Muhammad Asif Nawaz, Afsheen Aman and Shah Ali Ul Qader
Department of Biotechnology, Shaheed Benazir Bhutto University Sheringal Dir (Upper), KPK,
Maltase is one of the catalytic proteins that regulates the hydrolytic process of maltose and releases glucose monomers. This hydrolase has several applications in food processing and pharmaceutical industries. In the current study catalytic properties of maltase was examined after immobilizing the enzyme into various synthetic (polyacrylamide) and non-synthetic (calcium alginate, agar-agar and agarose) polymers via entrapment technique. It was observed that enzyme efficiency was improved after immobilization and agar-agar matrix was found to be the most promising support for maltase in terms of immobilization yield (82.77%). Reaction time of maltase was increased from 5.0 to 10.0 minutes when enzyme was immobilized within agar-agar and calcium alginate whereas; it remained same in the case of agarose and polyacrylamide with reference to its free counterpart. It was noticed that enzyme-substrate reaction pH shifted from 6.5 to 7.0 after enzyme immobilization within agar-agar and agarose while remained same when entrapped within calcium alginate and polyacrylamide as compared to free enzyme. The optimum temperature of maltase was increased up to 50°C, 55°C, 60°C and 65°C after immobilization within calcium alginate, polyacrylamide, agarose and agar-agar matrices, respectively with reference to free enzyme (45°C). Immobilization increased the Km and decreased the Vmax values of maltase. Thermal stability of maltase was also improved after immobilization within all of the investigated supports as compared to its free counterpart. The maltase exhibited significant recycling efficiency within agar-agar with reference to other supports. In term of maltase catalytic properties and stability, agar-agar support seemed to permit better results and can be used to design a bioreactor for continuous use in different industries.
Keywords: Maltase, Immobilization, Agar-agar, Thermal stability, Bioreactor.