N-glycosylation as an effective strategy to enhance characteristics of Rhizomucor miehei lipase for biodiesel production.
Biodiesel
Loop structure
Methanol tolerance
N-glycosylation
Rhizomucor miehei lipase
Journal
Enzyme and microbial technology
ISSN: 1879-0909
Titre abrégé: Enzyme Microb Technol
Pays: United States
ID NLM: 8003761
Informations de publication
Date de publication:
Oct 2022
Oct 2022
Historique:
received:
29
01
2022
revised:
27
05
2022
accepted:
30
05
2022
pubmed:
12
6
2022
medline:
10
8
2022
entrez:
11
6
2022
Statut:
ppublish
Résumé
The construction of methanol-resistant lipases with high catalytic activity is world-shattering for biodiesel production. A semi-rational method has been constructed to enhance the properties of Rhizomucor miehei lipase with propeptide (ProRML) by introducing N-glycosylation sites in the Loop structure. The enzyme activities of the mutants N288 (1448.89 ± 68.64 U/mg) and N142 (1073.68 ± 33.87 U/mg) increased to 56.09 and 41.56 times relative to that of wild type ProRML (WT, 25.83 ± 0.73 U/mg), respectively. After incubation in 50 % methanol for 2.5 h, the residual activities of N314 and N174-1 were 95 % and 85%, which were higher than the WT (27 %). Additionally, the biodiesel yield of all mutants was increased after a one-time addition of methanol for 24 h. Among them, N288 increased the quantity of biodiesel from colza oil from 9.49 % to 88 %, and N314 increased the amount of biodiesel from waste soybean oil from 8.44% to 70%. This study provides an effective method to enhance the properties of lipase and improve its application potential in biodiesel production.
Identifiants
pubmed: 35689964
pii: S0141-0229(22)00091-6
doi: 10.1016/j.enzmictec.2022.110072
pii:
doi:
Substances chimiques
Biofuels
0
Lipase
EC 3.1.1.3
Methanol
Y4S76JWI15
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
110072Informations de copyright
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