Protein Casein Food

Protein casein paint Food repute -Protein CaseinIntroductionProteins argon considered as the third class of macro components of each(prenominal) living systems, and alike that of the regimen stuffs .Proteins are polymers with highly complex expressions and their molecular weight ranges from 10,000 to several million. The structure of protein is quite unprejudiced they are made up of monomeric units called as Amino acids. These aminic acids are mostly linked by a single peptide bond.The range of amino group acids is highly limited in summate and mostly ordinary to all proteins. Mostly all proteins are mixtures of 20 standard amino acids. The polypeptide bonds of proteins are never branched. The singularity of protein lies in the diversity of variation in its structure and function. All proteins have their own sequence of amino acids of defined length. All amino acids that occur in protein have a general formulaRH2NC HCOOHProteins are broadly made up of one of the four stru cture .They may be primary, alternate, tertiary or foursome structure.Primary structureThey are the sequence of a chain of amino acids.Secondary protein structureWhen the sequence of a chain of amino acids is linked by an amino acid. E.g. either alpha helix or pleated sheet.Tertiary protein structure Three dimensional structure of a protein mote formed by the spatial arrangement of the secondary structures like alpha helix and pleated sheet.Source http//cropandsoil.oregonstate.edu/classes/css430/ yap away%209-07/figure-09-03.JPGQuaternary protein structureIf a protein has more than one amino acid chain then its called quaternary protein structure.Milk proteins ( casein paint)Milk of cow is the important source of protein for man and most importantly for children. Milk is a mixture of aqueous solution of proteins, lactose, minerals and certain vitamins which carry emulsified copious globules and casein micelles which have protein along with phosphate, citrate, and calcium. The fa t removed milk is called glide milk. If the pH of the skim milk is reduced to 4.6 at 20C, the casein is precipitated and the counterpoise is called whey or serum. The proportion of antithetic casein in milk varies and so does the whey. The content of casein vary in different types of milk like in cows milk it accounts for 80% where as in human milk its just 40%.The various proportion of casein in skimmed milk is shown in the below tableCasein proteins (80%)Skimmed milk protein%-Casein40-Casein24-Casein12-Casein4Source Coultate,T.P.1989.Food-The Chemistry of its Components.2nd ed.London The Royal society of Chemistry The Greek letters that are use in casein proteins are used on basis of the protein mobility in electrophoresis. Thes in s-casein refers to its predisposition to over-confidence by the calcium ion. Where as , , , and define particular protein species, it has been discovered that there are a lot of different versions of each that only differ slightly in their ami no acid sequences. For example, s1C casein is different from that of s1B casein by having glycine residue instead of glutamic acid residue at position 192 in the polypeptide chain. With these advancements one fag end even identify the breed of cow from which the sample milk was obtained by examining the proportions of these variants. heterogeneousness of caseinsHeterogeneity is seen in caseins. For example, in bovine casein there are four major types of casein .They are s1, s2, and -casein. Each of these at least exhibit micro heterogeneity in one of the below reason outsVariation in the degree of phosphorylation.Variation in the degree of glycosylation in -casein alone.Genetically controlled substitution in the amino acids, which results in the genetic polymorphism.Proteolysis of the indigenous proteinases.Molecular properties of caseinCasein are well characterized proteins and and then they are quite small proteins, with a molecular mass say around 20-25kDa .Which is the m ain reason for their high stability. For example -casein has high level of proline say like 35 out of the 209 amino acids are proline which is equally distri plainlyed. Due to the presence of high level of proline the alpha helix, beta-sheets and beta-turns are absent.Casein are generally hydrophobic .Apart from this it is alike said that caseins have very low secondary and tertiary structures .As they lack secondary structures its been told that they are very flexible and unstable which makes it rheomorphic(they are so flexible in solution that they can adopt any structure dictated by the environment).The lack of stable secondary and tertiary structures also make them stable against denaturing agents like heat and urea. This latter situation also confers good foaming and emulsifying property on casein. This also makes casein quick susceptible to proteolysis. These properties of casein make them unique in dietetic applications like in that of cheese ripening etc.Properties of t he principal caseins in cows milkproteinmolecular massAmino acidsproline residuescysteine residues PO4 groupconcentration(g/L)glycoproteingenetic variants s1 -casein23164199170810noA, B, C, D, E, F, G, H s2-Casein25388207102102.6noA, B, C, D-casein2398320935059.3noA1, A2, A3, B, C, D, E, F, G-casein19038169202110.3yesA, B, C, E, FS, FI, GS, GSTable2 Properties of caseins present in cows Milk.SourceYada, Rickey Yoshio,1954-, Proteins in food touch on ,pg29-62,Knovel firmRole of casein in dairy productsIn