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Purification of an iron‐binding peptide from scad ( Decapterus maruadsi ) processing by‐products and its effects on iron absorption by Caco‐2 cells
Author(s) -
Jiang Han,
Zhang Wenting,
Chen Fangyuan,
Zou Jiong,
Chen Wenwei,
Huang Guangrong
Publication year - 2019
Publication title -
journal of food biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.507
H-Index - 47
eISSN - 1745-4514
pISSN - 0145-8884
DOI - 10.1111/jfbc.12876
Subject(s) - peptide , chemistry , ultrafiltration (renal) , chelation , size exclusion chromatography , hydrolysis , chromatography , biochemistry , iron deficiency , absorption (acoustics) , inorganic chemistry , enzyme , medicine , physics , acoustics , anemia
This work was aimed at producing peptides containing iron‐binding capabilities from scad ( Decapterus maruadsi ) processing by‐product with alcalase hydrolysis. The chelating peptides were purified by ultrafiltration, immobilized‐metal affinity chromatography, gel filtration chromatography, and reversed‐phase high‐performance liquid chromatography. A novel iron‐binding peptide was purified with 1,386.63 Da molecular weight and amino acid sequence of QKGTYDDYVEGL. The peptide binds to iron mainly through carboxyl and hydroxyl oxygen bonds. The iron‐binding peptide can significantly promote the absorption of inorganic iron in Caco‐2 cells. These results have contributed to development of the peptide from scad processing by‐products hydrolyzate in iron supplementations. Practical applications Iron deficiency is one of the most common and widespread nutritional disorders in the world. Iron‐peptide chelates may be suitable for iron‐fortification. Our study shows that a peptide purified from scad processing by‐product has iron‐chelating activity, and significantly increases iron absorption by Caco‐2 cells. Hence, this peptide has potential application as a novel carrier for enhancing iron absorption.