Premium
Properties of a Newly Identified Acetyl Esterase and Its Degradation of Diisobutyl Phthalate
Author(s) -
Guan Ziran,
Dai Shuang,
Yao Qian,
Zong Wei,
Deng Zujun,
Liu Shan,
Yun Jeonyun,
Xiao Xiong,
Liu Liyang,
Li He
Publication year - 2020
Publication title -
chemistryselect
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.437
H-Index - 34
ISSN - 2365-6549
DOI - 10.1002/slct.202003720
Subject(s) - chemistry , phthalic acid , degradation (telecommunications) , esterase , enzyme , biodegradation , phthalate , salt (chemistry) , environmental pollution , dimethyl phthalate , enzyme assay , chromatography , environmental chemistry , organic chemistry , telecommunications , computer science , environmental protection , environmental science
Phthalic acid esters (PAEs) are attracting growing attention because of environmental pollution and their harms to mammals, and diisobutyl phthalate (DiBP) in PAEs is still little studied. Biodegradation is a fast, efficient and inexpensive treatment preferentially used to deal with the pollution of PAEs. In this study, the recombinant esterase Est824 was obtained by heterologous expression and purification. The optimal reaction temperature and pH of the enzyme are 40 °C and 8.0 respectively. The enzyme reserves activity above 70 % in metal ion solutions at varying concentrations and thus shows high metal ion resistance. In high‐concentration salt solutions, the enzyme activity remains above 50 %, indicating that the enzyme has strong salt tolerance. The response surface method was used to optimize the fermentation conditions. With the Box‐Behnken design, the esterase yield was 1003.54 U/L. The DiBP degradation effect of the enzyme was detected by HPLC, and the degradation rate was 100 %. Therefore, the enzyme has good industrial application prospects and may be a potential candidate for the degradation of PAEs.