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Characterization of β-glucosidase immobilized on chitosan-multiwalled carbon nanotubes (MWCNTS) and their application on tea extracts for aroma enhancement
•The covalent binding of β-glucosidase on chitosan-MWCNTs beads were investigated.•The prepared supports were characterized by FTIR, TGA and SEM.•The immobilized β-glucosidase was applied to aroma-increasing of tea extracts. β-Glucosidase was covalently immobilized on chitosan-MWCNTs carrier and its...
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Published in: | International journal of biological macromolecules 2016-08, Vol.89, p.406-414 |
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Main Authors: | , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | •The covalent binding of β-glucosidase on chitosan-MWCNTs beads were investigated.•The prepared supports were characterized by FTIR, TGA and SEM.•The immobilized β-glucosidase was applied to aroma-increasing of tea extracts.
β-Glucosidase was covalently immobilized on chitosan-MWCNTs carrier and its aroma enhancement effect in different tea samples was investigated. Chitosan-MWCNTs carrier was prepared by mixing chitosan with MWCNTs (5:1w/w) and characterization of prepared composite carrier was done by FTIR, TGA and SEM analysis. β-Glucosidase was covalently immobilized on the composite carrier after glutaraldeyde activation. After optimization of the immobilization conditions, immobilization yield was achieved as 95.22%. Optimum pH was found as pH 6.0 and pH 5.0 for free and immobilized enzyme, respectively. Optimum temperature of the enzyme was shifted from 35°C to 45°C after immobilization. The Km and Vmax values for immobilized β-glucosidase calculated as 5.55mM and 7.14U/mg protein respectively. Immobilized β-glucosidase showed better pH and storage stability than free enzyme. After storage at +4°C for 50days, the immobilized enzyme retained its 68.4% of the initial activity. The calculated half-life (t1/2) of immobilized enzyme was 115.8min. After 10 cycles of reuse, immobilized β-glucosidase showed 72.83% of its initial activity. |
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ISSN: | 0141-8130 1879-0003 |
DOI: | 10.1016/j.ijbiomac.2016.05.008 |