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Title 

Development of an enzymatic system for the production of dopamine from catechol, pyruvate, and ammonia

Authors 

Seung Goo LeeSeung Pyo HongMoon Hee Sung

Publisher 

Elsevier

Issue Date 

1999

Citation 

Enzyme and Microbial Technology, vol. 25, no. 0, pp. 298-302

Keywords 

DopamineTyrosine phenol-lyaseTyrosine decarboxylaseSymbiobacteriumStreptococcus faecalis

Abstract 

To produce dopamine from catechol, pyruvate, and ammonia, an enzymatic process consisting of a two-step reaction, catechol → L-DOPA → dopamine, was developed. For the first reaction step to synthesize L-DOPA, tyrosine phenol-lyase of Symbiobacterium sp. SC-1 was used successfully as a biocatalyst, resulting in the high conversion yield of 92%. Two aromatic amino acid decarboxylases, rat liver L-DOPA decarboxylase and Streptoccus faecalis tyrosine decarboxylase (TDC), were tested for the subsequent step to produce dopamine. In investigating the effect of L-DOPA concentration, a serious substrate inhibition of L-DOPA decarboxylase activity was observed at concentrations over 1 mM, while no inhibition was detected for TDC up to 40 mM L-DOPA. Therefore, the TDC of S. faecalis was selected as the biocatalyst for the second reaction step. Enzymatic conversion of L-DOPA to dopamine was carried out in a reactor controlling the reaction pH with an HCl solution containing pyridoxal 5'-phosphate, to compensate for the loss of pyridoxal 5'-phosphate by an enzyme-catalyzed side reaction, i.e. decarboxylation-dependent transamination. When the enzyme reactor was operated at 37°C for 12 h, 100 mM of L-DOPA was converted to dopamine with the conversion yield of 100%. Simultaneous reactions of tyrosine phenol-lyase and TDC were tested for direct synthesis of dopamine, but the productivity was much lower than the separated two-step reactions.

ISSN 

0141-0229

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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