Evidence map›Paper›PMID 41663626›Full record

ArticleScientific reports2026

Engineering polyethylenimine-metal functionalized cryogels for superior catalase binding, activity, and long-term durability.

Kadir Erol, Mehmet Hüseyin Alkan, İhsan Alacabey

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Article in Scientific reports, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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1 · What the graph read from it

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2 · The registry

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3 · Its place in the literature

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4 · The record

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5 · Who and what money

Authors and funding

3 authors.

Kadir ErolVocational School of Health Services, Department of Environmental Protection Technologies, Hitit University, 19030, Çorum, Turkey. kadirerol86@gmail.com.
Mehmet Hüseyin AlkanFaculty of Pharmacy, Department of Basic Pharmaceutical Sciences, Dicle University, 21280, Diyarbakır, Turkey. mhalkan@dicle.edu.tr.
İhsan AlacabeyVocational School of Health Services, Department of Medical Services and Techniques, Mardin Artuklu University, 47100, Mardin, Turkey.

Funding

Dicle Üniversitesi ECZACILIK.25.025
6 · The paper itself

Abstract

Cryogels with interconnected macroporous architectures offer significant advantages as enzyme immobilization supports due to their high permeability, mechanical robustness, and tunable surface chemistry. In this study, a novel Poly(HEMA-co-GMA) cryogel was synthesized and subsequently modified through polyethyleneimine (PEI) grafting and transition-metal chelation to create high-affinity matrices for catalase immobilization. Among the metal ions tested with Cu(II), Ni(II), and Co(II), the Cu(II)-functionalized cryogel exhibited superior physicochemical properties, including the highest water retention capacity (438.4%), well-preserved porosity, and strong coordination interactions with amine-rich PEI domains. FT-IR, SEM, TGA, BET, elemental analysis, and ICP-OES results confirmed successful stepwise modification and metal loading. Catalase immobilization studies revealed that the Poly(HEMA-co-GMA)-PEI-Cu(II) cryogel achieved the highest enzyme loading (391.9 mg·g⁻¹), with an optimal immobilization time of 8 h and optimum pH near neutrality. Kinetic analysis demonstrated a substantial decrease in Km (from 57.3 to 14.4 mM), indicating enhanced substrate affinity, while kcat/Km increased 2.8-fold relative to the free enzyme. The immobilized catalase exhibited improved thermal tolerance, strong operational stability (34.2% activity after 15 cycles), high desorption efficiency (96% in the first cycle), and markedly superior storage stability (62.1% activity after 70 days at 4 °C) compared to its free counterpart. These results validate the Cu(II)-chelated Poly(HEMA-co-GMA)-PEI cryogel as a highly efficient and reusable biocatalytic platform with significant potential for industrial and environmental enzyme-based applications.

Indexed as

CatalaseCryogelsEnzymes, ImmobilizedMetalsPolyethyleneimineCopperEnzyme StabilityHydrogen-Ion ConcentrationKineticsPolyhydroxyethyl MethacrylatePorosityProtein BindingSpectroscopy, Fourier Transform InfraredCatalaseCopperCryogelsEnzymes, ImmobilizedMetalsPolyethyleneiminePolyhydroxyethyl MethacrylateCatalaseCopperCryogelImmobilizationPolyethyleniminePoly(HEMA-GMA)

Identifiers

PMID41663626
PMCPMC12953862

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.