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Reusability of immobilized β-glucosidase on sodium alginate-coated magnetic nanoparticles and high productivity applications

Fawze Alnadari, Yemin Xue, Nouf H. Alsubhi, Soha A. Alamoudi, Afaf S. Alwabli, Diana A. Al-Quwaie, Yahya S. Hamed, Mustapha Muhammad Nasiru, Alia A. M. Ebrahim, Mohamed T. El‐Saadony, Fei Pan

2022Journal of Saudi Chemical Society22 citationsDOIOpen Access PDF

Abstract

The purpose of this study is to detect the impact of the covalent immobilization of β-glucosidase (β-Glu) from Thermatoga maritima on sodium alginate-based magnetically recyclable iron nanoparticles (SA-Fe3O4 MNPs) for boosting robustness, facile retrieval, and recycling of enzyme. We developed a novel green method to amend the transformation of lactose to galacto-oligosaccharides (GOS). The interaction of the Immobilized β-Glu and SA-Fe3O4 MNPs were characterized by SDS-PAGE, Transmission electron microscope (TEM) and FT-IR spectroscopy. After immobilization, the ideal pH maintained 7.0, the optimum temperature (temp.) increased to 85 °C and deceptive Km and Vmax raised by 65 and 41%, respectively. Immobilization provided low activation energy and enhanced pH and heat stability. The SA-Fe3O4 MNPs maintained the effectiveness of enzyme by 39.52% up to the 6th cycle of reuse and the hydrolysis power exceed 28.13% of lactose to GOS. Conclusively, thermal stability, improved pH, and excellent reusability over β-Glu make SA-Fe3O4 MNPs a viable option for long-term GOS production as well as other industrial uses.

Topics & Concepts

ChemistryImmobilized enzymeThermal stabilityHydrolysisReusabilityNanoparticleLactoseChemical engineeringNuclear chemistryMaterials scienceNanotechnologyEnzymeOrganic chemistryComputer scienceSoftwareProgramming languageEngineeringEnzyme Catalysis and ImmobilizationEnzyme Production and CharacterizationElectrochemical sensors and biosensors
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