Immobilization of a thermostable • -amylase on agarose and agar matrices and its application in starch stain removal

Abstract

The purified and thermostable • -amylase from soybean seeds was immobilized by entrapment on agarose and agar matrices and their catalytic properties were compared. The optimum pH of • -amylase immobilized on both matrices was 7.0. The 1% of agarose (w/v) and 4% of agar (w/v) yielded an optimum immobilization of about 75 and 77% respectively. The K m and V max values as determined from the GraphPad Prism Software was found to be 3.46 and 0.224 (for agarose) and 3.16 and 0.227 (for agar) respectively. The reusability of agarose and agar immobilized enzyme was found to be upto 5 cycles. The effect of thiol inhibitors and thiols on immobilized • -amylase had been investigated. The easy availability of the purified soybean • -amylase and the ease of its immobilization on matrices of low cost makes it suitable for further use in industrial applications. The application of the agarose and agar immobilized enzyme in removal of starch stain from clothes was assessed. © IDOSI Publications, 2011.