<abstract xmlns="http://www.w3.org/1999/xhtml"><p> 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 60°C 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 50°C as well as in continuous reactors operated at fl ow 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.</p></abstract>

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 60°C 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 50°C as well as in continuous reactors operated at fl ow 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.

Future Applications of Apricot (Prunus Armeniaca Kaisa) ß Galactosidase in Dairy Industry

King Abdulaziz University, Center of Excellence in Genomic and Medicine Research, Jeddah-21589, Saudi Arabia

Ibn Sina National College for Medical Studies, Department of Biochemistry, Jeddah-21418, Saudi Arabia

Universiti Kebangsaan Malaysia, School of Chemical Sciences and Food Technology, Faculty of Science and Technology, 43600 Bangi, Selangor Darul Ehsan, Malaysia

Polish Journal of Chemical Technology

This work is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 3.0 License.

The present study demonstrates the immobilization of β galactosidase from apricots (Prunus armeniaca kaisa) on an inexpensive concanavalin A layered...

Future Applications of Apricot (Prunus Armeniaca Kaisa) ß Galactosidase in Dairy Industry

Publicado en línea: 03 oct 2014

Páginas: 74 - 79

DOI: https://doi.org/10.2478/pjct-2014-0054

Palabras clave
Apricots, β galactosidase, lactose hydrolysis, dairy industries

© by Shakeel Ahmed Ansari

This work is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 3.0 License.

Future Applications of Apricot (Prunus Armeniaca Kaisa) ß Galactosidase in Dairy Industry

Publicado en línea: 03 oct 2014

Páginas: 74 - 79

DOI: https://doi.org/10.2478/pjct-2014-0054

Palabras claveApricots, β galactosidase, lactose hydrolysis, dairy industries

© by Shakeel Ahmed Ansari

This work is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 3.0 License.

Palabras clave
Apricots, β galactosidase, lactose hydrolysis, dairy industries