Reseach On Immobilization Of Halohydrin Dehalogenase HheC

Industrial enzymes play an important role in industrial production. Halohydrin dehalogenase HheC that was isolated from Agrobacterium radiobacter AD1, catalyzes the dehalogenation of vicinal haloalcohols to produce the corresponding epoxides and its reverse reaction. It was demonstrated that HheC is a promising biocatalyst in industry and pharmaceutics, such as catalyzing the degradation of 1,3-DCP which is an important environmental pollutant. But free-HheC is sensitive to acid, alkali, and high temperature. Immobilized enzyme could avoid these shortages, which greatly facilitates their application as biocatalysts.We tested many immobilization methods to study which one is suitable for HheC. We found that HheC was inactive when it was absorpt in silica gel, while encapsulation or covalent methods showed exciting results. Encapsulated HheC which depend on calcium alginate carrier could enhance stability by 120 folds as compared with free enzyme, whereas the carrier was easy to swell after several times’ washing. The covalent immobilized HheC displayed at least 500 folds higher stability than free-HheC, and it excellent performance depends on the commercial Relizyme 403 S. The so called “Standard Protocol” of covalent immobilized method was modified to suit for the immobilization of HheC.