How a Cheese-Making Enzyme Works Better with Certain Milk Protein Pieces
Peptide substrates for chymosin (rennin). Isolation and substrate behaviour of two tryptic fragments of bovine kappa casein.
Not medical advice. For informational purposes only. Always consult a healthcare professional. Terms
Surprising Findings
A mere 5-amino acid addition caused a 30-fold improvement in substrate efficiency.
Such a dramatic increase from a small structural change is unexpected; one might assume larger fragments or different regions would be needed for major functional changes.
Practical Takeaways
Understanding which protein segments enhance enzyme binding could help optimize dairy processing enzymes for faster or more efficient cheese production.
Not medical advice. For informational purposes only. Always consult a healthcare professional. Terms
Surprising Findings
A mere 5-amino acid addition caused a 30-fold improvement in substrate efficiency.
Such a dramatic increase from a small structural change is unexpected; one might assume larger fragments or different regions would be needed for major functional changes.
Practical Takeaways
Understanding which protein segments enhance enzyme binding could help optimize dairy processing enzymes for faster or more efficient cheese production.
Publication
Journal
European journal of biochemistry
Year
1980
Authors
S. Visser, P. J. VAN ROOIJEN, C. Slangen
Related Content
Claims (3)
Rennet cuts a protein on milk's tiny particles, making them clump together and turn into cheese curds.
Scientists found two tiny pieces of a milk protein, and one of them works better than the other when interacting with an enzyme used in cheese-making because it's easier for the enzyme to grab onto it.
Adding a few extra pieces to a milk protein fragment makes it work way better with an enzyme, because the enzyme grabs onto it more tightly.