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Future applications of apricot (Prunus armeniaca kaisa) ß galactosidase in dairy industry

Ansarin S. A, Satar R., Zaidi S. K., Khan M. J., Naseer M. I., Al-Qahtani M. H., Maskat M. Y.

Polish Journal of Chemical Technology

2014

Vol. 16, nr 3

74--79

The present study demonstrates the immobilization of β galactosidase from apricots (Prunus armeniaca kaisa) on an inexpensive concanavalin A layered cellulose-alginate hybrid gel. Immobilized β galactosidase retained 78% of the initial activity after crosslinking by glutaraldehyde. It exhibited greater fraction of activity at both acidic and basic pH, and showed broad spectrum temperature optimum as compared to free enzyme. Moreover, immobilized enzyme exhibited higher thermal stability at 60oC and retained 80% of the original enzyme activity in presence of 3% galactose. The crosslinked immobilized enzyme showed improved hydrolysis of lactose from milk and whey in batch processes at 50oC as well as in continuous reactors operated at flow rate of 20 mL/h and 30 mL/h even after one month. Moreover, crosslinked adsorbed β galactosidase retained 76% activity even after its sixth repeated use, thereby promoting its use for lactose hydrolysis in various dairy products even for longer durations.