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Milk caseins

Protein-Based Substitutes. Several plant and animal-based proteins have been used in processed meat products to increase yields, reduce reformulation costs, enhance specific functional properties, and decrease fat content. Examples of these protein additives are wheat flour, wheat gluten, soy flour, soy protein concentrate, soy protein isolate, textured soy protein, cottonseed flour, oat flour, com germ meal, nonfat dry milk, caseinates, whey proteins, surimi, blood plasma, and egg proteins. Most of these protein ingredients can be included in cooked sausages with a maximum level allowed up to 3.5% of the formulation, except soy protein isolate and caseinates are restricted to 2% (44). [Pg.34]

The enzymatic hydrolysates of milk casein and soy protein sometimes have a strong bitter taste. The bitter taste is frequently developed by pepsin [9001 -75-6] chymotrypsin [9004-07-3] and some neutral proteases and accounted for by the existence of peptides that have a hydrophobic amino acid in the carboxyhc terminal (226). The relation between bitter taste and amino acid constitution has been discussed (227). [Pg.296]

Since the discovery of the enkephalins in 1975 [11] a large number of endogenous opioid peptides have been detected in mammals, and at present three distinct families of opioid peptides are known (for a review, See Ref. 12). These are the enkephalins, the endorphins (a-, (J-, and y-), and the dynorphins and neoendorphins. The recently discovered endomor-phins [13] also may represent endogenous opioid peptides. Peptides with opioid activity have also been isolated from tryptic digests of milk casein... [Pg.155]

In this attempt, W. Krische coated paper with milk casein in 1897 but found that casein gets washed off with water. It was soon discovered that casein could be hardened and made waterproof by treatment with formaldehyde. [Pg.39]

Cyclo(Leu-Trp), a bitter compound isolated from the fermentation of milk casein by Bacillus subtilis, opened up the field to flavor and fragrance properties. It was further noted that dipeptides became more bitter when blockage of both the amino and carboxyl groups occurred or the dipeptide was converted into a DKP. This phenomenon opened the field of taste exhibition. ... [Pg.683]

Cheeseman, G. C. 1968. A preliminary study by gel filtration and ultracentrifugation of the interaction of bovine milk caseins with detergents. J. Dairy Res. 35, 439-446. [Pg.152]

Josephson, R. V. 1972. Isoelectric focusing of bovine milk caseins. J. Dairy Sci. 55, 1535-1543. [Pg.159]

Nagasawa, T., Kiyosawa, I., Kuwahara, K. and Ganguly, N. C. 1973. Fractionation of buffalo milk casein by acrylamide gel electrophoresis and DEAE cellulose column chromatography. J. Dairy Sci. 56, 61-65. [Pg.162]

McMahon, D. J., Brown, R. J. and Emstrom, C. A. 1984A. Enzymic coagulation of milk casein micelles. J. Dairy Sci. 67, 745-748. [Pg.630]

Philippos, S. G. and Christ, W. 1977. Studies on some microbial milk-clotting enzymes for cheesemaking and their effect on cow s milk casein. II. Differentiation of the milk-clotting enzyme. Milchwissenschaft 32, 67-71. [Pg.631]

Minamiura, N., Matsumera, Y., Fukumoro, J. and Yamamoto, T. 1972. Bitter peptides in cow milk casein digests with amino acid sequence of a bitter peptide. Agr. Biol Chem. 36, 588-595. [Pg.731]

Bioactive peptides Enzymatic hydrolysate Milk, casein... [Pg.116]

The BMEA procedure was also used to produce high-purity bovine milk casein (Bazinet et al., 1999a) and soybean isolates (Bazinet et al., 1997 1999b) or to fractionate soybean 1 IS and 7S fractions (Bazinet et al., 2000b). [Pg.316]

Bazinet, L., Lamarche, F., Ippersiel, D., and Amiot, J. 1999a. Bipolar membrane electro-acidification to produce bovine milk casein isolate. J. Agric. Food Chem. 47, 5291-5296. [Pg.352]

