• 文献标题:   Characterization of immobilized alpha-amylase on functionalized graphene oxide surface
  • 文献类型:   Article
  • 作  者:   ZHANG H, HUA SF, ZHANG L, FAN YC, GUO FZ, WEI DY, ZHANG MJ
  • 作者关键词:   amination, carboxylation, graphene oxide, immobilized enzyme, alphaamylase
  • 出版物名称:   INDIAN JOURNAL OF BIOCHEMISTRY BIOPHYSICS
  • ISSN:   0301-1208 EI 0975-0959
  • 通讯作者地址:   Henan Polytech Univ
  • 被引频次:   0
  • DOI:  
  • 出版年:   2020

▎ 摘  要

Carboxyl-functionalized graphene oxide (GO-COOH) and amino-functionalized graphene oxide (GO-NH2) were prepared for use as carriers for alpha-amylase immobilization with 2-3% glutaraldehyde as a coupling agent. The alpha-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 degrees C 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 alpha-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 a-amylase on the modified carrier. The constant values, the K-m 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 V-max 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 after 7 reaction cycles, indicating excellent reusability.