دورية أكاديمية
Influence of Ternary Complexation between Bovine Serum Albumin, Sodium Phytate, and Divalent Salts on Turbidity and In Vitro Digestibility of Protein.
| العنوان: | Influence of Ternary Complexation between Bovine Serum Albumin, Sodium Phytate, and Divalent Salts on Turbidity and In Vitro Digestibility of Protein. |
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| المؤلفون: | Kaspchak E; Chemical Engineering Department , Federal University of Paraná , Francisco H. dos Santos Street , 81531-980 Curitiba , Paraná , Brazil., Igarashi-Mafra L; Chemical Engineering Department , Federal University of Paraná , Francisco H. dos Santos Street , 81531-980 Curitiba , Paraná , Brazil., Mafra MR; Chemical Engineering Department , Federal University of Paraná , Francisco H. dos Santos Street , 81531-980 Curitiba , Paraná , Brazil. |
| المصدر: | Journal of agricultural and food chemistry [J Agric Food Chem] 2018 Oct 10; Vol. 66 (40), pp. 10543-10551. Date of Electronic Publication: 2018 Sep 28. |
| نوع المنشور: | Journal Article |
| اللغة: | English |
| بيانات الدورية: | Publisher: American Chemical Society Country of Publication: United States NLM ID: 0374755 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1520-5118 (Electronic) Linking ISSN: 00218561 NLM ISO Abbreviation: J Agric Food Chem Subsets: MEDLINE |
| أسماء مطبوعة: | Original Publication: Washington, American Chemical Society. |
| مواضيع طبية MeSH: | Calcium/*chemistry , Magnesium/*chemistry , Phytic Acid/*chemistry , Serum Albumin, Bovine/*chemistry, Animals ; Calcium/metabolism ; Cattle ; Digestion ; Magnesium/metabolism ; Models, Biological ; Phytic Acid/metabolism ; Protein Binding ; Serum Albumin, Bovine/metabolism ; Solubility ; Thermodynamics |
| مستخلص: | Phytate decreases mineral and protein availability and influences protein properties, such as solubility and stability. The binding constants and turbidity data can help with the understanding of the influence of phytate and divalent salts on protein behavior. Ternary complexes formed between bovine serum albumin, sodium phytate, and divalent salts were investigated by isothermal titration calorimetry, turbidity, and in vitro protein digestibility. Results showed a positive entropy change and a negative and small enthalpy change as a result of electrostatic binding forces and ternary and binary complex precipitation. The interaction was favored for the systems containing calcium and manganese, whereas those containing magnesium showed a low heat of interaction. Despite the high protein digestibility, the stability of divalent phytates in a wide pH range may decrease mineral bioavailability. These results can provide important insights for the study of mineral bioavailability and diverse processes that involve protein and minerals in several areas of knowledge. |
| فهرسة مساهمة: | Keywords: calcium; isothermal titration calorimetry; magnesium; manganese; phytic acid; simplex lattice design |
| المشرفين على المادة: | 27432CM55Q (Serum Albumin, Bovine) 7IGF0S7R8I (Phytic Acid) I38ZP9992A (Magnesium) SY7Q814VUP (Calcium) |
| تواريخ الأحداث: | Date Created: 20180920 Date Completed: 20181019 Latest Revision: 20181019 |
| رمز التحديث: | 20240628 |
| DOI: | 10.1021/acs.jafc.8b03142 |
| PMID: | 30227705 |
| قاعدة البيانات: | MEDLINE |
Find this issue from the American Chemical Society | تدمد: | 1520-5118 |
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| DOI: | 10.1021/acs.jafc.8b03142 |