Immobilization of Xylanase into Zeolitic Imidazolate Framework-67 (ZIF-67) and Manganese-Doped ZIF-67 (Mn/ZIF-67): A Comparison Study

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dc.authoridAtes, Burhan/0000-0001-6080-229X
dc.authoridDik, Gamze/0000-0003-4798-8127
dc.contributor.authorBakar, Busra
dc.contributor.authorDik, Gamze
dc.contributor.authorUlu, Ahmet
dc.contributor.authorAtes, Burhan
dc.date.accessioned2024-08-04T20:55:01Z
dc.date.available2024-08-04T20:55:01Z
dc.date.issued2024
dc.departmentİnönü Üniversitesien_US
dc.description.abstractIt has been discovered that metal-organic frameworks (MOFs) have desirable qualities for the immobilization of enzymes, including a high surface area, significant interior pore volumes, and easily changeable pore size. Herein, the xylanase (Xyl) enzyme was immobilized for the first time to two different carrier supports, zeolitic imidazolate framework-67 (ZIF-67) and manganese-doped ZIF-67 (Mn/ZIF-67) by in situ method. The physicochemical characterizations of MOFs with and without Xyl were performed by FT-IR, XRD, SEM, and EDAX techniques. Xyl@ZIF-67 and Xyl@Mn/ZIF-67 were evaluated in terms of optimum temperature, optimum pH, kinetic parameters, thermal stability, reusability as well as juice clarification and compared with free Xyl. Optimum temperature values were 50 degrees C for Xyl@ZIF-67 and 70 degrees C for free Xyl and Xyl@Mn/ZIF-67. Optimum pH values for free Xyl, Xyl@ZIF-67, and Xyl@Mn/ZIF-67 were recorded as 6.0, 8.0, and 7.0, respectively. Km values for free Xyl, Xyl@ZIF-67, and Xyl@Mn/ZIF-67 were calculated as 3.139, 5.430, and 0.799 mg/mL, respectively, while Vmax values were calculated as 0.167, 0.226, and 0.062 mu mol/min/mL, respectively. The results revealed that in comparison to the free Xyl, Xyl@ZIF-67, and Xyl@Mn/ZIF-67 exhibited more thermal resistance. After incubation at 70 degrees C for 120 min, the free Xyl remained at 28.7% of the activity, while the Xyl@ZIF-67 and Xyl@Mn/ZIF-67 remained at 85.7% and 40.0%, respectively. Moreover, after eight cycles, the Xyl@ZIF-67 and Xyl@Mn/ZIF-67 retained more than 70% of their initial activity. Further, the transmittance of apple juice was increased from 65.61 to 94.73% and from 77.80 to 84.13%, respectively, when Xyl@ZIF-67 and Xyl@Mn/ZIF-67 were used as biocatalysts. Overall, these findings indicated that the suggested Xyl@ZIF-67 and Xyl@Mn/ZIF-67 have a high potential for juice clarification as an efficient heterogeneous biocatalyst.en_US
dc.description.sponsorshipInoenue University [FBG-2021-2731]en_US
dc.description.sponsorshipThis work was partially financed by the Scientific Research Projects Unit of Inoenue University (Project Number: FBG-2021-2731). Buesra Bakar is a 100/2000 the Council of Higher Education PhD Scholar Biomaterial and Tissue Engineering subdivision.en_US
dc.identifier.doi10.1007/s11244-023-01898-1
dc.identifier.endpage713en_US
dc.identifier.issn1022-5528
dc.identifier.issn1572-9028
dc.identifier.issue9-12en_US
dc.identifier.scopus2-s2.0-85183701158en_US
dc.identifier.scopusqualityQ2en_US
dc.identifier.startpage698en_US
dc.identifier.urihttps://doi.org/10.1007/s11244-023-01898-1
dc.identifier.urihttps://hdl.handle.net/11616/101787
dc.identifier.volume67en_US
dc.identifier.wosWOS:001153197200001en_US
dc.identifier.wosqualityN/Aen_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/openAccessen_US
dc.subjectZeolitic imidazole framework-67 (ZIF-67)en_US
dc.subjectManganeseen_US
dc.subjectXylanaseen_US
dc.subjectEnzyme immobilizationen_US
dc.subjectJuice clarificationen_US
dc.titleImmobilization of Xylanase into Zeolitic Imidazolate Framework-67 (ZIF-67) and Manganese-Doped ZIF-67 (Mn/ZIF-67): A Comparison Studyen_US
dc.typeArticleen_US

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