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dc.contributor.authorHosseinipour, SL
dc.contributor.authorKhiabani, MS
dc.contributor.authorHamishehkar, H
dc.contributor.authorSalehi, R
dc.date.accessioned2018-08-26T07:42:02Z
dc.date.available2018-08-26T07:42:02Z
dc.date.issued2015
dc.identifier.urihttp://dspace.tbzmed.ac.ir:8080/xmlui/handle/123456789/47720
dc.description.abstractEnzymes play an essential role in catalyzing various reactions. However, their instability upon repetitive/prolonged use, elevated temperature, acidic or alkaline pH remains an area of concern. alpha-Amylase, a widely used enzyme in food industries for starch hydrolysis, was covalently immobilized on the surface of two developed matrices, amino-functionalized silica-coated magnetite nanoparticles (AFSMNPs) alone and covered with chitosan. The synthesis steps and characterizations of NPs were examined by FT-IR, VSM, and SEM. Modified nanoparticles with average diameters of 20-80 nm were obtained. Enzyme immobilization efficiencies of 89 and 74 were obtained for AFSMNPs and chitosan-coated AFSMNPs, respectively. The optimum pH obtained was 6.5 and 8.0 for the enzyme immobilized on AFSMNPs and chitosan-coated AFSMNPs, respectively. Optimum temperature for the immobilized enzyme shifted toward higher temperatures. Considerable enhancements in thermal stabilities were observed for the immobilized enzyme at elevated temperatures up to 80 degrees C. A frequent use experiment demonstrated that the immobilized enzyme retained 74 and 85 % of its original activity even after 20 times of repeated use in AFSMNPs and chitosan-coated AFSMNPs, respectively. Storage stability demonstrated that free enzyme lost its activity completely within 30 days. But, immobilized enzyme on AFSMNPs and chitosan-coated AFSMNPs preserved 65.73 and 78.63 % of its initial activity, respectively, after 80 days of incubation. In conclusion, a substantial improvement in the performance of the immobilized enzyme with reference to the free enzyme was obtained. Furthermore, the relative activities of immobilized enzyme are superior than free enzyme over the broader pH and temperature ranges.
dc.language.isoEnglish
dc.relation.ispartofJOURNAL OF NANOPARTICLE RESEARCH
dc.subjectalpha-Amylase
dc.subjectEnzyme activity
dc.subjectCovalent immobilization
dc.subjectMagnetite nanoparticles
dc.subjectSilica
dc.subjectChitosan
dc.subjectNanostructure
dc.titleEnhanced stability and catalytic activity of immobilized alpha-amylase on modified Fe3O4 nanoparticles for potential application in food industries
dc.typeArticle
dc.citation.volume17
dc.citation.issue9
dc.citation.indexWeb of science
dc.identifier.DOIhttps://doi.org/10.1007/s11051-015-3174-3


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