Page last updated: 2024-11-07

chymosin

Description Research Excerpts Clinical Trials Roles Classes Pathways Study Profile Bioassays Occurs in Manufacturing Related Drugs Related Conditions Protein Interactions Research Growth Market Indicators

Description

Chymosin is an aspartic protease enzyme that is naturally produced in the stomachs of ruminant mammals, primarily calves. It plays a crucial role in the digestion of milk by cleaving the milk protein casein, specifically at the phenylalanine-methionine bond. This cleavage results in the formation of para-kappa-casein, which leads to the coagulation of milk. Chymosin is commercially produced using genetically modified microorganisms, such as Aspergillus niger, and is used in the cheesemaking process. The enzyme's ability to coagulate milk efficiently and produce high-quality cheese makes it a critical component in the dairy industry. Research on chymosin focuses on optimizing its production, understanding its enzymatic properties, and exploring alternative sources for its production. The study of chymosin also extends to its potential use in other applications, such as the production of bioactive peptides and the development of novel medical treatments.'

Chymosin: The predominant milk-clotting enzyme from the true stomach or abomasum of the suckling calf. It is secreted as an inactive precursor called prorennin and converted in the acid environment of the stomach to the active enzyme. EC 3.4.23.4. [Medical Subject Headings (MeSH), National Library of Medicine, extracted Dec-2023]

Cross-References

ID SourceID
PubMed CID115709
MeSH IDM0018781

Synonyms (2)

Synonym
chymosin
rennin

Research Excerpts

Overview

Chymosin is a predominant enzyme in rennet and is used in cheese production because of its excellent milk-clotting activity. It is an extremely specific aspartatic protease responsible for milk coagulation.

ExcerptReferenceRelevance
"Chymosin is a predominant enzyme in rennet and is used in cheese production because of its excellent milk-clotting activity. "( A novel electrochemical assay for chymosin determination using a label-free peptide as a substrate.
Li, CP; Liu, F; Zhao, H; Zheng, J, 2021
)
2.34
"Chymosin is a commercially important enzyme in the manufacturing of cheese. "( Hot-spot mapping of the interactions between chymosin and bovine κ-casein.
Palmer, DS; Schiøtt, B; Sørensen, J, 2013
)
2.09
"Chymosin is a protease that cleaves specifically caseins."( Rapid quantification of casein in skim milk using Fourier transform infrared spectroscopy, enzymatic perturbation, and multiway partial least squares regression: Monitoring chymosin at work.
Baum, A; Hansen, PW; Mikkelsen, JD; Nørgaard, L; Sørensen, J, 2016
)
1.35
"Chymosin is an important industrial enzyme widely used in cheese manufacturing. "( Disruption of PMR1 in Kluyveromyces lactis improves secretion of calf prochymosin.
Feng, Z; Ren, J; Zhang, H; Zhang, L, 2011
)
2.04
"Chymosin is an important industrial enzyme widely used in cheese manufacture. "( [Gene synthesis of the bovine prochymosin gene and high-level expression in Kluyvermyces lactis].
Chu, X; Du, M; Hu, F; Hui, F; Ke, T; Yuan, W, 2010
)
2.08
"Chymosin is an extremely specific aspartatic protease responsible for milk coagulation. "( Assignment of human prochymosin pseudogene to chromosome 1.
Alhonen, L; Hyttinen, JM; Jänne, J; Kolmer, M; Ord, T; Saarma, M; Villems, R, 1991
)
2.03
"Prochymosin is a monomeric protein containing three disulfide bridges."( Examination of calf prochymosin accumulation in Escherichia coli: disulphide linkages are a structural component of prochymosin-containing inclusion bodies.
Brasnett, AH; Marston, FA; Schoemaker, JM, 1985
)
1.09

Effects

ExcerptReferenceRelevance
"Pig chymosin has optimal general proteolytic activity around pH 3.5."( Demonstration of chymosin (EC 3.4.23.4) in the stomach of newborn pig.
Axelsen, NH; Foltmann, B; Lønblad, P, 1978
)
1.08

Bioavailability

ExcerptReferenceRelevance
"Although the bioavailability of large peptides with biological activity is of great interest, the intestinal transport has been described for peptides up to only nine residues."( The (193-209) 17-residues peptide of bovine β-casein is transported through Caco-2 monolayer.
Boutrou, R; Dupont, D; Gabai, G; Leonil, J; Mollé, D; Regazzo, D; Tomé, D, 2010
)
0.36
[information is derived through text-mining from research data collected from National Library of Medicine (NLM), extracted Dec-2023]

Occurs in Manufacturing (4 Items)

ItemProcessFrequency
Appetizerscore-ingredient1
Salty snackscore-ingredient1
Snackscore-ingredient1
Craquelincore-ingredient1

Research

Studies (971)

TimeframeStudies, This Drug (%)All Drugs %
pre-1990354 (36.46)18.7374
1990's152 (15.65)18.2507
2000's183 (18.85)29.6817
2010's231 (23.79)24.3611
2020's51 (5.25)2.80
[information is prepared from research data collected from National Library of Medicine (NLM), extracted Dec-2023]

Market Indicators

Research Demand Index: 65.78

According to the monthly volume, diversity, and competition of internet searches for this compound, as well the volume and growth of publications, there is estimated to be very strong demand-to-supply ratio for research on this compound.

MetricThis Compound (vs All)
Research Demand Index65.78 (24.57)
Research Supply Index6.93 (2.92)
Research Growth Index4.54 (4.65)
Search Engine Demand Index114.56 (26.88)
Search Engine Supply Index2.00 (0.95)

This Compound (65.78)

All Compounds (24.57)

Study Types

Publication TypeThis drug (%)All Drugs (%)
Trials6 (0.59%)5.53%
Reviews42 (4.13%)6.00%
Case Studies5 (0.49%)4.05%
Observational0 (0.00%)0.25%
Other965 (94.79%)84.16%
[information is prepared from research data collected from National Library of Medicine (NLM), extracted Dec-2023]