Home
Resources
Publications
Process Development for Efficient Biosynthesis of L-DOPA With Recombinant Escherichia Coli Harboring Tyrosine Phenol Lyase From Fusobacterium Nucleatum

Process Development for Efficient Biosynthesis of L-DOPA With Recombinant Escherichia Coli Harboring Tyrosine Phenol Lyase From Fusobacterium Nucleatum

Xiao-Ling Tang, Xiao Liu, Hui Suo, Zhi-Chao Wang, Ren-Chao Zheng, Yu-Guo Zheng

Bioprocess Biosyst Eng. 2018 Sep;41(9):1347-1354.

PMID: 29869726

Abstract:

The tyrosine phenol lyase (TPL) catalyzed synthesis of L-DOPA was regarded as one of the most economic route for L-DOPA synthesis. In our previous study, a novel TPL from Fusobacterium nucleatum (Fn-TPL) was exploited for efficient biosynthesis of L-DOPA. However, the catalytic efficiency decreased when the reaction system expanded from 100 mL to 1 L. As such, the bioprocess for scale-up production of L-DOPA was developed in this study. To increase the stability of substrate and product, as well as decrease the by-product formation, the optimum temperature and pH were determined to be 15 °C and pH 8.0, respectively. The initial concentration of pyrocatechol, pyruvate and ammonium acetate was fixed at 8, 5 and 77 g/L and a fed-batch approach was applied with sodium pyruvate, pyrocatechol and ammonium acetate fed in a concentration of 5, 5 and 3.5 g/L, respectively. In addition, L-DOPA crystals were exogenously added to inhibit cell encapsulation by the precipitated product. The final L-DOPA concentration reached higher than 120 g/L with pyrocatechol conversion more than 96% in a 15-L stirred tank, demonstrating the great potential of Fn-TPL for industrial production of L-DOPA.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP53587294	L-Dopa-(phenyl-d3)		53587-29-4	Price

As a specialist in analytical chemical Products, Alfa Chemistry offers consumers a wealth of raw materials and a full range of technologies and services.

QUICK LINKS

HEADQUARTERS

Tel:

Fax:

Email: