Characterization of a d‐Lactate Dehydrogenase from Lactobacillus fermentumJN248 with High Phenylpyruvate Reductive Activity

• Autores: Lixia Chen, Yajun Bai, Tai‐Ping Fan, Xiaohui Zheng, Yujie Cai
• Localización: Journal of food science, ISSN 0022-1147, Vol. 82, Nº 10, 2017, págs. 2269-2275
• Idioma: inglés
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• Resumen

  • Phenyllactic acid (PLA) is a novel antimicrobial compound. A novel NADH‐dependent d‐lactate dehydrogenase (d‐LDH), named as LF‐d‐LDH0653, with high phenylpyruvate (PPA) reducing activity was isolated from Lactobacillus fermentumJN248. Its optimum pH and temperature were 8.0 and 50 °C, respectively. The Michaelis–Menten constant (Km), turnover number (kcat), and catalytic efficiency (kcat/Km) for NADH were 1.20 mmol/L, 67.39 s−1, and 56.16 (mmol/L)−1s−1, respectively. The (Km), (kcat), and (kcat/Km) for phenylpyruvate were 1.68 mmol/L, 122.66 s−1, and 73.01 (mmol/L)−1s−1, respectively. This enzyme can catalyze phenylpyruvate and the product presented excellent optical purity (enantioselectivity >99%). The results suggest that LF‐d‐LDH0653 is a promising biocatalyst for the efficient synthesis of optically pure d‐PLA. A novel d‐LDH with phenylpyruvate reducing activity has been isolated and identified. It could be used as a reference for improving the production of optically pure d‐PLA. d‐PLA has a potential for application as antimicrobial an agent in dairy industry and baking industry, pharmaceutical agent in medicine and cosmetics.