Substrate and binding specificity of aspartic proteases with milk clotting properties.
The hydrolysis of whole casein and isolated casein components were investigated with the purpose of obtaining information concerning the kinetic and specifty of aspartic proteases in rennin, pepsin and 4 microbial rennet substitutes. The velocity of hydrolysis decreased rapidly within the first hour. However, the hydrolysis was not completed after 2 days. A mathematical description of the slope of hydrolysis is possible by use of exponential equations. More than 40 peptides were detected by capillary electrophoresis or PAGE. The characterization of the C- and N-terminal amino acids of peptides shows that the hydrolysis of any peptide bond depends mainly on the structure of the C-terminal side chains of the amino acids. The detection of the basic amino acids lysin and arginin in the C-terminal position of peptides is a new result, furthering the knowledge about the specificity of aspartic proteases. Differences in the reaction velocity or in the extent of hydrolysis are one of the possible explanations for the described differences in the rennet curd yield. It was concluded that the rennet enzymes are active also in the later phases of cheese ripening and are able to support the action of cheese ripening flora.
Krause
W
W
Technical University of Dresden, Institute of Food Chemistry, Germany.
Partzsch
M
M
Hassan
Z M
ZM
Haufe
T
T
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D016282:Aspartic Acid Endopeptidases / Q000737:chemistry / Q000378:metabolism*; D002364:Caseins / Q000737:chemistry; D012085:Chymosin; D004591:Electrophoresis, Polyacrylamide Gel; D006868:Hydrolysis; D007700:Kinetics; D008892:Milk / Q000737:chemistry*; D013379:Substrate Specificity
D000596:Amino Acids; D002364:Caseins; D016282:Aspartic Acid Endopeptidases; D012085:Chymosin