Curds casein

Whey concentration, both of whole whey and ultrafiltration permeate, is practiced successfully, but the solubility of lactose hmits the practical concentration of whey to about 20 percent total sohds, about a 4x concentration fac tor. (Membranes do not tolerate sohds forming on their surface.) Nanofiltration is used to soften water and clean up streams where complete removal of monovalent ions is either unnecessary or undesirable. Because of the ionic character of most NF membranes, they reject polyvalent ions much more readily than monovalent ions. NF is used to treat salt whey, the whey expressed after NaCl is added to curd. Nanofiltration permits the NaCl to permeate while retaining the other whey components, which may then be blended with ordinaiy whey. NF is also used to deacidify whey produced by the addition of HCl to milk in the production of casein. 

The condition of the curd on precipitation is important. As the milk starts to gel, agitators in the coagulation tanks are started as the temperature is raised to about 65°C. Under these conditions the protein is thrown out in fine particles. Too slow an agitation will produce large clots difficult to wash whilst too fine a curd also presents washing problems. In order to obtain the requisite consistency of the precipitate it may be necessary to add inorganic material to the skimmed milk. For example, the addition of phosphate ions will prevent undesirable flaky polymer. Similarly, calcium-deficient casein will not coagulate satisfactorily and the addition of calcium ions may be necessary. 

Kase-lab, n. rennet, -leim, m. casein glue, k sen, v.i. curd, curdle. 

Calcium caseinate is produced from skim milk by adding an acid to cause the protein to coagulate, at which point it can be filtered to separate the curds from the whey. 

Milk from cows contains 3.2% protein, about 80% of which is casein. Casein is isolated by a precipitation process from milk, involving heating, rinsing to remove whey, and drying to a powder. The yield is about 3 kg/ 100 kg skim milk. Rennet casein is obtained when the casein is precipitated by chymosin enzyme, also known as rennet, and acid casein is produced when precipitation is accomplished by acidification. Acid casein is usually found in the form of sodium caseinate or calcium caseinate, which are water-soluble salts. Caseinates are made by reacting NaOH or CaOH with a slurry of casein curd or powder and then spray drying (Southward, 2010). 

The most abundant milk protein is casein, of which there are several different kinds, usually designated a-, (1-, and K-casein. The different caseins relate to small differences in their amino acid sequences. Casein micelles in milk have diameters less than 300 nm. Disruption of the casein micelles occurs during the preparation of cheese. Lactic acid increases the acidity of the milk until the micelles crosslink and a curd develops. The liquid portion, known as whey, containing water, lactose and some protein, is removed. Addition of the enzyme rennet (chymosin) speeds up the process by hydrolysing a specific peptide bond in K-casein. This opens up the casein and encourages further cross-linking. 

Cathepsin D (EC3.4.23.5). It has been known for more than 20 years that milk also contains an acid proteinase, (optimum pH ss 4.0) which is now known to be cathepsin D, a lysozomal enzyme. It is relatively heat labile (inactivated by 70°C x 10 min). Its activity in milk has not been studied extensively and its significance is unknown. At least some of the indigenous acid proteinase is incorporated into cheese curd its specificity on asl- and / -caseins is quite similar to that of chymosin but it has very poor milk-clotting activity (McSweeney, Fox and Olson, 1995). It may contribute to proteolysis in cheese but its activity is probably normally overshadowed by chymosin, which is present at a much higher level. 

ADD ONE TEST TUBE FULL OF WHITE VINEGAR TO THE WARM SKIM MILK. THE CASEIN SEPARATES IN HEAVY, WHITE CURDS. 

Minerals found in milk which are insoluble remain in water in the curd and are more concentrated in the cheese than in milk. About two-thirds of the calcium and one-half of the phosphorus of milk remains in cheese. A major portion of the milk calcium is retained in the curd of cheese made with coagulating enzymes. Acid coagulation alone results in the loss of portions of both calcium and phosphorus salts in the acid whey, since these minerals are more soluble in the acidic medium. Most milk fat and fat-soluble vitamins are retained in the curd, but a considerable amount of water-soluble vitamins is lost during cheese manufacture. Retention of part of some B-complex vitamins in curd is due to their extended association with casein in the original milk. 

To increase curd elasticity and improve eye formation, the milk used to produce Swiss cheese must be clarified. Standardization of the fat content of the milk after clarification ensures uniform composition. Rennet and lactic acid from the bacteria cause casein coagulation. Swiss cheeses made in the United States are cured for three to four... 

With the increase in the production of cheese, not only in the United States but throughout the world (USDA 1981C), and more stringent controls on disposal of waste materials, the use of surplus cheese whey is one of the most critical problems facing the dairy industry. Whey, the liquid that remains after casein and fat are separated as curds in... 

