Yandri, Yandri and Suhartati, Tati and Satria, Heri and Hadi, Sutopo (2020) Increasing Stability of -amylase Obtained from Bacillus subtilis ITBCCB148 by Immobilization with Chitosan. Mediterranean Journal of Chemistry, 10 (2). pp. 155-161. ISSN 2028-3997

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Abstract: In this research, the immobilization of a-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 a-amylase. The results showed that the native a-amylase has an optimum temperature of 65 o C, K M = 1.6 mg mL -1 substrate, and V max = 39.7 µmol mL -1 min -1 . The immobilized a-amylase has optimum temperature of 75 o C, K M = 3.5 mg mL -1 substrate, and V max = 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 = 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 a-amylase with chitosan can increase the thermal stability of this enzyme.

Item Type: Article
Subjects: Q Science > QD Chemistry
Divisions: Fakultas Matematika dan Ilmu Pengetahuan Alam (FMIPA) > Prodi Kimia
Depositing User: Prof. YANDRI AS
Date Deposited: 09 Mar 2021 02:47
Last Modified: 09 Mar 2021 02:47
URI: http://repository.lppm.unila.ac.id/id/eprint/28288

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