Physiology and characterization of a fungal milk-clotting enzyme from Aspergillus flavus.
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.
D000818:Animals; D001231:Aspergillus flavus / Q000201:enzymology*; D002118:Calcium / Q000494:pharmacology; D003470:Culture Media; D010450:Endopeptidases / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D008892:Milk; D010447:Peptide Hydrolases / Q000096:biosynthesis; D012965:Sodium Chloride / Q000378:metabolism; D013696:Temperature
D003470:Culture Media; D012965:Sodium Chloride; D010450:Endopeptidases; D010447:Peptide Hydrolases; D002118:Calcium