Please use this identifier to cite or link to this item: http://nopr.niscair.res.in/handle/123456789/54772
Title: Characterization of immobilized α-amylaseonfunctionalizedgraphene oxide surface
Authors: Han, Zhang
Shaofeng, Hua
Lei, Zhang
Yunchang, Fan
Fengzhe, Guo
Dongyue, Wei
Meijin, Zhang
Keywords: Amination;Carboxylation;Graphene oxide;Immobilized enzyme;α-amylase
Issue Date: Aug-2020
Publisher: NISCAIR-CSIR, India
Abstract: Carboxyl-functionalized graphene oxide (GO-COOH) and amino-functionalized graphene oxide (GO-NH2) were prepared for use as carriers for α-amylase immobilization with 2-3% glutaraldehyde as a coupling agent. The α-amylase immobilized onto modified GO exhibited shifts in both working optimum pH and temperature with an increase from pH 6.0 to pH 7.0, and increased optimum temperature by 5-10℃ compared with the free enzyme. The loading capacity of the carriers is 786.8 mg/g (GO-COOH) and 437 mg/g (GO-NH2), respectively. The immobilized α-amylase exhibited a comparable stability activity in comparison with the free enzyme. The FT-IR spectra, UV-visible spectra as well as SEM analysis proved the presence of amine groups and carboxyl groups in the GO, and also covalent immobilization of α-amylase on the modified carrier. The constant values, the Km  was 3.541 mg·mL-1, 4.072 mg·mL-1 and 8.004 mg·mL-1 for free enzymes, GO-COOH-E, and GO-NH2-E, respectively,and their Vmax  were 7.341 mg·mL-1·min-1, 4.968 mg·mL-1·min-1 and 6.655 mg·mL-1·min-1, respectively. Furthermore, above 54% of the original activity of the immobilized enzyme was retained after7 reaction cycles,indicatingexcellent reusability.
Page(s): 411-419
URI: http://nopr.niscair.res.in/handle/123456789/54772
ISSN: 0975-0959 (Online); 0301-1208 (Print)
Appears in Collections:IJBB Vol.57(4) [August 2020]

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