Hinrichs Jörg, Rademacher Britta
Institute for Food Technology, Department of Animal Foodstuff Technology, University of Hohenheim, Garbenstr 21, D-70599 Stuttgart, Germany
J Dairy Res. 2004 Nov;71(4):480-8. doi: 10.1017/s0022029904000238.
Pressure processing of foodstuff has been applied to produce or modify proteinaceous gel structures. In real pressure processing the treatment is non-isothermal, due to the adiabatic nature of the process and the heat loss from the product to the vessel. In order to estimate the effect of pressurization on milk constituents pressure and temperature dependent kinetics were determined separately from each other. In a detailed kinetic study whey protein isolate was treated under isobaric (200 to 800 MPa) and isothermal conditions (-2 to 70 degrees C), and the resulting degree of denaturation of beta-lactoglobulin A and B and alpha-lactalbumin was analysed. Kinetic parameters of denaturation were estimated using a one step non-linear regression method which allowed a global fit of the whole data set. The isobaric isothermal denaturation of beta-lactoglobulin and alpha-lactalbumin was found to follow third and second order kinetics, respectively. Isothermal pressure denaturation of both beta-lactoglobulin fractions do not differ significantly and were characterized by an activation volume decreasing with increasing temperature from -10 to about -30 ml mol(-1), which demonstrates that the denaturation rate is accelerated with increasing temperature. The activation energy of about 70 to 100 kJ mol(-1) obtained for beta-lactoglobulin A and B is not dependent to a great extent on the pressure which indicates that above 200 MPa denaturation rate is limited by the aggregation rate while pressure forces unfolding of the molecule.
食品的压力处理已被用于生产或改变蛋白质凝胶结构。在实际的压力处理中,由于该过程的绝热性质以及产品向容器的热损失,处理是非等温的。为了评估加压对牛奶成分的影响,分别测定了压力和温度依赖性动力学。在一项详细的动力学研究中,乳清蛋白分离物在等压(200至800兆帕)和等温条件(-2至70摄氏度)下进行处理,并分析了β-乳球蛋白A和B以及α-乳白蛋白的变性程度。使用一步非线性回归方法估计变性动力学参数,该方法允许对整个数据集进行全局拟合。发现β-乳球蛋白和α-乳白蛋白的等压等温变性分别遵循三级和二级动力学。两种β-乳球蛋白组分的等温压力变性没有显著差异,其特征是活化体积随温度从-10增加到约-30毫升摩尔-1而减小,这表明变性速率随温度升高而加快。β-乳球蛋白A和B获得的约70至100千焦摩尔-1的活化能在很大程度上不依赖于压力,这表明在200兆帕以上,变性速率受聚集速率限制,而压力促使分子展开。