Akademik Veri Yönetim Sistemi
Food Bioscience, cilt.50, 2022 (SCI-Expanded)
The amylase obtained from Cladophora hutchinsiae was purified by the starch affinity method (11.4-fold and specific activity of 89.7 ± 2.6 U/mg protein) and examined for its biochemical characterization, thermodynamic properties, and use in some industrial applications. As a result of SDS-PAGE analysis, the presence of a single band of 66.2 kDa was determined. It was determined that the enzyme showed optimum activity at pH 6.00 and 10 °C. In the presence of soluble starch as substrate, Km, Vmax and kcat values were calculated as 1.49 ± 0.03 mg/mL, 0.18 ± 0.01 U and 0.003 s−1respectively. The enzyme demonstrated remarkable pH stability. Enzyme activity was investigated in a medium containing some organic solvent and cations. While amylase was inhibited by ethanol, acetonitrile, glycerol, and acetone (10%), no change in activity was observed in the presence of isopropanol. In addition, it was determined that while Cu2+ and Hg2+ metal ions (5 mM) effectively inhibited the amylase enzyme, Ca2+ ion activates the amylase enzyme. The activation energy (Ea) was calculated as at 28.3 kJ mol−1. It was also found to be effective in releasing the reducing sugar from different fruit juice and fish feed. The amount of reducing sugar released as a result of incubation of fruit juices with enzyme for 3 h was observed the most in apple juice (from 1658.3 ± 33.8 μg/mL to 1945.6 ± 36.7 μg/mL) and the increase in the amount of reducing sugar was found to be 1.53 times in fish feed. According to the results obtained from the study, it can be said that the amylase obtained from seaweed can be used in different industrial areas.