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Biotechnol Lett ; 41(8-9): 1059-1065, 2019 Sep.
Article in English | MEDLINE | ID: mdl-31302814

ABSTRACT

OBJECTIVES: To obtain a new acetyl esterase from Paenibacillus sp. XW-6-66 and apply the enzyme to 7-aminocephalosporanic acid (7-ACA) deacetylation. RESULTS: The acetyl esterase AesZY was identified from Paenibacillus sp. XW-6-66, and its enzymatic properties were investigated. With the putative catalytic triad Ser114-Asp203-His235, AesZY belongs to the Acetyl esterase (Aes) family which is included in the α/ß hydrolase superfamily and contains the consensus Gly-X-Ser-X-Gly motif. The maximum activity of AesZY was detected at pH 8.0 and 40 °C. AesZY was stable at different pH values ranging from 5.0 to 12.0, and was tolerant to several metal ions. Furthermore, the deacetylation activity of AesZY toward 7-ACA was approximately 7.5 U/mg, and the Kcat/Km value was 2.04 s-1 mM-1. CONCLUSIONS: Our results demonstrate the characterization of a new acetyl esterase belonging to the Aes family with potential biotechnological applications.


Subject(s)
Acetylesterase/metabolism , Cephalosporins/metabolism , Paenibacillus/enzymology , Acetylesterase/genetics , Acetylesterase/isolation & purification , Biotransformation , Enzyme Stability , Hydrogen-Ion Concentration , Kinetics , Paenibacillus/genetics , Temperature
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