کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
11263224 | 1718108 | 2019 | 46 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Interaction between calcium and casein hydrolysates: Stoichiometry, binding constant, binding sites and thermal stability of casein phosphopeptide complexes
ترجمه فارسی عنوان
تعامل بین هیدرولیزات کلسیم و کازئین: استئشیومتری، ثابت اتصال، سایت های اتصال و پایداری حرارتی مجتمع های کازئین فسفاپتید
دانلود مقاله + سفارش ترجمه
دانلود مقاله ISI انگلیسی
رایگان برای ایرانیان
موضوعات مرتبط
علوم زیستی و بیوفناوری
علوم کشاورزی و بیولوژیک
دانش تغذیه
چکیده انگلیسی
The ability of a casein hydrolysate rich in casein phosphopeptides (CPPs) to form calcium complexes was studied. An association constant of 125 ± 32 L molâ1 at 25 °C was determined electrochemically, forming 1:1 complexes according to conductivity measurements. Chloride anions increased the affinity for calcium and number of CPPs bound to calcium in solution to more than one. From temperature dependence of the association constant, the enthalpy of binding of calcium chloride to CPPs was determined to be â24 kJ molâ1. Fourier transform infrared spectroscopy confirmed solid state binding of chloride and calcium to CPPs, further showing a positive cooperativity induced by calcium due to opening of the alpha-helix structure of CPPs. In addition, calcium chloride complexation was shown to increase the thermal stability of CPPs according to the results of thermogravimetry differential scanning calorimetry. In conclusion, hydrolysed casein could be considered as a potential enhancer of calcium availability in food.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: International Dairy Journal - Volume 88, January 2019, Pages 25-33
Journal: International Dairy Journal - Volume 88, January 2019, Pages 25-33
نویسندگان
Ricardo Troncoso Recio, Nelson P. Guerra, Ana Torrado, Leif H. Skibsted,