Part:BBa_K2924028
β-casein
The milk protein β-casein from Bos taurus
Usage and Biology
β-casein (CSN2), also named CASB_BOVIN1is a gene coding for a protein product, has the GeneID: 281099, which originates from <Bos taurus>2.
Caseins are among the most abundant proteins in native cow's milk. They are phosphoproteins and make up approximately 80% of total dairy protein mass. The milk proteins and their proportions are important to the parameters of milk manufacturing and the quality of milk protein. In general casein is anti-catabolic, reduces muscle breakdown and contains high amounts of calcium. Casein has a number of bioactive peptides that can benefit an individual digestive system and immune system. The said peptides can also help the body combat heart disease and heart problems by regulating inflammation and increasing blood clot forming. This is because the above-mentioned peptides have comparable medicinal effects to that of ACE inhibitors or angiotensin-converting enzyme that can help the body manage and control high blood pressure. Bovine β-casein is usually present as a single form with five phosphates. The calcium-insoluble protein also has a highly charged N-terminal region and a hydrophobic C-terminal region3,4. Just like ɑ-s1-casein, it does not have any cysteine residues4.
The DNA sequence of the gene was acquired by reverse-translating the amino acid sequence. Further, in order to reach optimal heterologous expression in Escherichia coli the DNA sequence was designed with optimized codons and synthesized commercially.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21INCOMPATIBLE WITH RFC[21]Illegal BamHI site found at 673
- 23COMPATIBLE WITH RFC[23]
- 25INCOMPATIBLE WITH RFC[25]Illegal AgeI site found at 630
- 1000COMPATIBLE WITH RFC[1000]
References
[1]: https://www.uniprot.org/uniprot/P02666
[2:] https://www.ncbi.nlm.nih.gov/gene/?term=P02666
[3]: Kumosinski, Thomas F., and Harold M. Farrell. "Calcium-induced associations of the caseins: thermodynamic linkage of calcium binding to colloidal stability of casein micelles." Journal of protein chemistry 10.1 (1991): 3-16.
[4]: Fang, Yuan, and Douglas G. Dalgleish. "DEPARTMENT OF FOOD SCIENCE, UNIVERSITY OF GUELPH, GUELPH, ONTARIO NIG 2W1, CANADA." Food Macromolecules and Colloids 156 (1995): 146
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