Preparation and properties of Rhizopus Oryzae lipase immobilized using an adsorption-crosslinking method

Abstract

The aim was to develop an enzyme immobilization method for Rhizopus oryzae lipase to improve its acidolysis activity and stability. Lipase was adsorbed into NKA-9 resin and then crosslinked with glutaraldehyde as a crosslinker. The optimum conditions obtained using the response surface methodology were as follows: 34.6 mg lipase/100 mg support, 4.1 h of adsorption time, 45°C, pH 6.8, 0.5% glutaraldehyde concentration, and 2.5 h of crosslinking time. The acidolysis activity of the immobilized lipase was 31.78%, the free lipase activity was only 11.02%. The immobilized lipase showed better performance, such as higher acidolysis activity, better pH tolerance and temperature stability, enhanced storage stability, and improved reusability.