دورية أكاديمية
Effect of divalent cations on bovine serum albumin (BSA) and tannic acid interaction and its influence on turbidity and in vitro protein digestibility.
| العنوان: | Effect of divalent cations on bovine serum albumin (BSA) and tannic acid interaction and its influence on turbidity and in vitro protein digestibility. |
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| المؤلفون: | Kaspchak E; Chemical Engineering Department, Federal University of Paraná, Polytechnic Center, Jardim das Américas, 81531-980 Curitiba, PR, Brazil., Goedert AC; Department of Biochemistry and Molecular Biology, Federal University of Paraná, Rua Francisco H. dos Santos s/n, 81531-980 Curitiba, PR, Brazil., Igarashi-Mafra L; Chemical Engineering Department, Federal University of Paraná, Polytechnic Center, Jardim das Américas, 81531-980 Curitiba, PR, Brazil., Mafra MR; Chemical Engineering Department, Federal University of Paraná, Polytechnic Center, Jardim das Américas, 81531-980 Curitiba, PR, Brazil. Electronic address: marcos.mafra@ufpr.br. |
| المصدر: | International journal of biological macromolecules [Int J Biol Macromol] 2019 Sep 01; Vol. 136, pp. 486-492. Date of Electronic Publication: 2019 Jun 15. |
| نوع المنشور: | Journal Article |
| اللغة: | English |
| بيانات الدورية: | Publisher: Elsevier Country of Publication: Netherlands NLM ID: 7909578 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1879-0003 (Electronic) Linking ISSN: 01418130 NLM ISO Abbreviation: Int J Biol Macromol Subsets: MEDLINE |
| أسماء مطبوعة: | Publication: Amsterdam : Elsevier Original Publication: Guildford, Eng., IPC Science and Technology Press. |
| مواضيع طبية MeSH: | Cations, Divalent/*pharmacology , Serum Albumin, Bovine/*metabolism , Tannins/*metabolism, Animals ; Cattle ; Digestion/drug effects ; Hydrogen-Ion Concentration ; Osmolar Concentration ; Protein Binding/drug effects ; Protein Stability ; Thermodynamics |
| مستخلص: | Tannins, proteins, and divalent cations interactions are important for many processes in the food industry and human and animal nutrition and health. The effect of magnesium, calcium, and manganese on the interaction, turbidity, and in vitro protein digestibility of bovine serum albumin and tannic acid complexes was studied. The divalent cations increase the affinity and influence the enthalpy and entropy changes of the protein and tannin binding. Magnesium maintained the nature of interactions, and calcium and manganese changed the binding mechanism. The factor that most influenced turbidity was the tannic acid and divalent cations binary interaction. Samples containing tannic acid and magnesium and calcium decreased the protein digestibility. Manganese increased the in vitro protein digestibility when compared with samples without salt addition; nevertheless, the complexes formed was higher. These finds can help in the understanding of interactions involved food system and in physiological conditions. (Copyright © 2019 Elsevier B.V. All rights reserved.) |
| فهرسة مساهمة: | Keywords: Bioavailability; Isothermal titration calorimetry; Ternary complex |
| المشرفين على المادة: | 0 (Cations, Divalent) 0 (Tannins) 27432CM55Q (Serum Albumin, Bovine) |
| تواريخ الأحداث: | Date Created: 20190618 Date Completed: 20191230 Latest Revision: 20191230 |
| رمز التحديث: | 20231215 |
| DOI: | 10.1016/j.ijbiomac.2019.06.102 |
| PMID: | 31207325 |
| قاعدة البيانات: | MEDLINE |
Full Text Finder | تدمد: | 1879-0003 |
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| DOI: | 10.1016/j.ijbiomac.2019.06.102 |