Protein concentrates available

Milk and egg products are highly desired in pet foods since they supply the highest quaHty amino acid profiles with nearly 100% digestibiHty. Most milk protein concentrates are used for human foods, but some are available to pets (see Milk and milk products). An enormous quantity of whole eggs (qv) derived from egg graders, egg breakers, and hatchery operations are handled as dehydrated, Hquid, or frozen ingredients. 

The mmen is not functional at birth and milk is shunted to the abomasum. One to two weeks after birth, the neonate consumes soHd food if offered. A calf or lamb that is nursing tends to nibble the mother s feed. An alternative method of raising the neonate is to remove it from its mother at a very young age, <1 week. A common example of an early weaning situation is the dairy calf that is removed from the cow soon after birth so that the cow s milk supply might be devoted entirely to production. In this instance, the neonate requires complete dietary supplementation with milk replacer. Sources of milk replacer protein have traditionally included milk protein but may also include soybean proteins, fish protein concentrates, field bean proteins, pea protein concentrates, and yeast protein (4). Information on the digestibiUty of some of these protein sources is available (4). 

The nutrient sparing effect of antibiotics may result from reduction or elimination of bacteria competing for consumed and available nutrients. It is also recognized that certain bacteria synthesize vitamins (qv), amino acids (qv), or proteins that may be utilized by the host animal. Support of this mode of action is found in the observed nutritional interactions with subtherapeutic use of antibiotics in animal feeds. Protein concentration and digestibiHty, and amino acid composition of consumed proteins may all influence the magnitude of response to feeding antibiotics. Positive effects appear to be largest... 

Eleven controlled diet and environment experiments have been designed in a way that can be used to investigate the effects of protein nutrition and heat and/or water stress on diet-tissue A N. Laboratory rats were raised on purified, pelletized diets in which the isotopic composition of proteins, lipids and carbohydrates were well characterized and their proportions accurately and precisely measured (Ambrose and Norr 1993). Four experiments involved manipulation of temperature and/or water availability. Of these four experiments, one used a diet with high (70%) protein concentrations and heat/water stress (36°C) and three used normal (20%) protein concentrations. Seven experiments were conducted at normal temperature (21°C) with water ad libitum. Of these seven experiments, two used diets formulated with veiy low protein (5%), three with normal protein and two with high protein concentrations. 

Another way in which to gain structural information concerning the N-terminal residue of glycophorins A" and A is to study the N-terminal, mono[ C]methyl derivatives these are produced by using limited amounts of [ C]formaldehyde. There are distinct differences between the N, N -di[ C]methylamino and N -mono[ C]methylamino species (i) a significant, chemical-shift difference exists between the N-terminal dimethyl and monomethyl species (43 and 34 p.p.m.) (li) all of the C resonances of the N-terminal dimethyl species move upheld as the pH is increased (if they move at all), whereas all of the C resonances of the N-terminal, monomethyl species move downfield as the pH is increased and (in) A for the N-terminal monomethyl species tends to be much larger than that for the N-terminal dimethyl species. Point (in) would tend to indicate that it may be more advantageous to study the N-terminal monomethyl species. However, because of allowable protein concentrations, detection limits on available instruments, and technical difficulties, it has thus far... 

The first four materials (IRMM/IFCC-452, 453, 454, 455) are expected to be released during 2000. Projects on the certification of reference materials for cardiac marker (myoglobin) and total protein concentration in serum are under discussion. Even so the number of available CRMs for clinical chemistry and occupational toxicology is still limited. This has to do with the complexity of physiological compounds (e.g. proteins), the instabihty (e.g. enzymes), or the volatility (e.g. solvents). 

The fascinating experience with 1000-year-old mortar, in which the protein concentration was extremely low, has shown that by using this method it is possible to work in fields where other methods fail. In the case of easel paintings, small samples are usually available the advantage of the method described here also lies in the true microdestructive character. Moreover, as most samples, mainly in the case of paintings, often contain more than one proteinaceous binder (see e.g. E. Munch Portrait of Friedrich Nietzsche , Section 6.4.3), it is very encouraging that the PMM allows the simultaneous determination of at least two of them. 

Soya Proteins. Early attempts to make albumen substitutes from soya protein also ran into problems. A bean flavour tended to appear in the finished product. A solution to these problems has been found. Whipping agents based on enzyme modified soy proteins are now available. The advantage of enzymatic modification is that by appropriate choice of enzymes the protein can be modified in a very controlled way. Chemical treatment would be far less specific. In making these materials the manufacturer has control of the substrate and the enzyme, allowing the final product to be almost made to order. The substrates used are oil-free soy flakes or flour or soy protein concentrate or isolate. The enzymes to use are chosen from a combination of pepsin, papain, ficin, trypsin or bacterial proteases. The substrate will be treated with one or more enzymes under carefully controlled conditions. The finished product is then spray dried. 