western countries, Dairy products account for some 30% of the daily dietary energy, lipids and protein. And even some of the vitamins are also got from dairy products like vitamin G and vitamin B12.Minerals also come into this list, followed by calcium it is also estimated that 80% of calcium is obtained from dairy products.Some of the functions of caseins in dairy products are given belowPasteurized liquid milk Appearance, heat stability, mouth sense of smell and flavor.fermented milksGel formation, mouth feel, flavor, syneresis of the gel and rheologyCreamsEmulsion stability, rheology (body) and whippability.ice creamsEmulsion stability, rheology (body) and whippabilityMilk powderswettability , dispersibility,solubility,flavor,color and other uses which attend upon the end use of the productCheesetexture, body and other rheological properties operative propertiessuch as meltability, stretchability, sliceability, adhesiveness, water-bindingProperties (off-) flavors.Coultate, T.P. Food-the Chemistry of Its Components. second ed. london The Royal society of Chemistry 1989The precipitation of casein is the basic answer involved in cheese making .In case of yogurt and some cottage cheese the precipitation is brought up by low pH.Functional food properties of casein (dairy products)Functional food is nothing except if a food ingredient or food provides some kind of health benefit which doesnt intromit the traditional nutrient it contains then it can be calle d as a functional food. Some of the park functional food characteristics of dairy products are Anti-microbial including control of gut micro flora, Anti-viral, Binding of E coli and epidemic cholera enter toxins, Anti-cancer, Immunomodulation, Anti-oxidative, Opioid effectsRetard osteoporosis. The bioactive peptides of casein are responsible for most of these functional properties like Casein glycomacropeptide which is responsible in Cancer Prevention, Immunomodulation, Diet Suppression, and Cardiovascular Effects (cholesterol reduction).Fractionation of caseinIts possible to separate whole casein into its component proteins from 1940 but it is limited to laboratory .It is done by exploiting the difference in solubility in the solution of urea pH4.6 or cacl2 .Its is also done by various chromatography methods but unfortunately none of these methods are suitable for industrial scale production of individual casein.But there is a huge scope or opportunity for this becauseThe Beta casein has high surface activeness hence they can be used has good emulsifying or good foaming agents.Human milk contains beta casein and k-casein .Alpha casein is almost absent in human milk hence the beta casein will be an attractive ingredient of bovine milk based infant formulae.As k-casein is responsible for the stability of the casein micelle it can be used in some of the milk products. up-to-the-minute discoveries have revealed that fortification of milk with Beta-casein improves cheese making properties.One of the successful methods of separation of beta casein is from skimmed milk by using rennet.sourcehttp//classes.ansci.uiuc.edu/ansc438/Milkcompsynth/milkcomp_protein.htmlsourcehttp//classes.ansci.uiuc.edu/ansc438/Milkcompsynth/milkcomp_protein.htmlThe Casein micelleThe Casein in milk exist as colloidal particles of 50-500nm, which are called as casein micelles. The casein micelles of milk are nearly spherical particles. Milk has about 1015 micelles dm-3.A casein micell e contain approximately about 2104 casein molecules. Of all structure models slattery and evards model comes near to accounting all the observed properties of casein. According to them micelle is an aggregate of sub micelles each consisting of 25-30 molecules of all types of casein in roughly similar proportions to those in milk as a whole.Figure A casein micelle A a submicelle B protruding chain C Calcium phosphate D -casein E phosphate groupsSource www.food-info.net/uk/protein/milk.htmCasein micelles are stable to-Compaction-Pellet that was recovered from ultracentrifugation can be readily redispersed.-Homogenization at normal or high pressure-Also to high Ca2+ concentrations, up to 200mM, at temperatures upto 50CHowever number things can destabilize, redisperse or affect the casein micelle hence they are usually destabilsed in certain food products like cheese etc.ConclusionAs its clear that casein has a great probable as a functional food more research should be carried out in this field. more(prenominal) studies should be undertaken in bioactive peptides of casein which are released by the enzymatic hydrolysis which have a huge employment in cancer prevention, cardiovascular disease prevention etc.As they are good emulsifying and foaming agents they can be extensively used in food industry.ReferenceMilk Proteins. Wageningen University, http//www.food-info.net/uk/protein/milk.htmhttp//209.85.141.104/search?q=cacheuIjin-nhDmIJwww.uft-plovdiv.bg/bg/Functional%2520Dairy%2520Foods.doc+functional+food+and+caseinhl=enct=clnkcd=17gl=auclient=firefox-a.Coultate, T.P. Food-the Chemistry of Its Components. second ed. london The Royal society of Chemistry 1989Harper, W. James. Functional Aspects of Dairy Foods , 2003.Yada, Rickey Yoshio. Proteins in Food Processing. Place Published, 1954.Hurley, Walter L. Milk Composition Proteins. http//classes.ansci.uiuc.edu/ansc438/Milkcompsynth/milkcomp_protein.html.7. Cropandsoil.oregonstate.edu/classes/css430/lecture%209-07 /figure-09- 03.JPG