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Bioconversion of trans-cinnamic acid to L-phenylalanine by Rhodotorula sp.

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Gientka I. , Blazejak S. , Duszkiewicz-Reinhard W.

2006

nr 2

117-129

The synthesis of the aromatic amino acid L-phenylalanine has received considerable attention in recent years due to its increasing importance as precursor to the dipeptide sweetener aspartame. Phenylalanine ammonia lyase (PAL), which occurs in yeast, catalyzes the nonoxidative deamination of L-Phe to trans-cinnamic acid (tCA), has industrial application in the synthesis of L-Phe. Superior producers of PAL are Rhodotorula sp. PAL is induced in yeast cell by the presence of L-Phe, while glucose represses PAL synthesis. Different additives and conditions during inducing PAL: permeabilizing, reducing and stabilization agents, as well as pH and temperature during bioconversion targeting to higher productivity of L-Phe were discussed.