Godwin Basil D’Cunha
Cape Breton University, Canada
Title: Phenylalanine/Tyrosine ammonia lyase enzyme catalyzed synthesis of the methyl ester of parahydroxycinnamic acid and its potential antibacterial activity
Biography
Biography: Godwin Basil D’Cunha
Abstract
Enzymes are molecular machines that are vital to sustain life in biological systems including humans. Enzyme catalysis has revolutionized manufacturing processes in pharmaceutical, chemical and food industries. We have shown that Phenylalanine Ammonia Lyase (PAL) enzyme functions efficiently in both aqueous and non-aqueous media. We have also successfully used PAL in the production of L-phenylalanine (L-Phe) and L-phenylalanine methyl ester (L-PM), fine chemicals with very high demand in chemical and food industries. Recently, we have successfully demonstrated Phenylalanine/tyrosine ammonia lyase (PTAL) catalyzed transformation of L-tyrosine methyl ester (L-TM) to para-hydroxycinnamic acid methyl ester (p-HCAM) and its antibiotic activity. Different conditions including pH, temperature, speed of agitating reaction milieu, enzyme concentration, and substrate concentration were optimized for the maximal formation of p-HCAM. The product (p-HCAM) was confirmed using Nuclear Magnetic Resonance spectroscopy (NMR). Fourier Transform Infra-Red spectroscopy (FTIR) was carried out to rule out potential hydrolysis of p-HCAM during overnight incubation. Potential antibacterial activity of p-HCAM was tested against several strains of Gram-positive and Gram-negative bacteria. In addition to using p-HCAM as an antibacterial agent (perhaps as a topical treatment agent or disinfectant), we also intend testing its potential applications as a food additive (inclusion in canned foods to prevent microbial contamination).