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Abstract:
The activity of phospholipase was studied in the cultural broth and cell extract of 112 strains of fungi and yeasts. The endoenzyme was detected in 19 strains of mycelial fungi, the exoenzyme was found in Mucor hiemalis 50 and Aspergillus niger 117. Phospholipase C of M. hiemalis was purified and compared to phospholipase of staphylococci. The values of Km are 8.9 and 1.07 mM, respectively, for the fungal and staphylococcal enzymes.
Insights
Researchers investigated phospholipase activity in fungi and yeasts, identifying exoenzymes in Mucor hiemalis and Aspergillus niger. Purified fungal phospholipase C showed distinct kinetic properties compared to staphylococcal enzymes.
Area of Science:
- Microbiology
- Enzymology
Background:
- Phospholipases are crucial enzymes involved in various biological processes.
- Fungal phospholipase activity is not fully characterized across diverse strains.
Purpose of the Study:
- To screen a collection of fungal and yeast strains for phospholipase activity.
- To characterize and compare fungal phospholipase C with its staphylococcal counterpart.
Main Methods:
- Screening of 112 fungal and yeast strains for endo- and exoenzyme activity.
- Purification of phospholipase C from Mucor hiemalis.
- Enzyme kinetic analysis (Km determination) and comparison with staphylococcal phospholipase.
Main Results:
- Phospholipase activity detected in 19 mycelial fungi strains.
- Exoenzyme activity identified in Mucor hiemalis and Aspergillus niger.
- Purified M. hiemalis phospholipase C exhibited a Km of 8.9 mM, differing from the staphylococcal enzyme's Km of 1.07 mM.
Conclusions:
- Specific fungal strains possess significant phospholipase activity.
- Fungal and staphylococcal phospholipases display distinct kinetic characteristics, suggesting structural and functional differences.