Immobilization and Characterization of Genistein Metabolizing and Glucose-tolerant β-glucosidases From Penicillium sp. NRC24 | ||
| Egyptian Journal of Chemistry | ||
| Volume 67, Issue 3, March 2024, Pages 55-69 PDF (724.69 K) | ||
| Document Type: Original Article | ||
| DOI: 10.21608/ejchem.2023.220595.8202 | ||
| Authors | ||
| Asmaa I. El-Shazly1; Douaa H Abdel Azizb2; Amira A Gamal3; Mohamed E. Hassan* 4 | ||
| 1Chemistry of Natural and Microbial Products Department, Pharmaceutical and Drug Industries Research Institute, National Research Center (NRC), Dokki, Cairo, Egypt. | ||
| 2Agricultural Microbiology Department, National Research Center, Cairo, Egypt. | ||
| 3Chemistry of Natural and Microbial Products Department, Pharmaceutical and Drug Industries Research Institute, National Research Center (NRC), Dokki, Cairo, Egypt | ||
| 4Center of Excellence, Encapsulation and Nano biotechnology Group, Chemistry of Natural and Microbial Products Department, Pharmaceutical and Drug Industries Research Institute,, National Research Center, El Behouth Street, Cairo 12622, Egypt. | ||
| Abstract | ||
| Glucose tolerant β-glucosidases have attracted considerable attention due to their important roles in various biotechnological processes. Penicillium sp. NRC24, a new fungal isolate was used to produce soy glycosides-hydrolyzing β-glucosidase. The ability of β-glucosidase to convert soy glucosides into aglycone forms, as well as its activity on p-NPG, was investigated. Penicillium sp. NRC24 β-glucosidase was partially purified with 8.04-fold and final recovery of 45.7%. This enzyme exhibited a glucose-tolerant activity of 60.4% while the partially purified enzyme showed 85.6% activity at 0.5 M of glucose. Moreover, the produced β-glucosidase could tolerate ethanol up to 60%. β-glucosidase retained all its initial activity at 37 °C in presence of 15-60 % ethanol at pH 5.0. The immobilization and characterization of the produced β-glucosidase are described. The efficacy of β-glucosidase covalently immobilized on alginate/polysorbate complex was 70.1%. The impact of pH, and thermal stability, on the free and immobilized β-glucosidase activities and hydrolysis of soybean extract were evaluated. The optimum pH remained at 5.0 after immobilization, while the optimum temperature leveled up to 50 °C in comparison to the free enzyme, which remained at 37 °C. This is the first report to our knowledge on the use of Penicillium sp. NRC24 for the production, characterization, and immobilization of β-glucosidase, which can hydrolyze genistein and daidzein into their aglycone forms. | ||
| Keywords | ||
| β -glucosidase; Glucose and ethanol tolerance; Alginate/polysorbate complex; Covalent immobilization, Soy daidzein and genistein | ||
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