Conversion of trans-Cinnamic Acid to L-Phenylalanine by Phenylalanine Ammonia Lyase
Jiyoung Chang, Yang-Mo Goo, Chang‐Hoon Lee, Youn-Young Lee, Kyoung-Ja Kim
Abstract
Jiyoung Chang, Yang-Mo Goo, Chang‐Hoon Lee, Youn-Young Lee, Kyoung-Ja Kim
Abstract
The conversion of trans-cinnamic acid to phenylalanine using phenylalanine ammonia lyase (PAL) was examined. The optimum concentration of trans-cinnamic acid for the reaction was observed at 100 mM in cells and at 20 mM in cell free extracts, respectively. The production of L-phenylalanine was increased in both experiments as the concentration of ammonia was increased up to 10 M. The optimal pHs for the maximal conversion of trans-cinnamic acid to L-phenylalanine were 9.5 and 9.0 in experiments carried out with cells and with cell free extracts, respectively.
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The conversion of trans-cinnamic acid to phenylalanine using phenylalanine ammonia lyase (PAL) was examined. The optimum concentration of trans-cinnamic acid for the reaction was observed at 100 mM in cells and at 20 mM in cell free extracts, respectively. The production of L-phenylalanine was increased in both experiments as the concentration of ammonia was increased up to 10 M. The optimal pHs for the maximal conversion of trans-cinnamic acid to L-phenylalanine were 9.5 and 9.0 in experiments carried out with cells and with cell free extracts, respectively.
Key concepts: Phenylalanine, Phenylalanine ammonia-lyase, Cinnamic acid, Chemistry, Ammonia, Biochemistry, Amino acid