부산대학교 도서관

The objective of the Phase I project was to develop new stabilization techniques for immobilized enzymes used in bioreactors. The rationale was to provide an environment for optimal stability surrounding the enzyme, then to bind it together by copolymerization with vinyl monomers to obtain a large molecular weight, but soluble, enzyme derivative that would then be immobilized. The enzyme chosen for the project was beta-galactosidase from Aspergillus oryzae which is used in enzyme reactors for hydrolyzing lactose from milk whey. Several methods were used to achieve covalent crosslinking of beta-galactosidase. Although some stabilization was achieved with soluble, crosslinked beta-galactosidase, the methods originally proposed did not give significant stabilization of the immobilized enzyme. However, preliminary evidence was obtained that significant stabilization of immobilized beta-galactosidase was achieved by a modified crosslinking technique. The modified technique could have wide commercial applications for stabilizing enzymes used in bioreactors for the cheese and other dairy industries, food processing applications, pharmaceutical production, biodegradation of hazardous chemicals, and other scientific applications.