Effect of Heating on Water Soluble Biuret-Positive Compounds of Canned Cured Pork Picnic Shoulder

Protein solubility loss as a result of heat denaturation/coaguiation was followed by a ratio of extractable biuret positive compounds (EBPR). Extracts of water-soluble proteins were evaluated by isoelectric focusing (IEF) on polyacrylamide gels. Four heat treatments (60°C, 62.8°C, 65.6°C and 68.8°C) were employed in processing canned (No. 300×407) cured pork. Center cores from canned samples were ground for water soluble protein extraction utilizing a 1:3.3 meat-to-water ratio by high-speed blending (Sorvall Omni-mixer) for 1 min at 0-2°C, centrifuging 10 min at 27,000 ×g at 0-2°C and filtering (0.45-μa.m) with vacuum assist. Eight ml of the clear extract was re-heated in a glass tube for 15 min at 70°C, removed, and chilled (0-2°C) immediately. Coagulum was removed by filtration. EBPR was calculated from mg of protein/ml of initial muscle extract divided by mg of protein/ml of reheated extract for each temperature treatment. EBPR values were 1.75, 1.24, 1.13, and 1.10, respectively. Using 70°C as the critical temperature, an upper 95% confidence limit EBPR value of 1.12 was calculated. Portions of protein extract were isoelectrofocused on thin layer (0.8 mm) low concentration (5% monomer) polyacrylamide gels (pH gradient 3-10). IEF gels generally showed resolution of 12 to 23 protein bands in the muscle extracts, depending upon temperature treatment. Certain bands with apparent isoelectric points (pis) ranging from 7.4 to 8.5 decreased in staining intensity (silver stain) as temperature increased. The general protein separation profiles correlated with decreasing EBPR values as temperature increased.