The Role of Microbial Aspartic Protease Enzyme in Food and Beverage Industries
Table 3
Microbial sources of milk-clotting aspartic proteases [13].
Microorganisms
Properties
Pleurotus sojur-caju (white rot fungi)
Clotting activity under cheese-making conditions
Mucor bacilliformis
High structural similarity to bovine chymosin lower thermostablity than Rhizomucor miehei protease
Thermoascus aurantiacus
Enzymatic hydrolysis of bovine casein differed largely from proteolysis patterns generated by bovine chymosin
Thermomucor indicae-seudaticae N31
Crude enzymatic extract showed high milk-clotting and low proteolytic activity and low thermostability
Metschnikowia reukaufii
Milk-clotting activity, successfully cloned into Escherichia coli
Myxococcus xanthus
Molecular mass: 40 kDa, highest clotting activity at pH 6 and 37°C, acceptable yield and properties of the curd in cheese-making experiments, successfully cloned into Escherichia coli
Enterococcus faecalis
Similar electrophoretic patterns of hydrolyzed k-casein as Rhizomucor miehei, effectively applied for camembert cheese manufacture
Nocardiopsis sp.
Milk-clotting ability of extracellular extracts, optimization of enzyme yield by fermentation conditions
Bacillus subtilis
Ratio of milk clotting to proteolytic activity is comparable with commercial fungal protease but has high thermostability
