Improving Soluble Expression of Tyrosine Decarboxylase from Lactobacillus brevis for Tyramine Synthesis with High Total Turnover Number

  • Mingyang Jiang
  • Guochao Xu
  • Jie Ni
  • Kai Zhang
  • Jinjun Dong
  • Ruizhi Han
  • Ye NiEmail author


The soluble expression of tyrosine decarboxylase (TDC) in heterologous host is often challenging. Here, acidic condition was found to be favorable for improving the soluble expression of TDC from Lactobacillus brevis in Escherichia coli, while addition of carbohydrates (such as glucose, arabinose, and fructose) was vital for decreasing the insoluble fraction. By simple pH control and addition of glucose, the specific activity of TDC in crude extract was enhanced to 46.3 U mg−1, 3.67-fold of that produced from LB medium. Optimization of the reaction conditions revealed that Tween-80 was effective in improving the tyramine production catalyzed by TDC, especially at high tyrosine loadings. As much as 400 mM tyrosine could be completely converted into tyramine with a substrate to catalyst ratio of 29.0 g g−1 and total turnover number of 23,300. This study provides efficient strategies for the highly soluble expression of TDC and biocatalytic production of tyramine.


Soluble expression Tyrosine decarboxylase Tyramine Glucose Tween-80 


Funding Information

The study was financially supported by the National Natural Science Foundation of China (21506073, 21776112), the Natural Science Foundation of Jiangsu Province (BK20150003, BK20171135), six talent peaks project of Jiangsu Province (2015-SWYY-008), national first-class discipline program of Light Industry Technology and Engineering (LITE2018-07), the Program of Introducing Talents of Discipline to Universities (111-2-06), and a project funded by the Priority Academic Program Development of Jiangsu Higher Education Institutions.

Compliance with Ethical Standards

Conflict of Interest

The authors declare that they have no conflicts of interest.

Supplementary material

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ESM 1 (DOCX 11450 kb)


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© Springer Science+Business Media, LLC, part of Springer Nature 2018

Authors and Affiliations

  1. 1.The Key Laboratory of Industrial Biotechnology, Ministry of Education, School of BiotechnologyJiangnan UniversityWuxiChina
  2. 2.Department of Biochemistry and Cell BiologyStony Brook UniversityStony BrookUSA

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