Characterization and Thermal Denaturation Kinetic Analysis of Recombinant l‑Amino Acid Ester Hydrolase from Stenotrophomonas maltophilia

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...

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Bibliographic Details
Published in:Journal of agricultural and food chemistry 2018-10, Vol.66 (42), p.11064-11072
Main Authors: Hossain, Md Saddam, Tanaka, Takahiro, Hayashi, Junji, Takagi, Kazuyoshi, Takeda, Yoichi, Wakayama, Mamoru
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Amino Acids - chemistry
Carboxylic Ester Hydrolases - genetics
Carboxylic Ester Hydrolases - metabolism
Cloning, Molecular
Dipeptides - chemical synthesis
Enzyme Stability
Escherichia coli
Esters - chemistry
Gene Expression
Hydrogen-Ion Concentration
Kinetics
Stenotrophomonas maltophilia - enzymology
Temperature
Thermodynamics
Xanthomonas - enzymology
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Summary: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.
ISSN:0021-8561
1520-5118
DOI:10.1021/acs.jafc.8b04573