Mechanism-based site-directed mutagenesis to shift the optimum pH of the phenylalanine ammonia-lyase from Rhodotorula glutinis JN-1

Mechanism-based site-directed mutagenesis to shift the optimum pH of the phenylalanine ammonia-lyase from Rhodotorula glutinis JN-1

Phenylalanine ammonia-lyase (RgPAL) from Rhodotorula glutinis JN-1 stereoselectively catalyzes the conversion of the l-phenylalanine into trans-cinnamic acid and ammonia, and was used in chiral resolution of dl-phenylalanine to produce the d-phenylalanine under acidic condition. However, the optimum...

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Bibliographic Details
Main Authors: Longbao Zhu, Li Zhou, Wenjing Cui, Zhongmei Liu, Zhemin Zhou
Format: Article
Language:English
Published: Elsevier 2014-09-01
Series:Biotechnology Reports
Subjects:
Phenylalanine ammonia-lyase
Rhodotorula glutinis JN-1
Friedel–Crafts-type mechanism
Site-directed mutagenesis
Resolution
The optimum pH
Online Access:http://www.sciencedirect.com/science/article/pii/S2215017X14000149

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