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Article

N-linked glycosylation of thermostable lipase from Bacillus thermocatenulatus to improve organic solvent stability.

Enzyme and microbial technology - 1 Jan 2020

Kajiwara Shota, Yamada Ryosuke, Matsumoto Takuya, Ogino Hiroyasu

Abstract excerpt

A thermostable lipase from Bacillus thermocatenulatus was glycosylated by forming the consensus sequence (-NXS/T-) for N-linked glycosylation by site-directed mutagenesis. Among the eight BTL2 mutants including the consensus sequence, six BTL2 mutants, A277 N, A290 N, Y200 N, T236 N, T238 N, and P261 N, were glycosylated. Among the six mutants, glycosylated A277 N and T236 N showed higher stability in the...

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Identifiers

PMID: 31731975
DOI: 10.1016/j.enzmictec.2019.109416

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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