Biosynthesis of 4-hydroxyphenylpyruvic acid from L-tyrosine using recombinant Escherichia coli cells expressing membrane bound L-amino acid deaminase

doi:10.1016/j.cjche.2017.08.009

Chinese Journal of Chemical Engineering ›› 2018, Vol. 26 ›› Issue (2): 380-385.DOI: 10.1016/j.cjche.2017.08.009

• Biotechnology and Bioengineering • 上一篇下一篇

Biosynthesis of 4-hydroxyphenylpyruvic acid from L-tyrosine using recombinant Escherichia coli cells expressing membrane bound L-amino acid deaminase

Huanru Ding^1,2, Weirui Zhao^1,2, Changjiang Lü^1,2, Jun Huang³, Sheng Hu¹, Shanjing Yao², Lehe Mei^1,2, Jinbo Wang¹, Jiaqi Mei⁴

1 School of Biotechnology and Chemical Engineering, Ningbo Institute of Technology, Zhejiang University, Ningbo 315100, China;
2 Department of Chemical and Biological Engineering, Zhejiang University, Hangzhou 310027, China;
3 School of Biological and Chemical Engineering, Zhejiang University of Science and Technology, Hangzhou 310023, China;
4 Department of Chemical Engineering, The University of Utah, Salt Lake City 84102, America

收稿日期:2017-05-17 修回日期:2017-08-14 出版日期:2018-02-28 发布日期:2018-03-16
通讯作者: Lehe Mei
基金资助:
Supported by the National Natural Science Foundation of China (31470793, 31670804), China Postdoctoral Science Foundation (2016M592003), the Natural Science Foundation of Zhejiang Province (LZ13B060002), and the General Scientific Research Project of Zhejiang Provincial Education Department (Y201432760).

Biosynthesis of 4-hydroxyphenylpyruvic acid from L-tyrosine using recombinant Escherichia coli cells expressing membrane bound L-amino acid deaminase

Huanru Ding^1,2, Weirui Zhao^1,2, Changjiang Lü^1,2, Jun Huang³, Sheng Hu¹, Shanjing Yao², Lehe Mei^1,2, Jinbo Wang¹, Jiaqi Mei⁴

1 School of Biotechnology and Chemical Engineering, Ningbo Institute of Technology, Zhejiang University, Ningbo 315100, China;
2 Department of Chemical and Biological Engineering, Zhejiang University, Hangzhou 310027, China;
3 School of Biological and Chemical Engineering, Zhejiang University of Science and Technology, Hangzhou 310023, China;
4 Department of Chemical Engineering, The University of Utah, Salt Lake City 84102, America

Received:2017-05-17 Revised:2017-08-14 Online:2018-02-28 Published:2018-03-16
Contact: Lehe Mei
Supported by:
Supported by the National Natural Science Foundation of China (31470793, 31670804), China Postdoctoral Science Foundation (2016M592003), the Natural Science Foundation of Zhejiang Province (LZ13B060002), and the General Scientific Research Project of Zhejiang Provincial Education Department (Y201432760).

摘要/Abstract

摘要： 4-Hydroxyphenylpyruvic acid (4-HPPA), a kind of α-keto acid, is an intermediate in the metabolism of tyrosine and has a wide range of application in food, pharmaceutical and chemical industry. Using amino acids as raw material to produce the corresponding α-keto acid is thought to be both economic and efficient. Among the enzymes that convert amino acid to α-keto acid, membrane bound L-amino acid deaminase (mL-AAD), which is anchored to the outer side of the cytomembrane, becomes an ideal enzyme to prepare α-keto acid since there is no cofactors needed and H₂O₂ production during the reaction. In this study, the mL-AAD from Proteus vulgaris was used to prepare whole-cell catalysts to produce 4-HPPA from L-tyrosine. The secretory efficiency of mL-AAD conducted by its own twin-arginine signal peptide (twin-arginine translocation pathway, Tat) and integrated pelB (the general secretory pathway, Sec)-Tat signal peptide was determined and compared firstly, using two pET systems (pET28a and pET20b). It was found that the Tat pathway (pET28a-mlaad) resulted in higher cell-associated mL-AAD activity and cell biomass, and was more beneficial to prepare biocatalyst. In addition, expression hosts Bl21(DE3) and 0.05 mmol·L^-1 IPTG were found to be suitable for mL-AAD expression. The reaction conditions for mL-AAD were optimized and 72.72 mmol·L^-1 4-HPPA was obtained from 100 mmol·L^-1 tyrosine in 10 h under the optimized conditions. This bioprocess, which is more eco-friendly and economical than the traditional chemical synthesis ways, has great potential for industrial application.

关键词: 4-Hydroxyphenylpyruvic acid, L-tyrosine, Membrane-bound L-amino acid deaminases, Biocatalysis, Molecular biology, Biological engineering

Abstract: 4-Hydroxyphenylpyruvic acid (4-HPPA), a kind of α-keto acid, is an intermediate in the metabolism of tyrosine and has a wide range of application in food, pharmaceutical and chemical industry. Using amino acids as raw material to produce the corresponding α-keto acid is thought to be both economic and efficient. Among the enzymes that convert amino acid to α-keto acid, membrane bound L-amino acid deaminase (mL-AAD), which is anchored to the outer side of the cytomembrane, becomes an ideal enzyme to prepare α-keto acid since there is no cofactors needed and H₂O₂ production during the reaction. In this study, the mL-AAD from Proteus vulgaris was used to prepare whole-cell catalysts to produce 4-HPPA from L-tyrosine. The secretory efficiency of mL-AAD conducted by its own twin-arginine signal peptide (twin-arginine translocation pathway, Tat) and integrated pelB (the general secretory pathway, Sec)-Tat signal peptide was determined and compared firstly, using two pET systems (pET28a and pET20b). It was found that the Tat pathway (pET28a-mlaad) resulted in higher cell-associated mL-AAD activity and cell biomass, and was more beneficial to prepare biocatalyst. In addition, expression hosts Bl21(DE3) and 0.05 mmol·L^-1 IPTG were found to be suitable for mL-AAD expression. The reaction conditions for mL-AAD were optimized and 72.72 mmol·L^-1 4-HPPA was obtained from 100 mmol·L^-1 tyrosine in 10 h under the optimized conditions. This bioprocess, which is more eco-friendly and economical than the traditional chemical synthesis ways, has great potential for industrial application.

Key words: 4-Hydroxyphenylpyruvic acid, L-tyrosine, Membrane-bound L-amino acid deaminases, Biocatalysis, Molecular biology, Biological engineering

Huanru Ding, Weirui Zhao, Changjiang Lü, Jun Huang, Sheng Hu, Shanjing Yao, Lehe Mei, Jinbo Wang, Jiaqi Mei. Biosynthesis of 4-hydroxyphenylpyruvic acid from L-tyrosine using recombinant Escherichia coli cells expressing membrane bound L-amino acid deaminase[J]. Chinese Journal of Chemical Engineering, 2018, 26(2): 380-385.

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Biosynthesis of 4-hydroxyphenylpyruvic acid from L-tyrosine using recombinant Escherichia coli cells expressing membrane bound L-amino acid deaminase

Biosynthesis of 4-hydroxyphenylpyruvic acid from L-tyrosine using recombinant Escherichia coli cells expressing membrane bound L-amino acid deaminase

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