Yagar, HulyaErtan, FigenBalkan, Bilal2024-06-122024-06-1220081082-60681532-2297https://doi.org/10.1080/10826060701774304https://hdl.handle.net/20.500.14551/18311Some properties of immobilized a-amylase by Aspergillus sclerotiorum within calcium alginate gel beads were investigated and compared with soluble enzyme. Optimum pH and temperature were found to be 5.0 and 40 degrees C, respectively, for both soluble and immobilized enzymes. The immobilized enzyme had a better Km value, but k(cat)/K-m values were the same for both enzymes. Entrapment within calcium alginate gel beads improved, remarkably, the thermal and storage stability of a-amylase. The half life values of immobilized enzyme and soluble enzyme at 60 degrees C were 164.2, and 26.2 min, respectively. The midpoint of thermal inactivation (T-m) shifted from 56 degrees C (for soluble enzyme) to 65.4 degrees C for immobilized enzyme. The percentages of soluble starch hydrolysis for soluble and immobilized alpha-amylase were determined to be 97.5 and 92.2% for 60 min, respectively.en10.1080/10826060701774304info:eu-repo/semantics/closedAccessAlpha-AmylaseAspergillus SclerotiorumEntrapmentCalcium AlginateSoluble StarchHydrolysisOptimizationHydrolysisStarchArticle3811323Q4WOS:0002523121000022-s2.0-3724901702918080907Q3