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Immobilized glucoamylase based on ZIF-8: Preparation, response surface optimization, characterization.
Zong, Xuyan; Huang, Min; Wen, Lei; Li, Yuanyi; Li, Li.
Affiliation
  • Zong X; Liquor Brewing Biotechnology and Application Key Laboratory of Sichuan Province, Sichuan University of Science and Engineering, Yibin, Sichuan, China.
  • Huang M; College of Bioengineering, Sichuan University of Science and Engineering, Yibin, Sichuan, China.
  • Wen L; Liquor Brewing Biotechnology and Application Key Laboratory of Sichuan Province, Sichuan University of Science and Engineering, Yibin, Sichuan, China.
  • Li Y; College of Bioengineering, Sichuan University of Science and Engineering, Yibin, Sichuan, China.
  • Li L; Liquor Brewing Biotechnology and Application Key Laboratory of Sichuan Province, Sichuan University of Science and Engineering, Yibin, Sichuan, China.
J Food Sci ; 88(8): 3460-3473, 2023 Aug.
Article in En | MEDLINE | ID: mdl-37326335
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.
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Glucan 1,4-alpha-Glucosidase / Enzymes, Immobilized Language: En Journal: J Food Sci Year: 2023 Document type: Article Affiliation country: China Country of publication: United States

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Glucan 1,4-alpha-Glucosidase / Enzymes, Immobilized Language: En Journal: J Food Sci Year: 2023 Document type: Article Affiliation country: China Country of publication: United States