Enhancement of phenyllactic acid biosynthesis by recognition site replacement of D-lactate dehydrogenase from Lactobacillus pentosus

被引：24
|
作者：
Zhu, Yibo [1 ,2 ]
Hu, Fagen [1 ,2 ,3 ]
Zhu, Yingyue [1 ,2 ]
Wang, Limei [1 ,2 ]
Qi, Bin [1 ,2 ]
机构：
[1] Changshu Inst Technol, Sch Biotechnol & Food Engn, Changshu 215500, Jiangsu, Peoples R China
[2] Changshu Inst Technol, Key Lab Food & Biotechnol Suzhou, Changshu 215500, Jiangsu, Peoples R China
[3] Soochow Univ, Sch Biol & Basic Med Sci, Suzhou 215123, Jiangsu, Peoples R China
来源：
BIOTECHNOLOGY LETTERS | 2015年 / 37卷 / 06期
基金：
中国国家自然科学基金;
关键词：
D-Lactate dehydrogenase; 3-Phenyllactic acid; Phenylpyruvic acid; Recognition site residue replacement; Whole-cell transformation; PHENYLPYRUVIC ACID; BIOTRANSFORMATION; CONVERSION; SUBSTRATE; SPECTRUM; FORMATE;
D O I：
10.1007/s10529-015-1778-4
中图分类号：
Q81 [生物工程学（生物技术）]; Q93 [微生物学];
学科分类号：
071005 ; 0836 ; 090102 ; 100705 ;
摘要：
The Tyr52 residue of d-lactate dehydrogenase (d-LDH) from Lactobacillus pentosus was replaced with small hydrophobic residues and overexpressed in E. coli BL21 (DE3) to enhance 3-phenyllactic acid (PLA) synthesis by whole-cell catalyst. Escherichia coli pET-28a-d-ldh produced 12.2 g PLA l(-1) in 3 h, with a molar conversion rate of 61 %, while E. coli pET-28a-d-ldh (Y52V) produced 15.6 g PLA l(-1), with a molar conversion rate of 77 %. This study demonstrates the feasibility of using engineered E. coli for PLA production from phenylpyruvate (PPA) and showed that site-directed mutagenesis of d-ldh markedly improved PLA yield and substrate conversion rate. This biocatalytic system is a promising platform for PLA production from PPA.
引用
收藏
页码：1233 / 1241
页数：9
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