作者: Trevor M. D'Souza , Lancelot Pereira
DOI: 10.3168/JDS.S0022-0302(82)82464-8
关键词: Rennet 、 Biochemistry 、 Chemistry 、 Ammonium sulfate 、 Bacillus licheniformis 、 Protease 、 Fractionation 、 Calcium 、 Mucor 、 Enzyme 、 Food science 、 Animal Science and Zoology 、 Genetics
摘要: Abstract An extracellular milk-clotting enzyme was obtained from a strain of Bacillus licheniformis isolated raw milk. Production studies improved yield the enzyme. The purified partially by fractionation with 70% ammonium sulfate. Milk-clotting properties were investigated and compared to corresponding Mucor miehei protease, chymosin-like Maximum activity both enzymes in milk at 65°C added calcium chloride dihydrate concentration 50mM. bacterial had maximum pH 5.0 5.5 protease 5.0. Both showed high inactivation after heating for 3min above 65°C. immobilized embedding paraffin wax. This immobilization technique no appreciable effect on factors affecting enzymes, such as pH, temperature, 2+ concentration. used continuous system.