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

doi:10.1016/j.enzmictec.2019.109416

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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...

Topics

Bacillus
Bacterial Proteins
Enzyme Stability
Glycosylation
Lipase
Mutagenesis, Site-Directed
Mutation
Organic Chemicals
Solvents

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