Conformational changes in the muscle proteins of cured beef during heating.

Structural changes caused by heating in the proteins of cured beef longissimus dorsi muscle were examined by fluorescence and differential scanning calorimetry. Denaturation occurred in four temperature ranges-40-55°C, 55-61°C, 62-70°C and above 70°C, in contrast to the three endothermic transitions reported for non-cured meats.

Electron microscopic studies of artificial supramolecular structures from collagen solutions.

Changes in the molecular structure of collagen fibrils isolated from solutions of native tropocollagen (TC) and of soluble collagen, obtained by enzymic (ESC) and alkaline-salt (ASC) methods, were studied by electron microscopy. It was found that, under certain conditions, it is possible to derive native-like fibrils (NF), segments with long spacings (SLS) and fibrils with long spacings (FLS)_from collagen solutions, these being very similar to structures precipitated from TC. Despite the fact that more structures with clear cross-striations can be isolated from ESC than from ASC, neither enzymic nor alkali-salt treatments cause substantial changes in the molecular structure of solubilized collagen, this determining its orderly aggregation.

Review of the flavour-contributing volatiles and water-soluble non-volatiles in pork meat and derived products.

In relation to the problem of meat flavour, volatile and minor non-volatile components of raw, cooked and pre-cured cooked pork meat (carbonyls, sulphur compounds, volatile fatty acids, alcohols and other volatiles, nucleotides and their decomposition products, free fatty acids) are considered. Quantitative changes in some of the components, as effected by technological treatments such as heating, curing and curing and heating, are compared. The possibility of evaluating the quality of heated cured pork products by the hydrogen sulphide/mercaptan ratio is indicated.