For research use only. Not for therapeutic Use.
Rennin, also known as Chymosin, is a pepsin-related proteolytic enzyme synthesized by cells in the stomach of certain animals that efficiently converts liquid milk into a semi-solid, allowing it to remain in the stomach for longer. The natural substrate of Rennin is K-casein, which is specifically cleaved at the peptide bond between amino acid residues 105 and 106, phenylalanine and methionine, and is widely used in cheese production[1].
This product is derived fro M plant separation and can be used for emulsion coagulation. The amount of chymosin added is directly proportional to the coagulation time. The more added, the faster the coagulation time.
Molecular weight: 36 KDa
Temperature range: effective temperature range 35-95 ℃, optimal temperature 35-37 ℃;
pH range: effective p h range 5-8, optimal ph value 6 1 6 2;
Inhibitors: Fe3+、Cu2+、Hg+、Pb+
Solvent: water
| Catalog Number | I041900 |
| CAS Number | 9001-98-3 |
| Purity | ≥95% |
| Reference | [1]. Gilliland GL, et al. Dill J. Functional implications of the three-dimensional structure of bovine chymosin. Adv Exp Med Biol. 1991;306:23-37. |
