Structural and Biochemical Insights into Bis(2-hydroxyethyl) Terephthalate Degrading Carboxylesterase Isolated from Psychrotrophic Bacterium Exiguobacterium antarcticumopen access
- Authors
- Hwang, Jisub; Yoo, Wanki; Shin, Seung Chul; Kim, Kyeong Kyu; Kim, Han-Woo; Do, Hackwon; Lee, Jun Hyuck
- Issue Date
- Aug-2023
- Publisher
- MDPI
- Keywords
- carboxylesterases; Exiguobacterium antarcticum; biocatalyst
- Citation
- INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES, v.24, no.15
- Journal Title
- INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
- Volume
- 24
- Number
- 15
- URI
- https://scholarworks.sookmyung.ac.kr/handle/2020.sw.sookmyung/151684
- DOI
- 10.3390/ijms241512022
- ISSN
- 1661-6596
1422-0067
- Abstract
- This study aimed to elucidate the crystal structure and biochemically characterize the carboxylesterase EaEst2, a thermotolerant biocatalyst derived from Exiguobacterium antarcticum, a psychrotrophic bacterium. Sequence and phylogenetic analyses showed that EaEst2 belongs to the Family XIII group of carboxylesterases. EaEst2 has a broad range of substrate specificities for short-chain p-nitrophenyl (pNP) esters, 1-naphthyl acetate (1-NA), and 1-naphthyl butyrate (1-NB). Its optimal pH is 7.0, losing its enzymatic activity at temperatures above 50 & DEG;C. EaEst2 showed degradation activity toward bis(2-hydroxyethyl) terephthalate (BHET), a polyethylene terephthalate degradation intermediate. We determined the crystal structure of EaEst2 at a 1.74 & ANGS; resolution in the ligand-free form to investigate BHET degradation at a molecular level. Finally, the biochemical stability and immobilization of a crosslinked enzyme aggregate (CLEA) were assessed to examine its potential for industrial application. Overall, the structural and biochemical characterization of EaEst2 demonstrates its industrial potency as a biocatalyst.
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