文献类型：期刊文献

英文题名：Biodegradation of Structurally Diverse Phthalate Esters by a Newly Identified Esterase with Catalytic Activity toward Di(2-ethylhexyl) Phthalate

作者：Huang, Han[1];Zhang, Xiao-Yan[1];Chen, Tian-Lei[1];Zhao, Yu-Lian[1];Xu, Dian-Sheng[1];Bai, Yun-Peng[1]

机构：[1]East China Univ Sci & Technol, State Key Lab Bioreactor Engn, 130 Meilong Rd, Shanghai 200237, Peoples R China

年份：2019

卷号：67

期号：31

起止页码：8548

外文期刊名：JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY

收录：;EI(收录号：20193307310963);WOS:【SCI-EXPANDED(收录号:WOS:000480498000015)】；

基金：We are grateful to the National Key Research and Development of China (2016YFA0204300), the National Natural Science Foundation of China (Nos. 21506055 and 21505044), the Natural Science Foundation of Shanghai (Nos. 18ZR1409900 and 18DZ1112703), and the Fundamental Research Funds for the Central Universities (22221818014).

语种：英文

外文关键词：Gordonia polyisoprenivorans; esterase; bis(2-ethylhexyl) phthalate; phthalate esters; biodegradation

摘要：Herein, we report a double enzyme system to degrade 12 phthalate esters (PAEs), particularly bulky PAEs, such as the widely used bis(2-ethylhexyl) phthalate (DEHP), in a one-pot cascade process. A PAE-degrading bacterium, Gordonia sp. strain 5F, was isolated from soil polluted with plastic waste. From this strain, a novel esterase (GoEst15) and a mono(2-ethylhexyl) phthalate hydrolase (GoEstM1) were identified by homology-based cloning. GoEst15 showed broad substrate specificity, hydrolyzing DEHP and 10 other PAEs to monoalkyl phthalates, which were further degraded by GoEstMl to phthalic acid. GoEst15 and GoEstM1 were heterologously coexpressed in Escherichia coli BL21 (DE3), which could then completely degrade 12 PAEs (5 mM), within 1 and 24 h for small and bulky substrates, respectively. To our knowledge, GoEst15 is the first DEHP hydrolase with a known protein sequence, which will enable protein engineering to enhance its catalytic performance in the future.