Influence of milk protein concentration on the gelling activity of chymosin and bovine pepsin
- 1 February 1980
- journal article
- research article
- Published by Cambridge University Press (CUP) in Journal of Dairy Research
- Vol. 47 (1) , 103-111
- https://doi.org/10.1017/s0022029900020938
Abstract
Summary: Two stages of gelling by the milk-clotting enzymes chymosin and pepsin were studied at different milk protein concentrations, using milk retentates. In each case, enzymic velocity versus protein concentration described a standard hyperbola. According to the experimental conditions such as pH and type of enzyme, which changed the enzyme concentration used, either the quasi-linear part of the hyperbola was observed, or the velocity hardly increased and tended to a limiting value. Gelling occurred with a lower degree of proteolysis of κ-casein when the protein concentration increased but a minimum proteolysis (1% of total nitrogenous matter content) was required for aggregation to take place. Gelling time varied with the protein concentration, the pH and the enzyme concentration. The final degree of proteolysis of κ-casein was the same whatever the substrate concentration used.This publication has 21 references indexed in Scilit:
- On enzymatic clotting processesBiophysical Chemistry, 1977
- A rennin-sensitive bond in αs1Β-caseinJournal of Dairy Research, 1974
- Kinetics of rennin action on casein prepared by ultracentrifugationJournal of Dairy Research, 1973
- The action of rennets on the caseins: I. Rennin action on β-casein-B in solutionJournal of Dairy Research, 1971
- κ-Casein and Its Attack by Rennin (Chymosin)Published by Elsevier ,1971
- The action of calf rennet and other proteolytic enzymes on κ-caseinJournal of Dairy Research, 1969
- Fractionation of S-Carboxymethyl-κ-casein and characterization of the componentsBiochimica et Biophysica Acta (BBA) - General Subjects, 1965
- Caseino-glycopeptides: Characterization of a methionine residue and of the N-terminal sequenceBiochemical and Biophysical Research Communications, 1965
- Amino acid composition of κ-casein and terminal amino acids of κ- and para-κ-caseinArchives of Biochemistry and Biophysics, 1962
- Das Lab und seine Wirkung auf das Casein der Milch. VII. Über die Abspaltung von Nicht‐Protein‐Stickstoff (NPN) aus Casein durch Lab und ihre Beziehung zur Primärreaktion der Labgerinnung der MilchHelvetica Chimica Acta, 1953