Yandri, Yandri and Suhartati, Tati and Hadi, Sutopo and Satria, Heri and Karlinasari, Surtini (2019) Enzymatic Conversion of Potato Starch into Glucose using The purified α-Amylase Enzyme from Locale Isolate Bacteria Bacillus subtillis ITBCCB148. In: Semirata & ICST Bengkulu 2019. (Submitted)

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Abstract

Abstract. 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, the researcher isolated and purified the α-amylase from locale isolate bacteria Bacillus subtillis ITBCCB148. The isolation of the extracellular α-amylase was conducted by using cold centrifuge method done to separate the enzyme from the cells. The purification of the α-amylase was examined by fractionation using ammonium sulphate salt followed by dialysis. The activity of the α-amylase enzyme was determined by using the Fuwa method and Mandels while the protein content was determined by using the Lowry method. Purified α-amylase obtained from 20–80% of ammonium sulphate saturation has specific activity 11312.64 U.mg-1. Regarding the purity, it was increased to 6.41 times compared with the crude one (1765.25 U.mg-1). On the other hand, the purification in dialysis step could increse the specific activity at 28834.13 U.mg-1, which the purity rose to 16.33 times higher than crude. 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 consentration could respectively produce glucose at 0.14; 0.33; 0.49; 0.72 and 0.71 mg.mL-1. The activity of α-amylase since it conversed the starch potato were respectively 26.54; 60.51; 91.18; 133.33 and 131.72 U.mL-1. In brief, The purified α-amylase enzyme is able to convert potato starch to glucose with an optimum concentration of potato starch 0.6%.

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. YANDRI AS
Date Deposited: 04 Nov 2019 08:28
Last Modified: 04 Nov 2019 08:28
URI: http://repository.lppm.unila.ac.id/id/eprint/15058

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