Witazora, Y and Yandri, Yandri and Suhartati, Tati and Satria, Heri and Hadi, Sutopo (2020) Effect of glutaraldehyde addition on the stability of the α-amylase from Bacillus subtilis ITBCCB148. In: International Conference on Applied Sciences Mathematics and Information (ICASMI) 3 2020, 3-4 September 2020, Bandar Lampung.

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α-Amylase is widely used in industry because of its ability to hydrolyze starch to glucose. Limited enzyme activity in extreme pH and temperature makes it necessary to increase enzyme stability. The purpose of this study was to improve the stability of the α-amylase from the bacteria Bacillus subtilis ITBCCB148 by chemical modification using glutaraldehyde (GA). The results showed that the specific activity of the α-amylase from the purification of 4,008.733 U/mg increased 5 times compared to the crude extract of the enzyme which had a specific activity of 787.851 U/mg. This native enzyme has an optimum pH of 5.5; optimum temperature of 50oC; KM = 2.08 mg/mL substrate; Vmax = 188.68 μmol mL-1 min-1; ki = 0.0298 min-1; t1/2 = 23.26 min and ΔGi = 99.829 kJ mol-1. Modified enzymes using glutaraldehyde 0.01; 0.03 and 0.05% have an optimum pH of 5.5; optimum temperature of 55oC; KM of 4.74; 5.03 and 3.87 mg/mL substrate,; the Vmax of 285.71; 270.27 and 212.77 μmol mL-1 min-1; ki of 0.0183; 0.0111 and 0.0160 min-1; half-life (t1/2) 37.87; 62.43 and 43.31 min; ΔGi 101.091; 102.365 and 101.407 kJ mol-1, respectively. Chemical modification of the α-amylase from B. subtilis ITBCCB148 using glutaraldehyde can increase thermal stability by 1.6-2.7 times which can be seen from a decrease in the value of ki, an increase in half-life and ΔGi.

Item Type: Conference or Workshop Item (Speech)
Subjects: Q Science > QD Chemistry
Divisions: Fakultas Matematika dan Ilmu Pengetahuan Alam (FMIPA) > Prodi Kimia
Depositing User: Prof. Sutopo Hadi
Date Deposited: 12 Nov 2020 08:36
Last Modified: 12 Nov 2020 08:36
URI: http://repository.lppm.unila.ac.id/id/eprint/25060

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