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Pakistan Journal of Biological Sciences

Year: 2001 | Volume: 4 | Issue: 10 | Page No.: 1271-1274
DOI: 10.3923/pjbs.2001.1271.1274
Purification and Properties of Invertase from Mango Fruit
M. Habibur Rahman, A.S.M. Aynul Haque Akand, Tanzima Yeasmin, Md. Salim Uddin and Mahbubur Rahman

Abstract: A mango invertase was purified from the flesh of Himsagar variety to an electrophoretically homogeneous state, by successive ion-exchange chromatography on DEAE-Cellulose and CM-Cellulose column chromatography. The molecular weight of the purified enzyme was 68 kDa in gel filtration chromatography and 65.5 kDa on SDS-polyacrylamide gel electrophoresis. However, SDS-polyacrylamide gel electrophoresis revealed four bands, indicating that the enzyme was a tetramer. The enzyme was a glycoprotein as it gave yellow-orange colour in the presence of phenol sulphuric acid. The optimum pH for the enzyme was 4.5 and the enzyme was found to be stable from pH 2.5 to 8. The optimum temperature for enzyme was 75°C and the enzyme was stable between 10 - 75°C. The Km for sucrose was 5.25 mM (pH 4.5). The activities of enzyme were remarkably enhanced by Cu++, K+, Ca++ whereas, completely ceased by Hg++ and sodium dodecylsulfate.

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How to cite this article
M. Habibur Rahman, A.S.M. Aynul Haque Akand, Tanzima Yeasmin, Md. Salim Uddin and Mahbubur Rahman, 2001. Purification and Properties of Invertase from Mango Fruit. Pakistan Journal of Biological Sciences, 4: 1271-1274.

Keywords: himsager, mangifera indica, properties and invertase

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