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Proteins, meat

Bone Cleaning. As an alternative to rendering, an en2ymatic process can be used to upgrade fresh bones to valuable products, eg, cleaned bone suitable for gelatin production and a meat protein hydrolysate for the food industry. This process is performed as a two-step en2yme process, ie, scrap meat recovery and bone cleaning. [Pg.302]

The carbon dioxide removed in synthesis gas preparation can be reacted with ammonia, to lonn urea CO(NH2)2- This is an excellent fertilizer, highly concentrated in nitrogen (46.6%) and also useful as an additive in animal feed to provide the nitrogen for formation of meat protein. Urea is also an important source of resins and plastics by reacting it with formaldehyde from methanol. [Pg.265]

The first slaughterhouse in Denmark for organic meat was set up in 1994, for an organic pig farm nearby. It now produces organic cold meats and sausages. It advertises its products by informing the consumers that their products are made without additives, that all the meat is hand-cut, and that no mechanically recovered meat, blood plasma and extra meat proteins are ever used. [Pg.138]

Feeding human subjects meat-rich diets has been clearly and repeatedly associated with elevated urinary acid and calcium loss. Anand, et al. (12) fed college men low, medium, and high-protein diets. Fecal calcium changed less than 15%, whereas urinary calcium losses accounted for the major loss of calcium. Calcium loss and meat protein intake correlated directly. Johnson, et al. (34) reported that women showed a similar response when fed such diets. [Pg.87]

USDA regulations also allow use of non-meat proteins in products such as pumped ham and corned beef, provided the finished product contains a minimum protein content of 17%. Pumping to achieve a cooked yield of 130% is permitted (32). [Pg.47]

Some of the uses of soy proteins to augment meat proteins are summarized in Table III. Textured soy flour, though not included in that table, can be used in the same meat systems, where soy grit or coarse soy protein concentrate are used. Besides the economics associated with the use of soy protein, they are utilized in such meat products because of their functional and nutritional properties. [Pg.82]

The non-meat protein product (e.g. isolated soy protein) must contain a prescribed vitamin/mineral pre-mix. [Pg.100]

The non-meat protein product must have biological quality of protein (including amino acids added) of not less than P.E.R. 2.0 (80% of casein) or an essential amino acid content (excluding tryptophan) of no less than 28% of total protein. [Pg.100]

Meat proteins comprise a water-soluble fraction (containing the muscle pigment myoglobin and enzymes), a salt-soluble fraction composed mainly of contractile proteins, and an insoluble fraction comprising connective tissue proteins and membrane proteins. As reviewed by Dierckx and Huyghebaert [107], HPLC analysis of meat proteins has been successfully applied to evaluate heat-induced changes in the protein prohle, to detect adulterations (addition of protein of lower value, the replacement of meat from high-value species with meat from lower-value species, etc.), and for specie identification in noncooked products (also for fish sample). [Pg.580]

Encourage the patient with folic acid deficiency to eat foods high in folic acid, including dried beans, meat proteins, and green leafy vegetables... [Pg.682]

The formation of free radicals after lipid oxidation is known to play a key role in the deterioration of meat flavor 8, 23), Since proteins constitute a major portion of the muscle s composition, the relationship between chemically active radical species and decomposition of food flavor proteins and peptides needs to be studied in detail. Data has been presented showing the correlation of proteins with flavor (Figures 5 and 6). Data is now presented showing how soluble meat proteins change in an environment where free radicals are induced by a free-radical oxidation generating system or FROG (Figure 10). [Pg.88]

Lee et al. (1978) investigated the possibility that sulfhydryl groups were required in the formation of the clostridial inhibitor in cured meats. Sulfhydryl groups of meat proteins were blocked by treatment with silver lactate, then the samples were cooked with sodium nitrite before inoculation with C. botuli num spores. Botulinal growth as measured by gas and toxin production was similar to controls without silver lactate treatment. They thus concluded that sulfhydryl groups were not required for the antibotulinal effects of nitrite in cured meats. [Pg.272]

Other Protein Components. Other protein components In complex food systems and In protein Ingredient preparations may Interfere with or modify gelation reactions. Protein Interaction between whey protein and casein upon heating has a profound Influence on the characteristics of the casein gel structure In cheesemaking. Similarly protein Interactions are Important to meat structures. Protein-protein Interaction between soy and meat proteins has also been demonstrated with heat treatment (28). While concrete Interaction data have not been collected on protein gels formed from protein combinations, gelation properties of whey proteln/peanut flour blends have been Investigated GU) ... [Pg.138]

Smith, D.M. Meat Proteins. Food Tkchy., 116 (March 1988). [Pg.1378]

RB Ashworth. Amino acid analysis for meat protein evaluation. J Assoc Off Anal Chem 70 80-85, 1987. [Pg.89]

Adulterants are any material deliberately added to the food material usually to reduce cost. Typical examples are incorporation of cheaper meats into more expensive ones or substituting non-meat proteins for meat. Additives, on the other hand, are added to impart improved flavor and/or texture characteristics to foods. However, either case creates problems for some of the consumers on health, economic and/or religious grounds. Therefore, it became imperative to... [Pg.362]

It thus seemed that the origin of the various components in meat volatiles could best be established by analyzing irradiation-induced compounds in meat protein and meat fat separately. Accordingly, a 500-gram sample of meat, the same size of sample normally used in irradiation studies of whole meat, was separated into a protein, a lipid, and a lipoprotein fraction by means of a methanol-chloroform extraction of the fat. The dry, air-free, fractions were then irradiated separately with 6 megarads of gamma radiation in the manner used for whole meat. The analytical results (Table V) show clearly that mainly sulfur compounds and aromatic hydrocarbons are formed in the protein fraction, whereas mainly aliphatic hydrocarbons are formed from the lipid. The lipoprotein fraction produced, as expected, both aliphatic hydrocarbons and sulfur compounds. Only the lipoprotein fraction had a characteristic irradiation odor. [Pg.38]

The study of radiochemical yields in such analytically difficult and variable systems as meat proteins is a complex problem. Fortunately, however, both chemical (4,12,23,46,49) and electron spin reasonance studies (6,16, 22-25, 42) by several workers have shown that the major radiochemical reactions in proteins closely parallel those of simple peptides and amino acids, justifying the use of these simpler systems for preliminary radiochemical investigations. [Pg.44]

This is the fundamental deformation band. It overlaps the protein amide I band. This band can be used to monitor changes in water content in a variety of materials including meats, protein isolates, and starch. [Pg.262]

Ayuso, R., Lehrer, S.B., Tanaka, L., Ibanez, M.D., Pascual, C., Burks, A.W., Sussman, G.L., Goldberg, B., Lopez, M., Reese, G. 1999a. IgE antibody response to vertebrate meat proteins including tropomyosin. Annals of Allergy Asthma Immunology 83(5) 399 105. [Pg.251]


See other pages where Proteins, meat is mentioned: [Pg.463]    [Pg.31]    [Pg.32]    [Pg.337]    [Pg.299]    [Pg.301]    [Pg.307]    [Pg.98]    [Pg.748]    [Pg.428]    [Pg.89]    [Pg.276]    [Pg.731]    [Pg.258]    [Pg.33]    [Pg.221]    [Pg.915]    [Pg.148]    [Pg.150]    [Pg.299]    [Pg.301]    [Pg.365]    [Pg.39]    [Pg.740]    [Pg.766]    [Pg.3]   


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