Purification and characterization of an intracellular esterase from a Fusarium species capable of degrading dimethyl terephthalate
Purification and characterization of an intracellular esterase from a Fusarium species capable of degrading dimethyl terephthalate
复制标题
能够降解对苯二甲酸二甲酯的镰刀菌胞内酯酶的纯化和表征
DOI：
10.1016/j.procbio.2012.01.015
复制
发表时间：
2012-05-01
影响因子：
4.4
通讯作者：
Vrijmoed, L. L. P.
中科院分区：
文献类型：
--
作者：
Luo, Zhu-Hua;Wu, Yi-Rui;Vrijmoed, L. L. P.
酯酶是微生物降解邻苯二甲酸酯（PAEs）的关键酶。在这项研究中，从沿海沉积物真菌Fusarium sp. DMT-5-3中纯化了一种细胞内酯酶，该酶能够利用对苯二甲酸二甲酯（DMT）作为底物。纯化后的酶是由两个相同的亚基组成的聚合蛋白，分子量约为84 kDa。该酶在50℃时酯酶活性最高，30℃以下酯酶活性稳定，最适pH为8.0，在6.0 ~ 10.0之间酯酶活性稳定。Cr3+、Hg2+、Cu2+、Zn2+、Ni2+和Cd2+抑制了酯酶活性。底物特异性分析表明，该酶对DMT的水解具有特异性，但对邻苯二甲酸二甲酯（DMPEs）或邻苯二甲酸一甲酯（MMPEs）的其他异构体没有影响。这些发现表明，镰刀菌产生的邻苯二甲酸酯酯酶DMT-5-3是一种可诱导且独特的酯酶，参与了DMPEs的两个羧酸酯键的水解。(C) 2012 Elsevier Ltd.版权所有。
Esterase is the key enzyme involved in microbial degradation of phthalate esters (PAEs). In this study, an intracellular esterase was purified from a coastal sediment fungus Fusarium sp. DMT-5-3 capable of utilizing dimethyl terephthalate (DMT) as a substrate. The purified enzyme is a polymeric protein consisting of two identical subunits with a molecular mass of about 84 kDa. The enzyme showed a maximum esterase activity at 50 degrees C and was stable below 30 degrees C. The optimal pH was 8.0 and the enzyme was stable between pH 6.0 and 10.0. The esterase activity was inhibited by Cr3+, Hg2+, Cu2+, Zn2+, Ni2+, and Cd2+. Substrate specificity analysis showed that the enzyme was specific to DMT hydrolysis, but had no effect on other isomers of dimethyl phthalate esters (DMPEs) or monomethyl phthalate esters (MMPEs). These findings suggest that the phthalate esterase produced by Fusarium sp. DMT-5-3 is inducible and distinctive esterases involved in hydrolysis of the two carboxylic ester linkages of DMPEs. (C) 2012 Elsevier Ltd. All rights reserved.