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R4877

Sigma-Aldrich

Rennin from calf stomach

≥20 units/mg protein

Sinónimos:

Chymosin

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About This Item

Número de CAS:
9001-98-3
Comisión internacional de enzimas:
3.4.23.4 (BRENDA, IUBMB)
EC Number:
232-645-0
MDL number:
MFCD00132173
UNSPSC Code:
12352204
NACRES:
NA.54

form

lyophilized powder

specific activity

≥20 units/mg protein

purified by

crystallization

composition

Protein, ≥40%

storage temp.

−20°C

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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 .

Biochem/physiol Actions

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.

Packaging

Package size based on protein content

Unit Definition

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

Physical form

Lyophilized powder containing sodium chloride

Analysis Note

Protein determined by biuret.

pictograms

Health hazardExclamation mark
GHS08,GHS07

signalword

Danger

Hazard Classifications

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

target_organs

Respiratory system

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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Pepsina from porcine gastric mucosa powder, ≥250 units/mg solid

Sigma-Aldrich

P7000

Pepsina from porcine gastric mucosa

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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