Stenotrophomonas maltophilia HS1 exhibits l-amino acid ester hydrolase (SmAEH) activity, which can synthesize dipeptides such as Ile-Trp, Val-Gly, and Trp-His from the corresponding amino acid methyl esters and amino acids. The gene encoding SmAEH was cloned and expressed in Escherichia coli and was purified and characterized. SmAEH shared 77% sequence identity with a known amino acid ester hydrolase (AEH) from Xanthomonas citri, which belongs to a class of β-lactam antibiotic acylases. The thermal stability of SmAEH was evaluated using various mathematical models to assess its industrial potential. First-order kinetics provided the best description for the inactivation of the enzyme over a temperature range of 35-50 °C. Decimal reduction time ranged from 212.76 to 3.44 min, with a z value of 8.06 °C, and the deactivation energy was 204.1 kJ mol-1.
Keywords: Stenotrophomonas maltophilia HS1; cloning; inactivation kinetics; l-amino acid ester hydrolase; purification.