms. The dry immobilized tyrosinase became extremely thermostable in organic solvent, and the half-life of the dry immobilized tyrosinase in organic solvent is strongly related to the polarity of the organic solvent than their logP value. The immobilized tyrosinase loses its activity instantaneously in aqueous solution at 100 degrees C, but it keeps enzymatic activity within 10 min in hydrophilic methanol and over one month in hydrophobic hexane (logP: 4.66, non-polar) even incubating at 100 degrees C. This research provides valuable information for the design of new biocatalysts.

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