Production and characterization of a milk-clotting protease in the crude enzymatic extract from the newly isolated Thermomucor indicae-seudaticae N31: (Milk-clotting protease from the newly isolated Thermomucor indicae-seudaticae N31)

摘要: Abstract Microbial rennet-like milk-clotting enzymes are aspartic proteinases that catalyze milk coagulation, substituting calf rennet. Crude enzymatic extract produced by the thermophilic fungus, Thermomucor indicae-seudaticae N31, on solid state fermentation (SSF) using wheat bran, exhibited high activity and low proteolytic after 24 h of fermentation. Highest (MCA) was at pH 5.7, 70 °C in 0.04 M CaCl2; it stable pH range 3.5–4.5 for up to 45 °C 1 h. MCA highly inhibited pepstatin A. Hydrolytic profile crude whole bovine casein, analyzed gel electrophoresis (Urea–PAGE) RP-HPLC revealed action towards casein fractions a peptide similar one obtained with commercial Rhizomucor miehei protease (Hannilase).