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Rennin (chymosin, CAS 9001‑98‑3) is a proteolytic enzyme traditionally extracted from calf stomach, now largely produced via microbial fermentation. It specifically cleaves casein in milk, triggering curd formation and separating curds from whey. Approved as food‑processing enzyme, it is the key coagulant for cheese manufacturing. It optimises curd texture, yield and flavour development. It has no preservative function and is mostly inactivated during later cheese‑making heating steps.
Rennin, also named chymosin (CAS 9001‑98‑3), is a proteolytic enzyme. Originally isolated from calf abomasum, modern commercial rennin is mostly obtained by microbial fermentation. Approved by JECFA as a food‑processing aid, its core biochemical function is to cleave κ‑casein in milk, destabilise casein micelles and trigger milk coagulation, separating solid curd from liquid whey.
Its dominant and most important application is cheese production. When added into warmed milk, rennin hydrolyses κ‑casein. After enzymatic cleavage, milk forms firm curds, which are cut, stirred and pressed to expel whey. This process lays the foundation for cheese texture, moisture content and final yield. Compared with alternative coagulants, rennin produces elastic, compact curds, reduces fat loss into whey, and supports normal flavour ripening during ageing. It is widely used for hard, semi‑hard and soft cheese varieties such as cheddar, gouda and mozzarella.
Rennin influences subsequent ripening behaviour of finished cheese. Residual active enzyme trapped inside curd continues limited proteolysis during maturation. It breaks down large milk proteins into smaller peptides, generating desirable flavour compounds and preventing overly rubbery texture. Excessive residual activity, however, causes unwanted bitterness, so manufacturers control enzyme dosage, temperature and holding time carefully.
Apart from mainstream cheese‑making, rennin has limited secondary usage. It is occasionally applied in the manufacture of some fermented milk‑based desserts and curd‑type dairy snacks, yet it is rarely used for yoghurt, where acid‑driven coagulation dominates. Rennin is not deployed in non‑dairy food systems, as it acts specifically on milk casein.
As a processing‑aid enzyme, rennin is not a preservative. It cannot inhibit bacteria or mould growth. Partial enzyme inactivation occurs during heating, cooking and cheese maturation. Animal‑sourced rennin is gradually replaced by recombinant microbial chymosin, which offers stable performance, consistent quality and avoids supply constraints from calf stomach sources.
In summary, rennin is the primary milk‑coagulating enzyme for cheese manufacture. Its key food function is milk curd formation, optimising curd quality, product yield and cheese ripening characteristics. Enzyme dosage and reaction parameters require precise tuning to avoid bitter defects. Microbial recombinant chymosin has become the mainstream commercial form. It functions only as processing aid and does not serve as preservative, antioxidant or nutritional additive in final food products.
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