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[Aminopeptidase system of Aspergillus flavus]
Ukrains'Kyi Biokhimichnyi Zhurnal
|January 1, 1977
Summary
Researchers investigated aminopeptidases synthesized by Aspergillus flavus, identifying distinct leucine aminopeptidase and aminotripeptidase enzymes. Multiple forms of these enzymes were discovered, each with unique properties.
Area of Science:
- Biochemistry
- Enzymology
- Microbial Biochemistry
Background:
- Aspergillus flavus synthesizes a complex of exocellular peptidohydrolases.
- Aminopeptidases play crucial roles in protein metabolism and peptide hydrolysis.
Purpose of the Study:
- To characterize the aminopeptidase system produced by Aspergillus flavus.
- To separate and identify individual aminopeptidase enzymes within the complex.
Main Methods:
- Salt fractionation techniques were employed for initial enzyme separation.
- Chromatographic methods, including DEAE-Sephadex A-50 and DEAE-cellulose, were used for purification.
- Enzyme properties such as solubility, specific activity, and thermostability were analyzed.
Main Results:
- The study successfully separated leucine aminopeptidase, aminotripeptidase, and a specific leucyl-glycyl-glycine aminopeptidase.
- Multiple anionic and cationic forms of these enzymes were identified, exhibiting variations in purification degree and properties.
- Evidence suggests the presence of at least two distinct leucine aminopeptidases based on differential hydrolysis of leucinamide and leucyl-glycine.
Conclusions:
- The aminopeptidase system of Aspergillus flavus is complex, comprising multiple distinct enzymes.
- The identified multiple enzyme forms possess unique biochemical and physical characteristics.
- The findings indicate that different enzymes are responsible for the hydrolysis of leucinamide and leucyl-glycine, refuting a single enzyme catalysis.