Journal of Biotechnology & Biomaterials
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β-Glucosidase occurs in a variety of organisms and catalyzes the hydrolysis of aryl and alkyl β-D-Glycosides as well as glycosides with only carbohydrate moiety such as cellobiose and also cyanogenic glycosides. Here β-Glucosidase of the
Prunus armeniaca (wild apricot) was purified to 8 fold and 5.3% yield with specific activity of 281 units/mg protein. Assay conditions were optimized at 37oC as specific activity was found to be maximum. The enzyme showed maximum activity in 0.15M sodium citrate buffer of pH 6 with p-nitrophenyl β-D-Glucopyranoside (PNPG) as substrate. Kinetic properties of enzyme
have Km of 0.143 mM and Vmax of 143 μmole/mg/min using cellobiose as substrate. Stability profile of the enzyme was studied and half life of the enzyme was found to be 8 hr and 15 min during the reaction. After immobilization, the activity of the enzyme was decreased by 53%. Immobilized beads were used twice to carry out the reaction which proved the utility of immobilization.
Mohammad Asif has completed his post graduate in biotechnology and pursuing his Ph.D. from Dept. Of Biotechnology, H P University, Shimla. He
is presently working on the studies on Hydroxynitrile lyase and their application for synthesis of various cyanohydrins. He has qualified CSIR-JRF,
UGC-JRF, and GATE etc. He also worked at Bhabha Atomic Research Centre (BARC), Mumbai as research scholar. He attended several seminars,
workshops and published abstract at International conference.
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