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Purification and Biochemical Characterization of a Tyrosine Phenol-lyase from Morganella morganii. | LitMetric

Purification and Biochemical Characterization of a Tyrosine Phenol-lyase from Morganella morganii.

Appl Biochem Biotechnol

Key Laboratory of Bioorganic Synthesis of Zhejiang Province, College of Biotechnology and Bioengineering, Zhejiang University of Technology, Hangzhou, 310014, People's Republic of China.

Published: September 2020

Tyrosine phenol-lyase (TPL) is a valuable and cost-effective biocatalyst for the biosynthesis of L-tyrosine and its derivatives, which are valuable intermediates in the pharmaceutical industry. A TPL from Morganella morganii (Mm-TPL) was overexpressed in Escherichia coli and characterized. Mm-TPL was determined as a homotetramer with molecular weight of 52 kDa per subunit. Its optimal temperature and pH for β-elimination of L-tyrosine were 45 °C and pH 8.5, respectively. Mm-TPL manifested strict substrate specificity for the reverse reaction of β-elimination and ortho- and meta-substituted phenols with small steric size were preferred substrates. The enzyme showed excellent catalytic performance for synthesis of L-tyrosine, 3-fluoro-L-tyrosine, and L-DOPA with a yield of 98.1%, 95.1%, and 87.2%, respectively. Furthermore, the fed-batch bioprocess displayed space-time yields of 9.6 g L h for L-tyrosine and 4.2 g L h for 3-fluoro-L-tyrosine with a yield of 67.4 g L and 29.5 g L, respectively. These results demonstrated the great potential of Mm-TPL for industrial application.

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Source
http://dx.doi.org/10.1007/s12010-020-03301-1DOI Listing

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