Electrospun Polycaprolactone-Chitosan Nanofiber Scaffolds for Covalent Immobilization of Xylanase: Structural Characterization and Enzyme Performance

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dc.contributor.authorDogan, Tugba
dc.date.accessioned2026-04-04T13:37:29Z
dc.date.available2026-04-04T13:37:29Z
dc.date.issued2026
dc.departmentİnönü Üniversitesi
dc.description.abstractXylanases (XyL) are critical enzymes that release that hydrolyze xylan, a major component of hemicellulose, into xylose and its derivates, and they are vital in diverse industrial fields. However, their use in free form is limited due to instability and lack of reusability. Enzyme immobilization offers a promising approach to overcome these drawbacks. In this study, electrospun polycaprolactone/chitosan (PCL/CHI) nanofibers were fabricated and used as by nanocarriers for covalent immobilization of XyL. A solution containing 10% PCL and 0.5% CHI in acetic acid: formic acid (6:4) was electrospun under optimized conditions (22 kV, 1 mL/h, 18 cm). Fibers were cross-linked with glutaraldehyde, washed thoroughly to remove residual toxicity, and then used for enzyme immobilization. Structural and morphological analyses (SEM, EDX, XRD, and FTIR) confirmed successful fiber formation and enzym binding. The optimum temperature was determined as 50 degrees C for both forms, while the optimum pH was determined as 6 for the free form and 5 for the immobilized form. The activation energy decreased from 21.46 kJ/mol to 1.17 kJ/mol, indicating enhaced catalytic efficiency. Kinetic analysis revealed a reduction in Km (13.01\documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \usepackage{upgreek} \setlength{\oddsidemargin}{-69pt} \begin{document}$$\:\to\:$$\end{document} 4.80 mg/mL), suggesting improved substrate affinity. Furthermore, the decrease in Km value revealed that immobilization enhanced enzyme-substrate interaction, while reusability tests showed that the immobilized enzyme retained 45% of its initial activity after five cycles. The fact that the immobilized form maintained its high catalytic performance in the presence of metal ions highlights the system's potential for adaptation to industrial conditions. In conclusion, this developed platform has been demonstrated to be a promising approach for sustainable and economical solutions in enzyme technologies.
dc.identifier.doi10.1007/s10562-025-05290-4
dc.identifier.issn1011-372X
dc.identifier.issn1572-879X
dc.identifier.issue2
dc.identifier.scopus2-s2.0-105027581182
dc.identifier.scopusqualityQ2
dc.identifier.urihttps://doi.org/10.1007/s10562-025-05290-4
dc.identifier.urihttps://hdl.handle.net/11616/109864
dc.identifier.volume156
dc.identifier.wosWOS:001663080600001
dc.identifier.wosqualityQ3
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.institutionauthorDogan, Tugba
dc.language.isoen
dc.publisherSpringer
dc.relation.ispartofCatalysis Letters
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.snmzKA_WOS_20250329
dc.subjectXyL
dc.subjectEnzyme immobilization
dc.subjectElectrospinning
dc.subjectNanofibers
dc.subjectBiocatalysts
dc.titleElectrospun Polycaprolactone-Chitosan Nanofiber Scaffolds for Covalent Immobilization of Xylanase: Structural Characterization and Enzyme Performance
dc.typeArticle

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