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Article

Enhancing the thermostability of a mono- and diacylglycerol lipase from Malassizia globose by stabilizing a flexible loop in the catalytic pocket.

Enzyme and microbial technology - 1 Sept 2021

Xing Yan-Ni, Tan Jie, Wang Yonghua, Wang Jiaqi

Abstract excerpt

A lipase from Malassizia globose, named SMG1, is highly desirable for industrial application due to its substrate specificity towards mono- and diacylglycerol. To improve its thermostability, we constructed a mutant library using an error-prone polymerase chain reaction, which was screened for bo...

Topics

Basidiomycota
Enzyme Stability
Kinetics
Lipoprotein Lipase
Molecular Dynamics Simulation
Mutation
Temperature

Source

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Identifiers

PMID: 34311886
DOI: 10.1016/j.enzmictec.2021.109849

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-34311886-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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