Tailored expression of ICCM cutinase in engineered Escherichia coli for efficient polyethylene terephthalate hydrolysis.

Autor: Ma HN; Department of Chemical Engineering, National Cheng Kung University, Tainan 701, Taiwan., Hsiang CC; Department of Chemical Engineering, National Cheng Kung University, Tainan 701, Taiwan., Ng IS; Department of Chemical Engineering, National Cheng Kung University, Tainan 701, Taiwan. Electronic address: yswu@mail.ncku.edu.tw.
Jazyk: angličtina
Zdroj: Enzyme and microbial technology [Enzyme Microb Technol] 2024 Sep; Vol. 179, pp. 110476. Date of Electronic Publication: 2024 Jun 26.
DOI: 10.1016/j.enzmictec.2024.110476
Abstrakt: Enzymatic depolymerization of PET waste emerges as a crucial and sustainable solution for combating environmental pollution. Over the past decade, PET hydrolytic enzymes, such as PETase from Ideonella sakaiensis (IsPETases), leaf compost cutinases (LCC), and lipases, have been subjected to rational mutation to enhance their enzymatic properties. ICCM, one of the best LCC mutants, was selected for overexpression in Escherichia coli BL21(DE3) for in vitro PET degradation. However, overexpressing ICCM presents challenges due to its low productivity. A new stress-inducible T7RNA polymerase-regulating E. coli strain, ASIA hsp , which significantly enhances ICCM production by 72.8 % and achieves higher enzyme solubility than other strains. The optimal cultural condition at 30 °C with high agitation, corresponding to high dissolved oxygen levels, has brought the maximum productivity of ICCM and high PET-hydrolytic activity. The most effective PET biodegradation using crude or pure ICCM occurred at pH 10 and 60 °C. Moreover, ICCM exhibited remarkable thermostability, retaining 60 % activity after a 5-day reaction at 60 °C. Notably, crude ICCM eliminates the need for purification and efficiently degrades PET films.
Competing Interests: Declaration of Competing Interest The authors declare that they have no competing interests.
(Copyright © 2024 Elsevier Inc. All rights reserved.)
Databáze: MEDLINE
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