1987/04/05 by Alfred Carlson, Charles G. Hill, N.F. Olson · 45 citations
Biochemistry, Genetics and Molecular Biology · Agricultural and Biological Sciences · Chemistry · #Protein Hydrolysis and Bioactive Peptides #Proteins in Food Systems #Aquaculture Nutrition and Growth #Chemistry #Casein #Kinetics #Enzyme #Hydrolysis #Chromatography #Coagulation #Enzyme kinetics #Pepsin #Biochemistry #Active site
paper · doi:10.1002/bit.260290507
published in Biotechnology and Bioengineering 29(5), 582-589 (Wiley)
openalex publication_date 1987/04/05 · openalex created_date 2025/10/10 · openalex updated_date 2026/06/26
The kinetics of the primary phase of the enzymatic coagulation of milk, i.e., kappa-casein hydrolysis, was investigated in the presence and in the absence of concurrent enzyme deactivation processes. For conditions under which the enzyme is stable, the rate of hydrolysis can be described by Michaelis-Menten kinetics, as has been reported by previous investigators. A mathematical model, experimental data, and parameter estimates are provided for kappa-casein hydrolysis in the presence of concurrent deactivation of enzyme. The model accurately describes the experimental results when porcine pepsin was used as the renneting enzyme. The model and the experimental results indicate that samples of milk treated under conditions where deactivation of enzyme is significant can have fractional conversions of kappa-casein ranging from zero to unity and yet contain no active enzyme at the termination of the treatment.