作者: F. Speroni , N. Szerman , S.R. Vaudagna
DOI: 10.1016/J.IFSET.2014.03.011
关键词: Myosin head 、 Hydrostatic pressure 、 Protein aggregation 、 Salt content 、 Denaturation (biochemistry) 、 Pressure level 、 Sodium 、 Chemistry 、 Chromatography 、 Native state
摘要: Abstract Beef patties added with sodium tripolyphosphate (STPP; 0, 0.25 or 0.5%) and/or NaCl (0, 1 2%) were treated at 200 300 MPa (5 min, 5 °C) kept refrigerated (non-pressurized). In non-pressurized patties, NaCl-solubilized proteins denatured, whereas STPP-solubilized remained in native state. At 200 MPa, myosin head was more sensitive to high hydrostatic pressure (HHP) than actin. 1% favored HHP-induced denaturation of and actin, 0.25% STPP protected against that effect. 300 MPa, head, actin other proteins. The effect 200 MPa may depend on the presence specific binding sites for anion, which would be destroyed 300 MPa. Insoluble aggregates formed samples without salts. Salts minimized protein aggregation observed Noticeable differences thermal aggregative behavior occurred whether HHP level Industrial relevance Currently, reduction content manufacture meat products is a hot topic it expected this issue will become relevant next years, as response consumers' demands. Soluble pressure-denatured beef provide interesting texture technological properties reduced salt content.