Part of the process to make cheese involves the flocculation of an electrostatically stabilized colloidal O/W emulsion of oil droplets coated with milk casein. The flocculation is caused by the addition of a salt, leading to the formation of networks which eventually gel. The other part of the process involves reaction with an enzyme (such as rennet), an acid (such as lactic acid), and possibly heat, pressure and microorganisms, to help with the ripening [811]. The final aggregates (curd) trap much of the fat and some of the water and lactose. The remaining liquid is the whey, much of which readily separates out from the curd. Adding heat to the curd (-38 °C) helps to further separate out the whey and convert the curd from a suspension to an elastic solid. There are about 20 different basic kinds of cheese, with nearly 1000 types and regional names. Potter provides some classification [811]. [Pg.307]

HPLC-ESI-MS + XIC Cow, sheep, goat, and buffalo milk Caseins (42)... [Pg.210]

Umetsu, H., Matsuoka, H., and Ichishima, E. (1983). Debittering mechanism of bitter peptides from milk casein by wheat arboxypeptidase. J. Agric. Food Chem., 31, 50-53. [Pg.267]

Another beverage containing antihypertensive dodecapeptide was recently developed in Japan (Sugai, 1998). The peptide was obtained from tryptic hydrolysates of milk casein and the antihypertensive effect was studied in animals and humans. Those studies suggested the usefulness of the peptide as an ingredient of physiologically functional foods to prevent hypertension. Furthermore, the preventive effect of the peptide against cardiovascular diseases was shown stroke-prone SHR. The product, Casein DP , was approved by the Ministry of Health and Welfare as a FOSHU. [Pg.247]

Karaki, H., Doi, K., Sugano, S., Uchiwa, H., Sugai, R., Murakami, U., and Takemoto, S. 1990. Antihypertensive effect of tryptic hydrolysate of milk casein in spontaneously hypertensive rats. [Pg.258]

Neeser, J.R., Golliard, M., Woltz, A., Rouvet, M., Dillmann, M.L., and Guggenheim, B. 1994. In vitro modulation of oral bacterial adhesion to saliva-coated hydroxyapatite beads by milk casein derivatives. Oral Microbiol. Immunol. 9, 193-201. [Pg.265]

Otani, H. and Hata, I. 1995. Inhibition of proliferative responses of mouse spleen lymphocytes and rabbit Peyer s patch cells by bovine milk caseins and their digests. J. Dairy Res. 62, 339-348. [Pg.265]

As it can be seen in Table 13.2, human milk composition is quite different from that of cow s milk. Casein and mineral contents are lower in human milk than in cow s milk, whilst the lactose content is higher in the former. With regards to fatty matter, both types of milk present similar contents, but the total protein is over three-fold higher in cow s milk. [Pg.402]

ELEMENTAL DISTRIBUTIONS IN THE DIFFERENT FRACTIONS OF MILK CASEINS, FAT, AND MILK WHEY... [Pg.426]

These regenerated proteins are obtained from milk (casein), soya beans, corn, and peanuts. More or less complex chemical separation and purification processes are required to isolate them from the parent materials. They may be dissolved in aqueous solutions of caustic, and wet-spun to form fibers, which usually require further chemical... [Pg.454]

Bitterness occurs as a defect in dairy products as a result of casein proteolysis by enzymes that produce bitter peptides. Bitter peptides are produced in cheese because of an undesirable pattern of hydrolysis of milk casein (Habibi-Najafi and Lee 1996). According to Ney (1979), bitterness in amino acids and peptides is related to hydrophobic-ity. Each amino acid has a hydrophobicity value (Af), which is defined as the free energy of transfer of the side chains and is based on solubility properties (Table 7-6). The average hydrophobicity of a peptide, Q, is obtained as the sum of the Af of component amino acids divided by the number of amino acid residues. Ney (1979) reported that bitterness is found only in peptides with molecular weights... [Pg.187]


See other pages where Milk caseins is mentioned: [Pg.176]    [Pg.243]    [Pg.155]    [Pg.174]    [Pg.350]    [Pg.169]    [Pg.200]    [Pg.65]    [Pg.203]    [Pg.325]    [Pg.389]    [Pg.427]    [Pg.454]    [Pg.215]    [Pg.176]    [Pg.209]    [Pg.209]    [Pg.11]    [Pg.9]    [Pg.204]    [Pg.34]    [Pg.43]    [Pg.43]    [Pg.401]   
See also in sourсe #XX -- [ Pg.307 ]

See also in sourсe #XX -- [ Pg.129 ]

See also in sourсe #XX -- [ Pg.234 ]




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Caseins in milk

Homogenized milks, casein micelles

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Isolation of casein from milk

K-Caseins in milk

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