Covalent immobilization of glucoamylase enzyme onto chemically activated surface of κ-carrageenan

• DOI: 10.1186/s42269-019-0148-0
• Publication Date: 2019-06-25T15:02:46Z
• Authors: Mohamed E. Hassan; Qingyu Yang; Zhigang Xiao
• Keywords: Glutaraldehyde; Polyethylenimine

Glucoamylase enzyme is one of the most important enzymes. It catalyzes hydrolysis starch into soluble sugars. was covalently immobilized onto κ-carrageenan gel beads after activation by using polyethylenimine (PEI) followed glutaraldehyde (GA). All parameters in process were studied. The shows enhancement temperature profile as optimum for free 60 °C, and it becomes 60–80 °C that means broader range also stability acidic conditions more than enzyme. apparent Km enzyme, 147.46 mM, higher one, 110 mM maximum reaction velocity (Vmax) values decreased from 2.28 to 1.11 μmol min−1. can be reused kept its activity (100%) till 11 successive cycles. immobilization steps characterized FTIR SEM. These results confirm economic biotechnical benefits immobilization, particularly with regard number reuses, which open possibility different industrial applications.