کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
9891545 | 1540767 | 2005 | 4 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Improved absorption of caseinophosphopeptide-bound iron: role of alkaline phosphatase
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
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چکیده انگلیسی
Hydrolysis of proteins could lessen their inhibiting effect on the poor absorption of cow's milk iron (Fe), which is responsible for the high incidence of Fe deficiency worldwide. When bound to Fe, caseinophosphopeptides (CPP) derived from milk proteins resist luminal digestion, enhance Fe solubility and could improve its bioavailability; brush border enzyme alkaline phosphatase activity could influence iron absorption by releasing free Fe; this study assessed its role in the absorption of CPP-bound Fe. Rat duodenal loops were perfused with Fe gluconate or Fe bound to the CPP of β casein [β-CN (1-25)], with or without the addition of an inhibitor of alkaline phosphatase, Na2WO4. The uptake of Fe-β-CN (1-25) was greater than Fe gluconate. Na2WO4 enhanced the uptake of Fe-β-CN (1-25) and not of Fe gluconate. So the release of free, insoluble Fe, by alkaline phosphatase seems to be prevented by providing Fe in the Fe-β-CN (1-25) complex form. Its good disappearance rate makes β-CN (1-25)-bound Fe a candidate for food fortification.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: The Journal of Nutritional Biochemistry - Volume 16, Issue 7, July 2005, Pages 398-401
Journal: The Journal of Nutritional Biochemistry - Volume 16, Issue 7, July 2005, Pages 398-401
نویسندگان
Bertille Ani-Kibangou, Saïd Bouhallab, Daniel Mollé, Gwénaële Henry, François Bureau, Dominique Neuville, Pierre Arhan, Dominique Bouglé,