Isolation of Phenylalanine Ammonia-lyase Producing Strains and Properties of Its Enzyme
Zhiqun Liang
Abstract
Zhiqun Liang
Abstract
The yeast strain with high activity of producing phenylalanine ammonia-lyase, SA1, was screened from soil. The optimum enzyme productivity and conditions for the conversion of trans-cinnamic acid into L- phenylalanine were determined. The results showed that the production of enzyme was kept high by addition of L-phenylalanine, L-tyrosine and isoleucine, where L- tyrosine was optimum. The optimal parameters of the conversion reaction were: 2.0% trans-cinnamic acid, NH4HCO3:NH·3H2O (W:V)=4:4, pH10.6, 34℃, and the time of reaction 8h. The enzyme activity was kept stable by the addition of glycerol.
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The yeast strain with high activity of producing phenylalanine ammonia-lyase, SA1, was screened from soil. The optimum enzyme productivity and conditions for the conversion of trans-cinnamic acid into L- phenylalanine were determined. The results showed that the production of enzyme was kept high by addition of L-phenylalanine, L-tyrosine and isoleucine, where L- tyrosine was optimum. The optimal parameters of the conversion reaction were: 2.0% trans-cinnamic acid, NH4HCO3:NH·3H2O (W:V)=4:4, pH10.6, 34℃, and the time of reaction 8h. The enzyme activity was kept stable by the addition of glycerol.
Key concepts: Phenylalanine, Phenylalanine ammonia-lyase, Enzyme, Chemistry, Tyrosine, Biochemistry, Ammonia, Cinnamic acid