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Immobilized glucoamylase based on ZIF‐8: Preparation, response surface optimization, characterization.

Authors :
Zong, Xuyan
Huang, Min
Wen, Lei
Li, Yuanyi
Li, Li
Source :
Journal of Food Science (John Wiley & Sons, Inc.). Aug2023, Vol. 88 Issue 8, p3460-3473. 14p.
Publication Year :
2023

Abstract

The glucoamylase@ZIF‐8 was prepared using ZIF‐8 material as the carrier in this study. The preparation process was optimized by response surface methodology, and the stability of glucoamylase@ZIF‐8 was determined. The material was characterized by scanning electron microscopy, X‐ray diffraction, and Fourier transform infrared spectroscopy. The results showed that the optimum preparation process of glucoamylase@ZIF‐8 was 1.65 mol 2‐methylimidazole, 5.85 mL glucoamylase, 33°C stirring temperature, 90 min stirring time, and 84.0230% ± 0.6006% embedding rate. At 100°C, the free glucoamylase completely lost its activity, whereas the glucoamylase@ZIF‐8 still had a retained enzyme activity of 12.0123% ± 0.86158%; at pH 3–6, the highest activity of glucoamylase@ZIF‐8 was 95.9531% ± 0.96181%, and about 80% of glucoamylase activity could be retained under alkaline conditions. When the ethanol concentration was 13%, the retained enzyme activity was 7.9316% ± 0.19805%, significantly higher than free enzymes. The Km of glucoamylase@ZIF‐8 and free enzyme were 1235.6825 and 80.317 mg/mL, respectively. Vmax was 0.2453 and 0.149 mg/(mL min), respectively. The appearance, crystal strength, and thermal stability of glucoamylase@ZIF‐8 were improved after optimization, and they had high reusability. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
00221147
Volume :
88
Issue :
8
Database :
Academic Search Index
Journal :
Journal of Food Science (John Wiley & Sons, Inc.)
Publication Type :
Academic Journal
Accession number :
169784051
Full Text :
https://doi.org/10.1111/1750-3841.16667