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Molecular Characterization of a Novel Family VIII Esterase with β-Lactamase Activity ( Ps EstA) from Paenibacillus sp

Molecular Characterization of a Novel Family VIII Esterase with β-Lactamase Activity ( Ps EstA) from Paenibacillus sp

Sena Kwon, Wanki Yoo, Young-Ok Kim, Kyeong Kyu Kim, T Doohun Kim

Biomolecules. 2019 Nov 26;9(12):786.

PMID: 31779208

Abstract:

Molecular information about family VIII esterases, which have similarities with class C β-lactamases and penicillin-binding proteins, remains largely unknown. In this study, a novel family VIII esterase with β-lactamase activity (PsEstA) from Paenibacillus sp. was characterized using several biochemical and biophysical methods. PsEstA was effective on a broad range of substrates including tertiary butyl acetate, glyceryl tributyrate, glucose pentaacetate, olive oil, and p-nitrophenyl esters. Additionally, PsEstA hydrolyzed nitrocefin, cefotaxime, and 7-aminocephalosporanic acid. Interestingly, two forms of immobilized PsEstA (CLEAs-PsEstA and mCLEAs-PsEstA) showed high recycling property and enhanced stability, but hybrid nanoflowers (hNFs) of PsEstA require improvement. This study provides a molecular understanding of substrate specificities, catalytic regulation, and immobilization of PsEstA, which can be efficiently used in biotechnological applications.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP60015	Glyceryl tributyrate		60-01-5	Price

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