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In this research, the immobilization of α-amylase from Bacillus subtilis ITBCCB148 by crosslinking method on chitosan matrix has been performed. This research aims to know the effect of immobilization on the thermal stability of α-amylase. The results showed that the native α-amylase has an optimum temperature of  65 o C, K M = 1.6 mg mL -1 substrate, and V ma x = 39.7 µmol mL -1 min -1 . The immobilized α-amylase has optimum temperature of 75 o C, K M = 3.5 mg mL -1 substrate, and V ma x = 7.05 µmol mL -1 min -1 . The residual activity of the native and immobilized enzyme on thermal stability test at 65 o C for 80 minutes was 58% and 86.15%, respectively. The immobilized enzyme can be reused up to six repeated cycles.The thermodynamic data of native enzyme was t ½ = 113.6 min, k i = 6.1x10 -3 min -1 , and ΔG i = 107.3 kJ mol -1 , while the immobilized enzyme was t ½ = 433.1 min, k i = 1.6x10 -3 min -1 , and ΔG i 111.1 kJ mol -1 . Based on the decrease of k i , and the increase of ΔG i and half-life(t ½ ) values, the immobilization of α-amylase with chitosan can increase the thermal stability of this enzyme.

Increasing Stability of a-amylase Obtained from Bacillus subtilis ITBCCB148 by Immobilization with Chitosan