苯丙氨酸解氨酶
肉桂酸
苯丙氨酸
脱氨基
化学
对香豆酸
基质(水族馆)
氨
酪氨酸
生物化学
香豆酸
生物催化
红酵母
食品科学
酶
酵母
阿魏酸
生物
催化作用
氨基酸
生态学
离子液体
作者
Yuqi Liu,Weizhuo Xu,Wei Xu
出处
期刊:Catalysts
[MDPI AG]
日期:2022-09-30
卷期号:12 (10): 1144-1144
被引量:5
标识
DOI:10.3390/catal12101144
摘要
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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