Improved absorption of caseinophosphopeptide-bound iron: role of alkaline phosphatase

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• 作者：Bertille Ani-Kibangou ; Saï ; d Bouhallab ; Daniel Mollé ; Gwé ; naë ; le Henry ; Franç ; ois Bureau ; Dominique Neuville ; Pierre Arhan and Dominique Bouglé
• 关键词：Biologically active peptides ; Caseinophosphopeptides ; Iron absorption ; Alkaline phosphatase
• 刊名：Journal of Nutritional Biochemistry
• 出版年：2005
• 期刊代码：70_09552863
• 类别：abs
• 出版时间：2005
• 卷：16
• 期：7
• 页码：398-401
• 文件大小：100 K

摘要

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.