ENZYMIC STUDIES OF &-AMYLASE FROM SUGARCANE LEAVES (Saccharum officinarum L.)
Abstract
- In this research, &-amylase enzyme [EC 3.2.1.1] was extracted from sugarcane leaves (Saccharum officinarum L.) and the &-amylase activity was measured by Nelson-Somogyi method. The optimum pH and the optimum temperature were found to be 5.0 and 50.C respectively. The protein content of the enzyme was determined by using Biuret method. The purification of &-amylase extracted from sugarcane leaves was carried out by using ammonium sulphate precipitation method and Sephadex G-100 gel chromatographic method. The specific activity (the relative purity of the enzyme) increased about 7 folds from crude to final purification step. The homogeneity of the purified &-amylase was confirmed by non-sodium dodecyl sulphate polyacrylamide gel electrophoresis (non SDS-PAGE). The purified &-amylase enzyme showed a single band on non SDS-PAGE. An estimated molecular weight of purified &-amylase from sugarcane leaves sample was found as 57543 Dalton. In this research, immobilization of purified &-amylase was carried out on oxycellulose support. Then the optimum pH, optimum temperature and storage stability of immobilized &-amylase were determined. The pH and temperature profile of free and immobilized &-amylase enzyme were very similar in nature. There were the same optimum pH 5.0 and optimum temperature 50°C. In the case of storage stability, the immobilized enzyme was more stable than free enzyme. During 15 days storage time at 4°C free &-amylase enzyme lost 49.39 % of original activity, whereas immobilized one lost only 4.56 % of original activity.
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Year
- 2019
Author
-
Hla Hla Pyone Lwin
Subject
- Chemistry
Publisher
- Myanmar Academy of Arts and Science (MAAS)