Abstract
Stability of enzymes is a significant factor for their industrial feasibility. α-Amylase is an important enzyme for some industries, i.e., textile, food, paper, and pharmaceutics. Pumice particles (PPa) are non-toxic, natural, and low-cost alternative adsorbents with high adsorption capacity. In this study, Cu2+ ions were attached to pumice particles (Cu2+-APPa). Then, Cu2+-APPa embedded composite cryogel was synthesized (Cu2+-APPaC) via polymerization of gel-forming agents at minus temperatures. Characterization studies of the Cu2+-APPaC cryogel column were performed by X-ray fluorescence spectrometry (XRF), scanning electron microscopy (SEM), and Brunauer, Emmett, Teller (BET) method. The experiments were carried out in a continuous column system. α-Amylase was adsorbed onto Cu2+-APPaC cryogel with maximum amount of 858.7 mg/g particles at pH 4.0. Effects of pH and temperature on the activity profiles of the free and the immobilized α-amylase were investigated, and results indicate that immobilization did not alter the optimum pH and temperature values. kcat value of the immobilized α-amylase is higher than that of the free α-amylase while KM value increases by immobilization. Storage and operational stabilities of the free and the immobilized α-amylase were determined for 35 days and for 20 runs, respectively.
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References
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Acknowledgements
The author thanks Prof. Fatma Gurbuz for providing pumice particles. Also, the authors gratefully acknowledge the Scientific and Technological Application and Research Center of Aksaray University (ASUBTAM) for use of the services and facilities.
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Ömür Acet: investigation, writing—review and editing
Tülden İnanan: investigation, conceptualization, writing—review and editing
Burcu Önal Acet: investigation
Emrah Dikici: investigation
Mehmet Odabaşı: conceptualization, writing—review and editing
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Acet, Ö., İnanan, T., Acet, B.Ö. et al. α-Amylase Immobilized Composite Cryogels: Some Studies on Kinetic and Adsorption Factors. Appl Biochem Biotechnol 193, 2483–2496 (2021). https://doi.org/10.1007/s12010-021-03559-z
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DOI: https://doi.org/10.1007/s12010-021-03559-z