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Characterization of immobilized α-amylase on functionalized graphene oxide surface

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Title Statement Characterization of immobilized α-amylase on functionalized graphene oxide surface
 
Added Entry - Uncontrolled Name Han, Zhang
Shaofeng, Hua
Zhang, Lei
Yunchang, Fan
Fengzhe, Guo
Dongyue, Wei
Meijin, Zhang
 
Uncontrolled Index Term Amination; Carboxylation; Graphene oxide; Immobilized enzyme; α-amylase
 
Summary, etc. 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 after 7 reaction cycles, indicating excellent reusability.
 
Publication, Distribution, Etc. Indian Journal of Biochemistry and Biophysics (IJBB)
2020-07-29 16:48:33
 
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http://op.niscair.res.in/index.php/IJBB/article/view/26272
 
Data Source Entry Indian Journal of Biochemistry and Biophysics (IJBB); ##issue.vol## 57, ##issue.no## 4 (2020): IJBB Vol.57(4) [August 2020]
 
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