Acet, ÖmürAksoy, Neşe HayatErdönmez, DemetOdabaşı, Mehmet13.07.20192019-07-1613.07.20192019-07-1620182169-14012169-141Xhttps://doi.org/10.1080/21691401.2018.1501378https://hdl.handle.net/20.500.12451/4723In order to investigate the biocatalytic properties of alpha-amylase on a composite cryogel matrix with immobilized metal affinity chromatography, Cu+2-attached poly(2-hydroxyethyl methacrylate) (Cu+2-PHEMA) beads, (2 mu m size) were synthesized, then composite cryogel column was prepared by composing beads and PHEMA cryogels. After the preparation of Cu+2-PHEMA beads embedded cryogel column (Cu+2-BEC), some experiments were tested. Accordingly, the highest adsorption capacity (676.8 mg/g particles) of cryogels was achieved at acetate buffer of pH 5.0 with initial alpha-amylase concentration of 4 mg/mL. Immobilized enzyme has more stable pH range, between 6 and 7.5 than, the free one. Immobilization also increased the optimal activity from 25 to temperature range of 25-35 degrees C. V-max and K-m of alpha-amylase were detected as 1.149 U/mg protein, and 11.6 x 10(-1) mM, respectively. alpha-Amylase was utilized 35 times repeatedly without losing the productivity.eninfo:eu-repo/semantics/openAccessProtein AdsorptionIMACAlpha-AmylaseComposite CryogelBead EmbeddingArticle46S538S54510.1080/21691401.2018.150137830299164Q1WOS:000460141900051N/A