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Physiology and characterization of a fungal milk-clotting enzyme from Aspergillus flavus
Abstract:
Aspergillus flavus produced extracellularly an active rennin-like enzyme when grown aerobically in whey media. The enzyme was detected at early stages of growth reaching a maximum after three to four days at 25 degrees. The activity was destroyed by heating to temperatures higher than 50 degrees, whereas the presence of skim milk during heating preserved the enzyme activity, at least, up to 70 degrees. Calcium chloride significantly stimulated the milk-clotting activity up to 1% final concentration. The clotting time was inversely proportional to protein concentration in the range 0.2-0.6 mg/ml and the enzyme exhibited marked stability when stored at 37 degrees at pH 6.
Insights
Aspergillus flavus secretes a rennin-like enzyme from whey. This enzyme clots milk, is heat-sensitive, but protected by skim milk, and stabilized by calcium chloride.
Area of Science:
- Microbiology
- Enzymology
- Food Science
Background:
- Rennin, crucial for cheesemaking, is traditionally sourced from animal stomachs.
- Exploring microbial sources for rennin-like enzymes offers potential alternatives.
- Aspergillus flavus is known to produce various extracellular enzymes.
Purpose of the Study:
- To investigate the production and properties of a rennin-like enzyme from Aspergillus flavus.
- To evaluate the enzyme's milk-clotting activity and stability under different conditions.
Main Methods:
- Cultivating Aspergillus flavus aerobically in whey media.
- Assessing enzyme activity at different growth stages and temperatures.
- Testing enzyme stability with heat, skim milk, calcium chloride, and pH variations.
Main Results:
- An active extracellular rennin-like enzyme was produced by Aspergillus flavus in whey.
- Optimal enzyme activity was observed after 3-4 days of growth at 25°C.
- Enzyme activity was heat-labile above 50°C but stabilized by skim milk up to 70°C.
- Calcium chloride (up to 1%) enhanced milk-clotting activity.
- Clotting time correlated inversely with protein concentration (0.2-0.6 mg/ml).
- The enzyme showed good stability at 37°C and pH 6.
Conclusions:
- Aspergillus flavus produces a promising rennin-like enzyme with potential applications in dairy processing.
- The enzyme's activity and stability can be modulated by environmental factors and additives.
- Further research could optimize production and explore its use as a rennin substitute.
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Fungal Group Zygomycota
Fungal Phylum Ascomycota