Characterization of a GH3 halophilic ß-glucosidase from Pseudoalteromonas and its NaCl-induced activity toward isoflavones.
Int J Biol Macromol
; 164: 1392-1398, 2020 Dec 01.
Article
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| MEDLINE
| ID: mdl-32763400
ABSTRACT
A novel ß-glucosidase gene was isolated from Pseudoalteromonas sp. GXQ-1 and heterologously expressed in Escherichia coli. The activity of the encoded enzyme, PABGL, toward p-nitrophenyl-ß-D-glucopyranoside was increased 8.74-fold by the presence of 3 M NaCl relative to the absence of added NaCl. PABGL hydrolyzed a variety of soy isoflavone substrates. For the conversion of daidzin to daidzein, the production rate was 1.44 mM/h. The addition of NaCl enhanced the hydrolytic activity of PABGL toward daidzin and genistein; the maximum activation by NaCl was 3.48- and 6.79-fold, respectively. This is the first report of a halophilic ß-glucosidase from Pseudoalteromonas spp., and represents the ß-glucosidase with the highest multiple of activation by NaCl. PABGL exhibits strong potential for applications in food processing and industrial production.
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MEDLINE
Asunto principal:
Cloruro de Sodio
/
Beta-Glucosidasa
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Pseudoalteromonas
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Isoflavonas
Idioma:
En
Revista:
Int J Biol Macromol
Año:
2020
Tipo del documento:
Article