Abstract
Trans-cinnamic acid and p-coumaric acid are valuable intermediates in the synthesis of flavonoids and are widely employed in food, flavor and pharmaceutical industries. These products can be produced by the deamination of L-phenylalanine and L-tyrosine catalyzed by phenylalanine ammonia lyase or tyrosine ammonia lyase. Phenylalanine ammonia-lyase (PAL, EC 4.3.1.5) from Rhodotorula glutinis do not exhibit strong substrate specificity and can convert both L-phenylalanine and L-tyrosine. In this study, the PAL was utilized as the whole-cell biocatalyst, and the reaction conditions were optimized, and the production of trans-cinnamic acid and p-coumaric acid of 597 mg/L and 525 mg/L were achieved with high purity (>98%).
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