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Key Documents

Autres documents

R4877

Sigma-Aldrich

Rennin from calf stomach

≥20 units/mg protein

Synonyme(s) :

Chymosin

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About This Item

Numéro CAS:
9001-98-3
Numéro de classification (Commission des enzymes):
3.4.23.4 (BRENDA, IUBMB)
Numéro CE :
232-645-0
Numéro MDL:
MFCD00132173
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54

Forme

lyophilized powder

Niveau de qualité

200

Activité spécifique

≥20 units/mg protein

Produit purifié par

crystallization

Composition

Protein, ≥40%

Température de stockage

−20°C

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Catégories apparentées

Application

Rennin, also known as chymosin, is a milkclotting acid proteinase produced in the stomach of a calf. It is used in cheesemaking and to study neonatal gastric digestion .

Actions biochimiques/physiologiques

Rennin, a 323 amino acid chain, is secreted as an inactive precursor which is then converted into an active enzyme through limited proteolysis. It cleaves the peptide bond between phenylalanine and methionine in K-Casein.

Conditionnement

Package size based on protein content

Définition de l'unité

One unit will coagulate 10 mL of milk per min at 30 °C.

Forme physique

Lyophilized powder containing sodium chloride

Remarque sur l'analyse

Protein determined by biuret.

Pictogrammes

Exclamation markHealth hazard
GHS07,GHS08

Mention d'avertissement

Danger

Mentions de danger

H315 - H319 - H334 - H335

Classification des risques

Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3

Organes cibles

Respiratory system

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Certificats d'analyse (COA)

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Sigma-Aldrich

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Sigma-Aldrich

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B Foltmann et al.
The Journal of biological chemistry, 254(17), 8447-8456 (1979-09-10)
The complete amino acid sequence of calf chymosin (rennin) (EC 3.4.23.4) has been determined. The sequence consists of a single peptide chain of 323 amino acid residues. The primary structure of the precursor part of calf prochymosin was published previously
Kirsten Kastberg Møller et al.
Journal of agricultural and food chemistry, 60(21), 5454-5460 (2012-05-09)
Bovine chymosin constitutes a traditional ingredient for enzymatic milk coagulation in cheese making, providing a strong clotting capacity and low general proteolytic activity. Recently, these properties were surpassed by camel chymosin, but the mechanistic difference behind their action is not
Xin-ping Li et al.
Xi bao yu fen zi mian yi xue za zhi = Chinese journal of cellular and molecular immunology, 28(7), 715-717 (2012-07-10)
To optimize the prochymosin (pCHY) gene codons and express the gene in Escherichia coli (E.coli), and to prepare its antiserum and detect chymosin protein specifically. According to codon usage bias of E.coli, prochymosin gene sequence was synthesized based on the
Neil D Rawlings et al.
Nucleic acids research, 40(Database issue), D343-D350 (2011-11-17)
Peptidases, their substrates and inhibitors are of great relevance to biology, medicine and biotechnology. The MEROPS database (http://merops.sanger.ac.uk) aims to fulfil the need for an integrated source of information about these. The database has hierarchical classifications in which homologous sets
G L Gilliland et al.
Advances in experimental medicine and biology, 306, 23-37 (1991-01-01)
Many aspects of the structure of chymosin are quite unique even though structure comparisons indicate a high degree of structural homology with other eukaryotic aspartic proteinases. The structural homology is shown to be directly related to the sequence homology which
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