Homology analysis of 35 β-glucosidases in Oenococcus oeni and biochemical characterization of a novel β-glucosidase BGL0224.
Biochemistry
Evolution
Heterologous expression
Oenococcus oeni
β-Glucosidase
Journal
Food chemistry
ISSN: 1873-7072
Titre abrégé: Food Chem
Pays: England
ID NLM: 7702639
Informations de publication
Date de publication:
01 Jan 2021
01 Jan 2021
Historique:
received:
06
03
2020
revised:
07
07
2020
accepted:
13
07
2020
pubmed:
28
7
2020
medline:
15
12
2020
entrez:
26
7
2020
Statut:
ppublish
Résumé
β-Glucosidases play an important role in food industry. Oenococcus oeni are typical lactic acid bacteria that initiate malolactic fermentation of wines. 35 β-glucosidases from O. oeni were selected and their conserved domains and evolutionary relationships were further explored in this study. The homology analysis results indicated that 35 β-glucosidases were basically derived from GH1 and GH3 family. A novel β-glucosidase was successfully expressed and characterized. The recombinant protein, referred to as BGL0224, consisted of a total 480 amino acids with an apparent molecular weight of 55.15 kDa and was classified as GH1 family. It achieved the highest activity at pH 5.0 and 50 °C. The activity and stability were significantly increased when 12% ethanol was supplemented to the enzyme. Using p-NPG as substrate, the K
Identifiants
pubmed: 32711276
pii: S0308-8146(20)31455-2
doi: 10.1016/j.foodchem.2020.127593
pii:
doi:
Substances chimiques
Recombinant Proteins
0
Ethanol
3K9958V90M
beta-Glucosidase
EC 3.2.1.21
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
127593Informations de copyright
Copyright © 2020 Elsevier Ltd. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.