کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
5789645 | 1108080 | 2011 | 14 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: Physical properties, molecular structures, and protein quality of texturized whey protein isolate: Effect of extrusion moisture content1 Physical properties, molecular structures, and protein quality of texturized whey protein isolate: Effect of extrusion moisture content1](/preview/png/5789645.png)
To explore the complex relationship between processing conditions and functional and nutritional properties of food products containing whey protein isolate (WPI), we investigated the effect of extrusion texturization at various temperatures (50, 75, and 100°C) and varying moisture levels of the feed (20, 30, 40, and 50%) on changes in the composition, molecular structure, and protein quality of the extrudates. Bradford assay methods were used to determine protein solubility of the extruded WPI as a function of changing level of moisture. Protein compositional changes as a function of extrusion conditions were quantitatively characterized and analyzed by sodium dodecyl sulfate-PAGE and reversed-phase-HPLC techniques. We showed that at a given temperature, increasing the extrusion moisture content resulted in a slight increase in the overall protein water solubility (at 50 and 75°C), averaging approximately 5% per 10% increase in moisture content. A reduction in β-lactoglobulin content was observed at 50°C with increasing moisture content, indicative of the sensitive nature of β-lactoglobulin to extrusion treatment, whereas the amount of α-lactalbumin remained unchanged at all moisture contents used at a set temperature. The protein quality of the extruded WPI, determined chemically by available sulfhydryl and primary and secondary amines, remained relatively unchanged as a function of moisture level. Circular dichroism and intrinsic tryptophan fluorescence spectroscopic studies revealed considerable structural changes, both at the secondary structural level and the tertiary contacts as a function of increasing temperature, and higher moisture levels can slightly preserve secondary structures but not the tertiary contacts of the protein molecules. Atomic force microscopy provided direct visualization of the fine difference of the protein particles caused by changing extrusion moisture contents, which is in close agreement with the results obtained using other techniques in this work.
Journal: Journal of Dairy Science - Volume 94, Issue 5, May 2011, Pages 2231-2244