Proteolysis in cheddar cheese made with alternative coagulants

A fermentation-produced chymosin (Chymogen) and three fungal coagulants derived from Rhizomucor miehei (Fromase and Marzyme) and Cryphonectria parasitica (Thermolase) were assessed in cheddar cheese manufacture for their effect on proteolysis. During maturation, proteolysis, particularly the formation of larger peptides, was greater in the cheeses manufactured using the Thermolase coagulant, while protein degradation rates were similar in the Chymogen, Fromase and Marzyme cheeses. All coagulants were able to degrade α s1 -casein with the Chymogen and Thermolase coagulants generally the more active. In cheese manufactured with Thermolase coagulant, β-casein was degraded relatively rapidly, whereas in the Chymogen manufactured cheese β-casein hydrolysis was restricted. The Fromase and Marzyme coagulants were intermediate in their activity on β-casein. There were also consistent differences in the reversed phase high-performance liquid chromatography (HPLC) peptide patterns of the cheeses during maturation with the Thermolase coagulant forming a greater number and often increased concentrations of peptides. Cluster analysis (CA) and multi-dimensional scaling (MDS) were used to objectively differentiate the reversed phase-HPLC peptide patterns.