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α-Glucosidase immobilization on chitosan-modified cellulose filter paper: Preparation, property and application.
- Source :
-
International journal of biological macromolecules [Int J Biol Macromol] 2019 Feb 01; Vol. 122, pp. 298-305. Date of Electronic Publication: 2018 Oct 26. - Publication Year :
- 2019
-
Abstract
- In the present study, α-glucosidase (α-Glu) was immobilized on the chitosan-modified cellulose filter paper (CFP/CS). For α-Glu immobilization, glutaraldehyde (GA) was used as a coupling agent. CFP, environmentally friendly and commercially available with low cost, will avoid the tedious procedure for synthesizing immobilization carrier. In addition, the CFP/CS-immobilized α-Glu can be directly taken out from the reaction mixture after an enzymatic reaction. This makes the instantaneous separation of immobilized enzyme comes true and is convenient to the subsequent study. Combined with capillary electrophoresis (CE), the CFP/CS-immobilized α-Glu was then used for enzyme kinetic and inhibition study. The CFP/CS-immobilized α-Glu exhibited enhanced pH and temperature tolerance. In addition, the performance of the CFP/CS-immobilized α-Glu was studied. Immobilized α-Glu exhibited excellent batch-to-batch reproducibility (RSD = 6.7%, n = 5) and improved reusability (71.0% of its initial activity after 10 repeated cycles). Finally, immobilized α-Glu was used to screen enzyme inhibitors from 11 traditional Chinese medicines (TCMs). The results showed that CFP/CS has potential development prospects as a novel enzyme immobilization carrier.<br /> (Copyright © 2018 Elsevier B.V. All rights reserved.)
- Subjects :
- Enzymes, Immobilized antagonists & inhibitors
Enzymes, Immobilized metabolism
Glycoside Hydrolase Inhibitors pharmacology
Hydrogen-Ion Concentration
Kinetics
Reproducibility of Results
Temperature
alpha-Glucosidases metabolism
Cellulose chemistry
Chitosan chemistry
Enzymes, Immobilized chemistry
Filtration
Paper
alpha-Glucosidases chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 1879-0003
- Volume :
- 122
- Database :
- MEDLINE
- Journal :
- International journal of biological macromolecules
- Publication Type :
- Academic Journal
- Accession number :
- 30401648
- Full Text :
- https://doi.org/10.1016/j.ijbiomac.2018.10.177