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Purification and characterization of an alkaline pectin lyase from Aspergillus flavus by Sangeeta Yadav; Pramod Kumar Yadav; Dinesh Yadav; Kapil Deo Singh Yadav is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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An alkaline pectin lyase secreted by Aspergillus flavus MTCC 7589 was purified to electrophoretic homogeneity using ammonium sulphate fractionation, anion exchange chromatography on DEAE cellulose and gel filtration chromatography on sephadex G-100. The pH and temperature optima of the enzyme were found to be 8.0 and 50 8C. The enzyme was found to be stable for 24 h in the pH range 4.0-10.0. The enzyme does not loose activity up to 50 8C if exposed for 1 h. Addition of ammonium sulphate in the range of 0.1-2.0 M increased the thermostability of the enzyme, 0.6 and 1.8 M of ammonium sulphate providing complete stability at 60 and 70 8C respectively. The values of K m and k cat of the enzyme were 0.59 mg/ml and 52.2 s À1 respectively. The molecular weight was found to be 38 AE 01 kDa. The purified enzyme showed efficacy in retting of Crotalaria juncea fibers.

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Author

Sangeeta Yadav; Pramod Kumar Yadav; Dinesh Yadav; Kapil Deo Singh Yadav

Publisher

Elsevier Science; Elsevier ; Elsevier Applied Science; Elsevier BV (ISSN 1873-3298)

Published

2008

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)