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The soya protein industry has produced a wide variety of products with specific functionality properties to meet the targeted needs required by the food industry. It is important to recognize that certain of these soya protein products have and perform specific functions in these foods, such as texture forming, gelation, fat and water binding, and emulsification. They contribute to the nutritional and general overall eating quality. Also important is to recognize the limits of application of soya protein technology based on maintaining the traditional quality of the meat, poultry or seafood products. Today, unlike just a few years ago, soya protein products are able to contribute to, not just extend, high-quality meat, poultry and seafood products. The combination of resource efficiency of soya proteins and new technological advances is constantly expanding the long list of applications worldwide. The function of soy protein products in a variety of processed meat, poultry and seafood products is discussed. [ABSTRACT FROM AUTHOR]

Soy proteins and, in particular, isolated soy proteins are being used in coffee creamers and whip toppings. With the increasing cost of traditional protein sources, more food manufacturers are investigating and utilizing soy proteins in other dairy type products. Isolated soy protein added as a replacement for the nonfat dry milk in the production of yogurt increased the viscosity and gel strength to a greater amount than nonfat dry milk and sodium caseinate added on an equivalent protein basis. [ABSTRACT FROM AUTHOR]

Many textural characteristics of food products may be affected by soy protein products. Texture may produce, may limit, may restrict certain of the functional properties of soybean products which have been discussed at this meeting. This paper describes some of the types of textures which soybean products contribute to food products, some of the methodology employed in producing the more common textures, and the rationale for the production of varying textures. [ABSTRACT FROM AUTHOR]

The structure of human inosine triphosphate pyrophosphohydrolase (ITPA) has been determined using diffraction data to 1.6 A resolution. ITPA contributes to the accurate replication of DNA by cleansing cellular dNTP pools of mutagenic nucleotide purine analogs such as dITP or dXTP. A similar high-resolution unpublished structure has been deposited in the Protein Data Bank from a monoclinic and pseudo-merohedrally twinned crystal. Here, cocrystallization of ITPA with a molar ratio of XTP appears to have improved the crystals by eliminating twinning and resulted in an orthorhombic space group. However, there was no evidence for bound XTP in the structure. Comparison with substrate-bound NTPase from a thermophilic organism predicts the movement of residues within helix alpha1, the loop before alpha6 and helix alpha7 to cap off the active site when substrate is bound.

Several chemicals have been associated with risk of non-Hodgkin's lymphoma (NHL), many of which are substrates for N-acetyltransferase (NAT) and glutathione S-transferase (GST) enzymes. We investigated the association between polymorphisms in genes coding for these enzymes and NHL risk in a population-based study (389 cases and 535 controls). NAT1 slow genotype was associated with a slightly increased risk in women [odds ratios (OR) = 1.4; 95% confidence interval (CI) = 0.9-2.3], but not in men. NAT2 slow genotype was not associated with risk in either sex. The two slow genotypes of NAT1 and NAT2 combined were associated with a minor increase of risk in women (OR = 1.4; 0.8-2.4). There was no association with the GSTM1 or GSTT1 null genotype in either sex, irrespective of histological subtypes. Individuals with GSTP1 Val homozygotes had non-significant excessive risk of marginal zone lymphoma (OR = 1.8; 0.6-5.1) and 'other' B-cell NHLs (OR = 1.6; 0.7-3.6), but lower risk of diffuse large B-cell lymphoma (OR = 0.2; 0.1-0.96). Risk did not elevate with an increasing number of high-risk GST alleles in either sex. In summary, although NAT1, NAT2, GSTM1, GSTT1, or GSTP1 polymorphisms do not appear to be associated with NHL risk overall, there might be gender-specific and subtype-specific associations that require confirmation.