4.5 Article

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

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ENZYME AND MICROBIAL TECHNOLOGY
卷 132, 期 -, 页码 -

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ELSEVIER SCIENCE INC
DOI: 10.1016/j.enzmictec.2019.109416

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Lipase; N-linked glycosylation; Site-directed mutagenesis; Saccharomyces cerevisiae; Organic solvent stability

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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 presence of 25% (v/v) DMSO (74.3 and 72.8% of initial activity was remained after incubation at 45 degrees C for 20 h, respectively) than deglycosylated A277 N and T236 N (57.2 and 45.1% of initial activity was remained, respectively). These glycosylated mutants also showed higher remaining activity than wild-type BTL2 (56.0% of the initial activity were remained). Furthermore, the glycosylated mutant T236 N showed longer half-lives in the presence of 25% (v/v) ethylene glycol, DMSO, and DMF (161, 133, and 56.7 h at 45 degrees C, respectively) than deglycosylated mutant T236 N (107, 91.9, and 42.8 h, respectively). N-linked glycosylation may be a promising approach for preparing enzymes to retain their activity in the presence of organic solvents.

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