摘要：In this study, α-amylase formerly purified from Geobacillus sp. TF14 strain was covalently immobilized onto chitosan beads. Chitosan beads were prepared by dissolving chitosan powder in 5% acetic acid solution and by addition dropwise to 1 M NaOH solution. The consisted beads were washed to remove excessive amount of NaOH. Immobilization was carried out in two steps. Firstly, chitosan beads were activated by reacting with 2.5% Glutaraldehyde solution. Next, activated chitosan beads were mixed with enzyme solution to complete immobilization. Biochemical characterization of immobilized α-amylase was also carried out. It was found that immobilized α-amylase achieved maximum activity at pH 9.00 and the enzyme was quite stable at this pH over a period of 48 h. Temperature optimum of the enzyme was determined as 95 °C. It was also determined that the enzyme protected 50% of its initial activity after incubation of 48 h at this temperature. While Mn2+, Co2+ and EDTA almost completely inhibited the enzyme, other metal ions showed inhibitory effects at different ratio. In the presence of some detergents the enzyme conserved its initial activity. It can be concluded that the immobilized α-amylase may find application in many fields of starch based industries.
其他摘要：Bu calışmada, daha once Geobacillus sp. TF14den saflaştırılmış α-amilaz enzimi, kitosan boncuklara kovalent olarak immobilize edildi. Kitosan boncuklar, toz haldeki kitosanın % 5’lik asetik asit cozeltisinde cozulmesi ve 1 M NaOH cozeltisine damla damla e
