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.

3

Pro

0

Against

Evidence from Studies

Supporting (1)

3

Community contributions welcome

3

Peptide substrates for chymosin (rennin). Isolation and substrate behaviour of two tryptic fragments of bovine kappa casein.

Cross-Sectional Study

In Vitro

1980 Jul

The study tested the same two protein pieces mentioned in the claim and found the longer one works much better with the enzyme because it binds more easily.

Contradicting (0)

0

Community contributions welcome

No contradicting evidence found

Gold Standard Evidence Needed

According to GRADE and EBM methodology, here is what ideal scientific evidence would look like to definitively prove or disprove this specific claim, ordered from strongest to weakest evidence.

Source Study

Peptide substrates for chymosin (rennin). Isolation and substrate behaviour of two tryptic fragments of bovine kappa casein.

Score: 3

DOI: 10.1111/J.1432-1033.1980.TB04737.X

Similar Assertions

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.

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A specific spot on a milk protein might help an enzyme work better by sticking to it with a kind of molecular magnetism.

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In a specific part of a milk protein, both the histidine and proline building blocks help an enzyme called chymosin do its job in lab tests, and neither one is more important than the others.

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Some specific parts of a milk protein help it stick in the right spot on an enzyme, making it easier to cut and activate in lab tests.

4

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In milk protein, certain 'Pro' building blocks act like tiny braces that hold the protein in the right shape so an enzyme can cut it cleanly at a specific spot in a lab setting.

4

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