Immobilization of catalase on Fe (III) modified collagen fiber.
- Author:
Shuang CHEN
1
;
Na SONG
;
Xuepin LIAO
;
Bi SHI
Author Information
1. Department of Biomass Chemistry and Engineering, Sichuan University, Chengdu 610065, China.
- Publication Type:Journal Article
- MeSH:
Catalase;
chemistry;
metabolism;
Collagen;
chemistry;
metabolism;
Enzymes, Immobilized;
chemistry;
metabolism;
Ferric Compounds;
chemistry
- From:
Chinese Journal of Biotechnology
2011;27(7):1076-1081
- CountryChina
- Language:Chinese
-
Abstract:
Fe (III) modified collagen fibers were used to immobilize catalase through the cross-linking of glutaraldehyde. The loading amount of catalase on the supporting matrix was 16.7 mg/g, and 35% enzymatic activity was remained. A series of experiments were conducted on free and immobilized catalase in order to investigate their optimal pH and temperature, and the thermal, storage and operation stability. Results suggest that the free and immobilized catalase prefer similar pH and temperature condition, which were pH 7.0 and 25 degrees C. It should be noted that the thermal stability of catalase was considerably improved after immobilization owing to the fact that the enzyme kept 30% of relative activity after incubation at 75 degrees C for 5 h. On the contrary, the free catalase was completely inactive. As for the storage stability, the immobilized catalase kept 88% of relative activity after stored at room temperature for 12 days while the free one was completely inactive under the same conditions. Moreover, the immobilized catalase preserved 57% of relative activity after being reused 26 times, exhibiting excellent operation stability. Consequently, this investigation suggests that collagen fiber can be used as excellent supporting matrix for the immobilization of catalase, and it is potential to be used for the immobilization of similar enzymes.
