Application of nanoparticle-immobilized thermostable β-glucosidase for improving the sugarcane juice properties
2016
Agrawal, Ruchi | Verma, A.K. | Satlewal, Alok
β-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, β-glucosidase was isolated, purified, and characterized from an indigenously developed Bacillus subtilis mutant PS-5CM-UM3. It is a 56kDa protein monomer (isoelectric point of 5.6) belonging to 1 glycosyl hydrolase family. The purified β-glucosidase was immobilized on SiO2 nanoparticles (with 52% efficiency and 14.1% yield) to improve the thermostability and Michaelis constant (Km) value of β-glucosidase from 0.9 to 1.1mM. The immobilized enzyme showed improved storage stability and was reusable for up to 10cycles with 70% residual activity. β-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.In this study, β-glucosidase originally isolated and purified from an indigenously developed Bacillus subtilis mutant was immobilized on SiO2 nanoparticles. The immobilization has improved the thermostability, storage stability, and Michaelis constant (Km) value of the β-glucosidase. The immobilized β-glucosidase is now reusable for 10cycles with 70% residual activity. Further, β-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. Hence, this study provides a green and sustainable approach for the food industry to efficiently enhance the juice properties.
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