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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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Sigma-Aldrich

P7000

Pepsina from porcine gastric mucosa

Jung-Feng Hsieh et al.
Journal of agricultural and food chemistry, 60(8), 2039-2045 (2012-02-07)
Chymosin-induced coagulation of individual milk proteins during incubation at 30 °C was investigated using a proteomic approach. The addition of chymosin (0.006 units/mL) caused the milk proteins to coagulate after a 3 h incubation period. Approximately 88% of the milk
X P Jiang et al.
World journal of microbiology & biotechnology, 28(5), 2087-2093 (2012-07-19)
Chymosin can specifically break down the Phe105-Met106 peptide bond of milk κ-casein to form insoluble para-κ-casein, resulting in milk coagulation, a process that is used in making cheese. In this study, in order to obtain an alternative milk coagulant which
Filiz Kazak et al.
Veterinary research forum : an international quarterly journal, 13(4), 593-596 (2023-01-24)
Epidermal growth factor (EGF) has biological roles, including embryonic organ development, breast morphogenesis, breast cell proliferation, and mammary development. This study aimed to measure EGF concentration and evaluate its relationship with somatic cell count (SCC) in healthy water buffaloes (Bubalus
J A Vallejo et al.
Journal of dairy science, 95(2), 609-613 (2012-01-28)
The first step in cheesemaking is the milk clotting process, in which κ-caseinolytic enzymes contribute to micelle precipitation. The best enzyme for this purpose is chymosin because of its high degree of specificity toward κ-casein. Although recombinant bovine chymosin is
Katarina Kosalková et al.
Microbial cell factories, 11, 5-5 (2012-01-12)
The secretion of heterologous animal proteins in filamentous fungi is usually limited by bottlenecks in the vesicle-mediated secretory pathway. Using the secretion of bovine chymosin in Aspergillus awamori as a model, we found a drastic increase (40 to 80-fold) in
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