Thermostabilization of Naringinase From<i>Penicillium Decumbens</i>By Proteins in Solution and Immobilization on Insoluble Proteins

Abstract

Thermostabilization of α-rhamnosidase in Penicillium decumbens naringinase at pH 3.5 was observed in the following cases: a) increasing the concentration of the enzyme solutions; b) adding a protein such as bovine serum albumin to the solution; c) cross-linking the protein in solution with glutaraldehyde; d) immobilizing the enzyme on protein rich supports with glutaraldehyde as a bifunctional reagent. Papain treated fibroin of Bombix mori silk was the support that gave greatest stabilization, followed by keratins from bovine horn and papain treated sheep wool, and collagen (Calf hide powder). Bovine horn and hide powder showed more substrate and product adsorption than the other supports. The performance of the silk and wool immobilized enzyme was tested by successive hydrolysis of naringin suspensions.