Mining and modification of Oryza sativa-derived squalene epoxidase for improved β-amyrin production in Saccharomyces cerevisiae.

Metabolic engineering Protein engineering Saccharomyces cerevisiae Squalene epoxidase β-Amyrin

Journal

Journal of biotechnology
ISSN: 1873-4863
Titre abrégé: J Biotechnol
Pays: Netherlands
ID NLM: 8411927

Informations de publication

Date de publication:
20 Sep 2023
Historique:
received: 07 03 2023
revised: 13 07 2023
accepted: 14 08 2023
medline: 18 9 2023
pubmed: 20 8 2023
entrez: 19 8 2023
Statut: ppublish

Résumé

β-Amyrin is a pentacyclic triterpenoid and has anti-viral, anti-bacterial and anti-inflammatory activities. The synthetic pathway of β-amyrin has been analyzed and its heterogeneous synthesis has been achieved in Saccharomyces cerevisiae. Squalene epoxidase (SQE) catalyzes the oxygenation of squalene to form 2,3-oxidosqualene and is rate-limiting in the synthetic pathways of β-amyrin. The endogenous SQE in S. cerevisiae is insufficient for high production of β-amyrin. Herein, eight squalene epoxidases derived from different plants were selected and characterized in S. cerevisiae for improved biosynthesis of β-amyrin. Among them, the squalene epoxidase from Oryza sativa (OsSQE52) showed the best performance compared to other plant-derived sources. Through protein remodeling, the mutant OsSQE52

Identifiants

pubmed: 37597655
pii: S0168-1656(23)00143-8
doi: 10.1016/j.jbiotec.2023.08.004
pii:
doi:

Substances chimiques

Squalene Monooxygenase EC 1.14.14.17
2,3-oxidosqualene 0
oxidosqualene 2Y5JJZ8E4W
Squalene 7QWM220FJH
beta-amyrin KM8353IPSO
Triterpenes 0

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

1-11

Informations de copyright

Copyright © 2023 Elsevier B.V. All rights reserved.

Déclaration de conflit d'intérêts

Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.

Auteurs

Jinling Li (J)

Key Laboratory of Medical Molecule Science and Pharmaceutical Engineering, Ministry of Industry and Information Technology, Institute of Biochemical Engineering, School of Chemistry and Chemical Engineering, Beijing Institute of Technology, Beijing 100081, China.

Shuai Wang (S)

Key Laboratory of Medical Molecule Science and Pharmaceutical Engineering, Ministry of Industry and Information Technology, Institute of Biochemical Engineering, School of Chemistry and Chemical Engineering, Beijing Institute of Technology, Beijing 100081, China.

Yinan Miao (Y)

Key Laboratory of Medical Molecule Science and Pharmaceutical Engineering, Ministry of Industry and Information Technology, Institute of Biochemical Engineering, School of Chemistry and Chemical Engineering, Beijing Institute of Technology, Beijing 100081, China.

Ya Wan (Y)

Key Laboratory of Medical Molecule Science and Pharmaceutical Engineering, Ministry of Industry and Information Technology, Institute of Biochemical Engineering, School of Chemistry and Chemical Engineering, Beijing Institute of Technology, Beijing 100081, China.

Chun Li (C)

Key Laboratory of Medical Molecule Science and Pharmaceutical Engineering, Ministry of Industry and Information Technology, Institute of Biochemical Engineering, School of Chemistry and Chemical Engineering, Beijing Institute of Technology, Beijing 100081, China; Key Laboratory for Industrial Biocatalysis, Ministry of Education, Department of Chemical Engineering, Tsinghua University, Beijing 100084, China. Electronic address: lichun@bit.edu.cn.

Ying Wang (Y)

Key Laboratory of Medical Molecule Science and Pharmaceutical Engineering, Ministry of Industry and Information Technology, Institute of Biochemical Engineering, School of Chemistry and Chemical Engineering, Beijing Institute of Technology, Beijing 100081, China. Electronic address: wy2015@bit.edu.cn.

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Classifications MeSH