Ertan Figen, Yagar Hulya, Balkan Bilal
Faculty of Science and Art, Department of Biology, Trakya University, Edirne, Turkey.
Prep Biochem Biotechnol. 2007;37(3):195-204. doi: 10.1080/10826060701386679.
alpha-Amylase enzyme was produced by Aspergillus sclerotiorum under SSF conditions, and immobilized in calcium alginate beads. Effects of immobilization conditions, such as alginate concentration, CaCl(2) concentration, amount of loading enzyme, bead size, and amount of beads, on enzymatic activity were investigated. Optimum alginate and CaCl(2) concentration were found to be 3% (w/v). Using a loading enzyme concentration of 140 U mL(-1), and bead (diameter 3 mm) amount of 0.5 g, maximum enzyme activity was observed. Beads prepared at optimum immobilization conditions were suitable for up to 7 repeated uses, losing only 35% of their initial activity. Among the various starches tested, the highest enzyme activity (96.2%) was determined in soluble potato starch hydrolysis for 120 min at 40 degrees C.
α-淀粉酶由核盘曲霉在固态发酵条件下产生，并固定在海藻酸钙珠中。研究了固定化条件，如海藻酸钠浓度、氯化钙浓度、酶负载量、珠粒大小和珠粒数量对酶活性的影响。发现最佳海藻酸钠和氯化钙浓度为3%（w/v）。使用140 U mL(-1)的负载酶浓度和0.5 g的珠粒（直径3 mm）数量时，观察到最大酶活性。在最佳固定化条件下制备的珠粒适合重复使用多达7次，仅损失其初始活性的35%。在测试的各种淀粉中，在40℃下将可溶性马铃薯淀粉水解120分钟时，测定的最高酶活性为96.2%。
