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Pectin transeliminase complex from Aspergillus flavus
O Famurewa1, M A Oyede, P O Olutiola
1Department of Microbiology, Ondo State University, Ado-Ekiti, Nigeria.
Folia Microbiologica
|January 1, 1993
Summary
Aspergillus flavus produces pectin-degrading enzymes, identified as transeliminases. Enzyme production is inhibited by common sugars, and the active enzymes were purified and characterized.
Area of Science:
- Microbiology
- Enzymology
- Biochemistry
Background:
- Pectin degradation is crucial in various biological and industrial processes.
- Understanding microbial enzymes involved in pectin breakdown is essential for biotechnological applications.
Purpose of the Study:
- To investigate the production and characterization of pectinolytic enzymes from Aspergillus flavus.
- To identify and purify the specific enzymes responsible for pectin degradation.
Main Methods:
- Aspergillus flavus was cultured in pectin-containing medium.
- Extracellular enzymes were purified using ultrafiltration, ammonium sulfate precipitation, and chromatography (molecular exclusion and ion-exchange).
- Enzyme activity, optimal conditions, and kinetic parameters were determined.
Main Results:
- Aspergillus flavus produced extracellular enzymes degrading pectin via transeliminase activity.
- Enzyme synthesis was repressed by sucrose, glucose, fructose, and maltose.
- Purified fractions (I and II) showed optimal activity at pH 8.5 and 35°C, requiring divalent cations and inhibited by EDTA.
Conclusions:
- Aspergillus flavus possesses transeliminase enzymes capable of degrading pectin.
- These enzymes are subject to catabolite repression by common sugars.
- Characterization provides insights into their biochemical properties for potential applications.