The major component of whey is lactose, and while there various uses for the protein in making protein concentrates these leave a surplus of lactose. Impure grades of lactose have been available to the food industry for some time. They are relatively successful in biscuits as a raw material for the Maillard reaction to produce pleasant colours and flavours. 

Advances in soy protein processing technology have allowed extensive diversification of protein product applications. More sophisticated soy protein products now manufactured have more functionality, better performance, more consistency and better flavor than commercially available defatted soy flour and grits (50% protein dry basis). Among these products are improved textured soy flours, concentrates, and isolates (50%, 70% and 90% protein dry basis, respectfully), functional and non-functional soy protein concentrates (70% protein dry basis) and highly soluble, highly functional isolated soy proteins (90% protein dry basis) (6-8 14-18). 

Soy Protein Concentrates. Both non-functional (low or no solubility) and functional (good solubility, emulsification capacity, and dispersibility) soy protein concentrates (70% protein, dry basis) are commercially available for use in meat products (2-4, 6, j), 15) Normally, a highly functional product with no harsh or bitter flavors is desirable. When used to replace lean meat, non-hydrated concentrate can be used at levels up to 6-7% in finished nonspecific emulsion meats Higher replacement levels or formulas with specific cost/nutrition requirements may use soy protein concentrate with a judicious amount of textured soy protein (6). Excellent yields, cost savings, texture, flavor and nutrient profiles are possible. However, most soy protein concentrates lack sufficient solubility or sufficiently low viscosities to be used in brines for absorption or injection into whole muscle tissue. When legal standards for protein content exist (13), more concentrate must be used to achieve legal minimums. Brine viscosities increase and uniform distribution of brine components throughout the specific whole muscle piece is restricted. Finished product appearance and flavor are easily compromised. Thus, use of soy protein concentrates in whole muscle applications is limited. 

The first assay to be employed for protein concentration is the Bradford assay, a commercially available colorimetric assay used to quantitate the total extracted protein. Amb a 1 is approximately 1% of the total protein extracted from ragweed pollen hence the Bradford assay does not reflect Amb a 1 concentration. However, at this step of the production process, the protein concentration is used to calculate final yields and not to make time-dependent or expensive decisions. Hence the nonspecific Bradford assay is ideal. A simpler direct absorbance method is not suitable due to the presence of a nonprotein chromophore in the ragweed extract. 

In severe malnutrition where circulating protein concentrations are very low, in uraemia and in pregnancy, the distribution of the drug (e.g., anticonvulsants) between bound and free forms may alter, and when monitoring treatment it may be necessary to get the laboratory to measure free concentrations of the drug. However this can only be done in specialised centres, even in developed countries, and is not usually available elsewhere. 

Milk protein products. As indicated in Table 1, the food industry is placing major emphasis on the production and utilization of milk protein products in a wide variety of formulated food products (20,21,22). Although nonfat dry milk (NFDM) and whey powder are major milk protein ingredients in formulated foods, casein and whey protein concentrates, which contain their proteins in a more highly concentrated and functional form, are essential for certain food product applications, such as those products that require the proteins as an emulsifier agent. Additional details on the processing methods and conditions used to produce the various milk protein products are available (23). 

Whey protein concentrates (WPC) are produced by a variety of processing treatments to remove both lactose and minerals (20) as indicated in Figure 5. Even though it would be highly desireable to remove most of the lactose and minerals in these processes, it is not practical from an economic standpoint and thus most of these products only range in protein content from 35 to 50 %.The major objective of most of these processes is to produce a WPC with minimal protein denaturation in order to obtain a product with maximum protein solubility and functionality. However, from a practical consideration this objective is not readily obtainable, and thus most WPC products commercially available exhibit variable whey protein denaturation and functionality (20). 

Whey protein concentrates (WPC), which are relatively new forms of milk protein products available for emulsification uses, have also been studied (4,28,29). WPC products prepared by gel filtration, ultrafiltration, metaphosphate precipitation and carboxymethyl cellulose precipitation all exhibited inferior emulsification properties compared to caseinate, both in model systems and in a simulated whipped topping formulation (2. However, additional work is proceeding on this topic and it is expected that WPC will be found to be capable of providing reasonable functionality in the emulsification area, especially if proper processing conditions are followed to minimize protein denaturation during their production. Such adverse effects on the functionality of WPC are undoubtedly due to their Irreversible interaction during heating processes which impair their ability to dissociate and unfold at the emulsion interface in order to function as an emulsifier (22). 

---