期刊
BIOCHEMICAL ENGINEERING JOURNAL
卷 174, 期 -, 页码 -出版社
ELSEVIER
DOI: 10.1016/j.bej.2021.108119
关键词
Magnetic nanoparticles; Immobilized snailase; Biotransformation; Stability; Ginsenoside CK
资金
- National Natural Science Foundation of China [21706211, 21576160, 21878246, 21676214]
- National Key R&D Program of China [2019YFA0905200]
- Shaanxi Provincial Scientific Technology Research and Development Program [2019JQ-720]
The immobilization of glycosidases using Fe3O4@CYCTS nanoparticles shows promise for enhancing industrial production of ginsenoside CK. The immobilized enzyme exhibits higher affinity towards substrates and improved storage and stability against denaturants. The Fe3O4@CYCTS nanoparticles can be easily separated using a magnet, making them practical for enzyme immobilization applications.
Immobilization of glycosidases for ginsenoside CK production is a promising method to improve industrial production. Magnetite (Fe3O4) nanoparticles encapsulated with carboxylated chitosan (CYCTS) (Fe3O4@CYCTS) provide a large specific surface area for snailase immobilization. According to the morphology, structure, and magnetic properties determined by TEM, SEM, XRD, FTIR, and VSM, the spherical, 50-nm Fe3O4@CYCTS nanoparticles were synthesized and applied for the first time in snailase immobilization. The immobilized enzyme (Fe3O4@(CYCTS+Snailase)) could be easily separated from the reaction mixture using a simple magnet. Under optimum immobilization conditions (37, pH 5.5, 5 h), the protein adsorption on the surface of Fe3O4@CYCTS was mainly driven by electrostatic interactions and exhibited a maximum value of 67.67 mg enzyme/g of support. The storage stability of immobilized enzyme and the stability against thermal, pH, or chemical denaturants were improved. The immobilized snailase shows a higher affinity toward substrates as indicated by lower K-m values. At optimum reaction conditions (55, pH 5.5, 48 h), the immobilized snailase retained approximately 56% of its initial catalytic activity over 9 successive cycles. Our results revealed the potential applicability of Fe3O4@(CYCTS+Snailase) in ginsenoside transformation.
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