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==Molecular action of rennet enzymes== One of the main actions of rennet is its [[protease]] [[chymosin]] cleaving the kappa [[casein]] chain.<ref>{{Cite web | url=https://www.thecourtyarddairy.co.uk/blog/cheese-musings-and-tips/rennet-in-cheese-the-science-how-rennet-works/ | title=Rennet in cheese - the science: How rennet works| date=2013-06-12}}</ref> [[Casein]] is the main protein of [[Milk#Proteins|milk]]. Cleavage removes the slightly negatively charged [[glycomacropeptide]] (GMP) from the surface of the casein micelle. Because negative charges repel other negative charges, the GMP prevents casein micelles from adhering to each other. With the GMP removed, the casein micelles can begin to cluster and lose their polar charge, causing them to rise out of the polar water molecules and join non-polar milk fat as a portion of the cheese curd. This action is enhanced in the presence of strong ions like those formed from calcium and phosphate. As such, those chemicals are occasionally added to supplement pre-existing quantities in the cheese making process, especially in calcium phosphate-poor goat milk. The solid truncated casein protein network traps other components of milk, such as fats and minerals, to create cheese.{{citation needed|date=July 2023}}
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