α-Amylase Immobilized Composite Cryogels: Some Studies on Kinetic and Adsorption Factors
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Tarih
2021
Dergi Başlığı
Dergi ISSN
Cilt Başlığı
Yayıncı
Springer
Erişim Hakkı
info:eu-repo/semantics/openAccess
Özet
Stability of enzymes is a significant factor for their industrial feasibility. alpha-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. alpha-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 alpha-amylase were investigated, and results indicate that immobilization did not alter the optimum pH and temperature values. k(cat) value of the immobilized alpha-amylase is higher than that of the free alpha-amylase while K-M value increases by immobilization. Storage and operational stabilities of the free and the immobilized alpha-amylase were determined for 35 days and for 20 runs, respectively.
Açıklama
Anahtar Kelimeler
Protein adsorption, IMAC, alpha-Amylase, Composite cryogel, Bead embedding
Kaynak
Applied Biochemistry and Biotechnology
WoS Q Değeri
Q2
Scopus Q Değeri
Q2
Cilt
193
Sayı
8
