Physiology and characterization of a fungal milk-clotting enzyme from Aspergillus flavus

Acta Microbiologica Polonica
|January 1, 1976
PubMed

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.