Karlinasari, Surtini and Suhartati, Tati and Satria, Heri and Hadi, Sutopo and Yandri, Yandri (2020) Enzymatic Conversion of Potato Starch into Glucose using The purified α-Amylase Enzyme from Locale Isolate Bacteria Bacillus subtillis ITBCCB148. Proceeding 2nd International Conference on Science and Technology, 2019 (1). pp. 36-42. ISSN 9786025830198


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The objective of this study was to determine the ability of the purified α-amylase enzyme to convert potato starch into glucose. For this objective, we isolated and purified α-amylase from locale bacteria isolate Bacillus subtillis ITBCCB148. The isolation of the extracellular α-amylase was conducted by the use of cold centrifuge method which was carried out to separate the enzyme from the cells. The purification of α-amylase was examined by fractionation using ammonium sulphate followed by dialysis. The activity of α-amylase was determined using the Fuwa method and Mandels while the protein content was determined using the Lowry method. The purified α-amylase obtained from 20–80% of saturated ammonium sulphate has specific activity of 11312.64 U.mg-1. Based on the purity, it was increased to 6.41 times compared to the crude enzyme (1765.25 U.mg-1). Furthermore, the purification in dialysis step was able to increse the specific activity at 28834.13 U.mg-1, where the purity rose to 16.33 times higher than the crude enzyme. The purified enzyme had an optimum pH at 5 and optimum temperature at 65oC. The purified amylase from dialysis step was then applied for enzymatic conversion with various concentrations of potato starch 0.1; 0.2; 0.4; 0.6 and 0.8 % respectively to produce glucose. These starch concentration was able to produce glucose at 0.14; 0.33; 0.49; 0.72 and 0.71 mg.mL-1, respectively. The activity of α-amylase in the conversion of starch potato were 26.54; 60.51; 91.18; 133.33 and 131.72 U.mL-1 respectively. In conclusion, the purified α-amylase enzyme was able to convert potato starch to glucose with an optimum concentration of potato starch 0.6%.

Item Type: Article
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 02:13
Last Modified: 12 Nov 2020 02:13
URI: http://repository.lppm.unila.ac.id/id/eprint/24968

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