Immobilization and stabilization of α-galactosidase on Sepabeads EC-EA and EC-HA.

α-Galactosidase from tomato has been immobilized on Sepabead EC-EA and Sepabead EC-HA, which were activated with ethylendiamino and hexamethylenediamino groups, respectively. Two strategy was used for the covalent immobilization of α-galactosidase on the aminated Sepabeads: covalent immobilization of enzyme on glutaraldehyde activated support and cross-linking of the adsorbed enzymes on to the support with glutaraldehyde. By using these two methods, all the immobilized enzymes retained very high activity and the stability of the enzyme was also improved.

Efficient and rapid purification of lentil alpha-galactosidase by affinity precipitation with alginate.

Alpha-Galactosidase (alpha-D-galactoside galactohydrolase, EC 3.2.1.

Immobilization of avocado phytase on epoxy-activated Sepabead EC-EP and its application in soymilk phytate hydrolysis.

There is a great demand for using phytases to reduce phytate content in animal feed stuffs and food for human consumption. Industrial application of phytase requires efficient methods to immobilize the enzyme, yielding a biocatalyst with high activity and stability compared to the free enzyme. In the present study, phytase was immobilized on Sepabead EC-EP and then used in the biodegradation of soymilk phytate.

Purification of alpha-galactosidase by affinity precipitation with alginate.

Affinity precipitation is a technique which is known for over 20 years, but has recently received more attention due to the development of new materials for its implementation. It is a relatively simple, convenient, and reproducible technique that results in high target molecule recovery at high specificity. We describe, here, an efficient and rapid purification procedure for Vicia faba alpha-galactosidase (EC 3.