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Application of nanoparticle-immobilized thermostable ß-glucosidase for improving the sugarcane juice properties

-glucosidases are among the key enzymes for juice and beverage industries. They are responsible for the release of aromatic compounds in fruits and fermentation products. In this study, -glucosidase was isolated, purified, and characterized from an indigenously developed Bacillus subtilis mutant PS-5CM-UM3. It is a 56 kDa protein monomer (isoelectric point of 5.6) belonging to 1 glycosyl hydrolase family. The purified -glucosidase was immobilized on SiO2 nanoparticles (with 52% efficiency and 14.1% yield) to improve the thermostability and Michaelis constant (Km) value of -glucosidase from 0.9 to 1.1 mM. The immobilized enzyme showed improved storage stability and was reusable for up to 10 cycles with 70% residual activity. -glucosidase treatment in sugarcane juice elevated the phenolics content with about 2.6 folds and 2.4 folds increase in p-hydroxy benzoic acid (PHBA) and gallic acid, respectively. The results show that recyclable immobilized enzyme system is a novel green approach for improving the sugarcane juice properties

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