Purification and Characterization of Invertase from Aspergillus Fumigatus and Penicillium Brevicompactum
C. Uma* and K. Chandra kumar
Department of Biochemistry, School of Life sciences, Karpagam University, Coimbatore - 641 021 India.
Corresponding Author E-mail:umaradhakrishnan29@gmail.com
ABSTRACT: Invertase was isolated from selected soil micro organism namely A.fumigatus and P. brevicompactum, the enzyme was purified by ammonium sulfate precipitation and Ion Exchange chromatography. The purification fold was 7.85 for A.fumigatus and 6.35 for P.brevicompactum. The enzyme showed maximum activity at pH 6 and optimum temperature was 50o C at a substrate concentration of 1.0 gm. The activiy of the enzyme was inhibited by divalent metal ion Zn 2+ where as activated by Na+. Immobilisation by sodium alginate method increased the stability of the enzyme.
KEYWORDS: Invertase; Aspergillus fumigatus; Penicillium brevicompactum.
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Copy the following to cite this article: Uma C, Kumar K. C. Purification And Characterization Of Invertase From Aspergillus Fumigatus And Penicillium Brevicompactum. Biosci Biotech Res Asia 2010;7(1) |
Copy the following to cite this URL: Uma C, Kumar K. C. Purification And Characterization Of Invertase From Aspergillus Fumigatus And Penicillium Brevicompactum. Biosci Biotech Res Asia 2010;7(1). Available from: https://www.biotech-asia.org/?p=9599 |