Immobilization of ?-Amylase onto Quantum Dots Prepared from Hypericum perforatum L. Flowers and Hypericum capitatum Seeds: Its Physicochemical and Biochemical Characterization

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dc.authoridAteş, Burhan/0000-0001-6080-229X
dc.authoridUlu, Ahmet/0000-0002-4447-6233
dc.authorwosidKARACA ACARİ, Idil/GVU-4371-2022
dc.authorwosidAteş, Burhan/AAA-3730-2021
dc.authorwosidUlu, Ahmet/L-5180-2016
dc.contributor.authorAcari, Idil Karaca
dc.contributor.authorDik, Gamze
dc.contributor.authorBakar, Busra
dc.contributor.authorUlu, Ahmet
dc.contributor.authorOnal, Yunus
dc.contributor.authorAtes, Burhan
dc.date.accessioned2024-08-04T20:52:17Z
dc.date.available2024-08-04T20:52:17Z
dc.date.issued2023
dc.departmentİnönü Üniversitesien_US
dc.description.abstractEnzyme immobilization is an effective way to increase the catalytic activity and stability of the alpha-amylase (Amy) enzyme for industrial uses. For this purpose, carbon and graphene quantum dot (QDs) structures were prepared from Hypericum perforatum L. flowers (QD-1), and Hypericum capitatum seeds (QD-2) obtained from an herbalist in Hatay province of Turkey. Structural and morphological characterization of the prepared QDs and QDs/Amy were carried out by Fourier transform infrared spectrophotometer (FTIR), X-ray diffraction (XRD), scanning electron microscope (SEM), and energy dispersive X-ray (EDX). Meanwhile, biochemical characterizations such as optimum pH and temperature, kinetic parameters, effects of metal ions, organic solvents, and trypsin digestion on enzyme activity were performed and compared with free Amy. The Amy enzyme was immobilized with an activity efficiency of 71.15% for QD-1/Amy, and 81.51% for QD-2/Amy under optimal conditions. The difference in activity efficiency between QD-1/Amy and QD-2/Amy was likely due to a change in the surface porosity of QDs structures. While the optimal pH value of all three forms of Amy was recorded as 6.0, their optimal temperature was found to be 40 degrees C. The activation energy (E-a) of the free Amy was found to be 4.81 kJ/mol, while it was 9.61 kJ/mol, and 3.20 kJ/mol for QD-1/Amy, and QD-2/Amy, respectively. K-m values were calculated as 1.18, 1.57, and 1.35 mg/mL for free Amy, QD-1/Amy, and QD-2/Amy, respectively, and V-max values were calculated as 37.52, 37.60, and 39.93 mu mol/min, respectively. Kinetic data revealed that the immobilized enzymes had lower substrate affinity compared to the free Amy. Besides, the QD-1/Amy and QD-2/Amy exhibited more stability than free Amy against metal ions, organic solvents as well as trypsin digestion due to the increment in conformational rigidity caused by changes in the secondary structures of the immobilized enzyme. For instance, after incubation with trypsin for 120 min, free Amy, QD-1/Amy, and QD-2/Amy retained approximately 20%, 35%, and 26% of initial activities, respectively. Finally, it can be proposed that the prepared carriers in this work may a useful to produce stable and active immobilized Amy to be used in industrial applications.en_US
dc.description.sponsorshipScientific Research Projects Unit of Inonu Universityen_US
dc.description.sponsorshipThe authors thank the Scientific Research Projects Unit of Inonu University.en_US
dc.identifier.doi10.1007/s11244-022-01699-y
dc.identifier.endpage576en_US
dc.identifier.issn1022-5528
dc.identifier.issn1572-9028
dc.identifier.issue9-12en_US
dc.identifier.scopus2-s2.0-85137449607en_US
dc.identifier.scopusqualityQ2en_US
dc.identifier.startpage563en_US
dc.identifier.urihttps://doi.org/10.1007/s11244-022-01699-y
dc.identifier.urihttps://hdl.handle.net/11616/100873
dc.identifier.volume66en_US
dc.identifier.wosWOS:000849488400001en_US
dc.identifier.wosqualityQ2en_US
dc.indekslendigikaynakWeb of Scienceen_US
dc.indekslendigikaynakScopusen_US
dc.language.isoenen_US
dc.publisherSpringer/Plenum Publishersen_US
dc.relation.ispartofTopics in Catalysisen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectEnzyme immobilizationen_US
dc.subjectalpha-Amylaseen_US
dc.subjectHypericum perforatum L.en_US
dc.subjectHypericum capitatumen_US
dc.subjectQuantum dotsen_US
dc.subjectImproved stabilityen_US
dc.titleImmobilization of ?-Amylase onto Quantum Dots Prepared from Hypericum perforatum L. Flowers and Hypericum capitatum Seeds: Its Physicochemical and Biochemical Characterizationen_US
dc.typeArticleen_US

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