Molecular Characterization of a Novel Family VIII Esterase with beta-Lactamase Activity (PsEstA) from Paenibacillus sp.
- Authors
- Kwon, Sena; Yoo, Wanki; Kim, Young-Ok; Kim, Kyeong Kyu; Kim, T. Doohun
- Issue Date
- Dec-2019
- Publisher
- MDPI
- Keywords
- PsEstA; family VIII esterase; beta-lactamase; antibiotics; immobilization
- Citation
- BIOMOLECULES, v.9, no.12
- Journal Title
- BIOMOLECULES
- Volume
- 9
- Number
- 12
- URI
- https://scholarworks.sookmyung.ac.kr/handle/2020.sw.sookmyung/2706
- DOI
- 10.3390/biom9120786
- ISSN
- 2218-273X
2218-273X
- Abstract
- Molecular information about family VIII esterases, which have similarities with class C beta-lactamases and penicillin-binding proteins, remains largely unknown. In this study, a novel family VIII esterase with beta-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.
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