The high casein content of cow s milk is responsible for the formation of a large, firm curd which may be difficult for some infants to digest compared with the finer, soft curd formed from human milk. Consequently, cow s milk often is modified to conform more closely to the nutrient and physical requirements of infants (Fomon 1974). When cow s milk is heated, homogenized, or acidified to produce softer curd formation, the protein is used by infants as efficiently as that of human milk, which contains less casein than cow s milk (Fomon 1974). 

O Keeffe et al. (1977) reported that some porcine pepsin survives Cheddar cheesemaking and contributes to casein breakdown during cheese curing. However, it has been shown that the breakdown they attributed to pepsin occurs in curd containing neither coagulant nor starter bacteria (Majeed 1984). More recent studies have shown that porcine pepsin does not survive in Cheddar cheese when the milk is set at pH 6.6 (Yiadom-Farkye 1986). This supports earlier reports of Green (1972) and Wang (1969). 

M. pusillus var. Lindt protease has given satisfactory results as a chymosin substitute in the manufacture of a number of cheese varieties, but not all varieties of M. pusillus var. Lindt are capable of producing acceptable cheese (Babel and Somkuti 1968). The clotting activity of M. pusillus var. Lindt protease is more sensitive to pH changes between 6.4 and 6.8 than chymosin, but is much less sensitive than that of porcine pepsin (Richardson et al 1967). The same authors reported that CaCL added to milk affected the clotting activity of M. pusillus var. Lindt rennet more than it did that of chymosin rennet. They also reported that this rennet was more stable than chymosin between pH 4.75 and 6.25. M. pusillus var. Lindt rennet is not destroyed during the manufacture of Cheddar cheese, although less than 2% of the enzyme added to the milk remains in the curd. Nearly all of it is found in the whey (Holmes et al. 1977). Mickelsen and Fish (1970) found M. pusillus var. Lindt rennet to be much less proteolytic than E. parasitica rennet but more proteolytic than chymosin rennet on whole casein, a8-casein and /3-casein at pH 6.65. 

Milk-clotting is a complex process, involving a primary enzymic phase in which K-casein is altered and loses its ability to stabilize the remainder of the caseinate complex, a secondary non-enzymic phase in which aggregation of the altered caseinate takes place, a third step where the aggregate of casein micelles forms a firm gel structure and a possibly separate fourth step where the curd structure tightens and syneresis occurs (McMahon and Brown 1984B). 

Lawrence and Sanderson proposed another micro-method for measuring chymosin and other proteolytic enzymes. Measurement of concentration was based on the rate of radial diffusion of the enzyme through a thin layer of caseinate-agar gel. The limit of diffusion was marked by a zone of precipitated casein (Emstrom and Wong 1974). Holmes et al (1977) developed a microdiffusion assay for residual proteolytic enzymes in curd and whey that is more sensitive than the method of Lawrence and Sanderson or the clotting-time assay of Reyes (1971). 

The casein micelles become surrounded by whey proteins and cannot interact with one another, thus reducing whey syneresis. This results in a soft curd that retains more moisture. The yield of cheese is increased due to the incorporation of whey proteins and the higher moisture content. Overheated milk requires longer rennet coagulation times. If milk is heated for 30 min at 75° C, it will not clot at all (Ustu-nol and Brown 1985). 

The effects of homogenization on milk components have been summarized by Walstra and Jenness (1984) and Harper (1976). Homogenization disrupts fat globules and results in an increase in fat surface area (about 4-10 times). Casein micelles adsorb on the fat surface and constitute part of the fat globule membrane. The curd tension of milk is thus lowered. Walstra and Jenness (1984) have described the effect of homogenization on rennet coagulation. 

The physical and chemical characteristics of cheese curd depend on the method used to form the curd matrix. The curd is formed in basically one of two ways acid or enzymatic coagulation. In acid curd cheeses (cottage, baker s, cream), the curd is formed by direct addition of acid to the milk or by lactic acid produced by the fermentation of lactose. As the pH of the milk approaches the isoelectric point of casein (pH... 

The other major casein in cheese is /3-casein, but it is generally not hydrolyzed by rennet in low-pH cheeses. Alkaline milk protease (plas-min) plays the major role in the hydrolysis of /3-casein (Richardson and Pearce 1981). The plasmin level in cheese is related to the pH of the curd at whey drainage, since plasmin dissociates from casein micelles as the pH is decreased. Richardson and Pearce (1981) found two or three times more plasmin activity in Swiss cheese than in Cheddar cheese. Swiss cheese curds are drained at pH 6.4 or higher, while Cheddar cheese curds are drained at pH 6.3 or lower. Proteolysis of /3-casein is significantly inhibited by 5% sodium chloride. The inhibitory influence of sodium chloride is most likely due to alteration of /3-casein or a reduction in the attractive forces between enzyme and substrate (Fox and Walley 1971). 

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