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 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 65oC, KM = 1.6 mg mL-1 substrate, and Vmax = 39.7 µmol mL-1 min-1. The immobilized α-amylase has optimum temperature of 75oC, KM = 3.5 mg mL-1 substrate, and Vmax = 7.05 µmol mL-1 min-1. The residual activity of the native and immobilized enzyme on thermal stability test at 65oC 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 t½ = 113.6 min, ki = 6.1x10-3 min-1, and ΔGi = 107.3 kJ mol-1, while the immobilized enzyme was t½ = 433.1 min, ki= 1.6x10-3 min-1, and ΔGi 111.1 kJ mol-1. Based on the decrease of ki, and the increase of ΔGi and half-life(t½) values, the immobilization of α-amylase with chitosan can increase the thermal stability of this enzyme.

Item Type: Article
Uncontrolled Keywords: α-amylase, B. subtilis ITBCCB148, chitosan, immobiliza
Subjects: Q Science > QD Chemistry
Divisions: Fakultas Matematika dan Ilmu Pengetahuan Alam (FMIPA) > Prodi Magister Ilmu Kimia
Depositing User: Prof. Sutopo Hadi
Date Deposited: 13 Mar 2020 01:26
Last Modified: 13 Mar 2020 01:26
URI: http://repository.lppm.unila.ac.id/id/eprint/18659

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