期刊
FOOD CHEMISTRY
卷 129, 期 2, 页码 485-490出版社
ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2011.04.103
关键词
Chelating peptides; Chickpea; Protein hydrolysate; Pepsin; Pancreatin
资金
- Spanish Ministry of Innovation and Science [AGL2007-63580]
A chickpea protein hydrolysate produced with pepsin and pancreatin was used for the affinity purification of chickpea chelating peptides. Three chelating peptide fractions were obtained after affinity chromatography with immobilised copper. These peptide fractions showed a higher chelating activity and histidine contents than the original protein hydrolysate. Chelating activity was positively correlated with the histidine content of the purified fractions. Different subfractions were also obtained after gel filtration chromatography from the affinity purified peptide fractions. Some of these subfractions showed a higher chelating activity and histidine contents than the original fractions. These results suggest that a combination of high His contents, around 20-30%, and small peptide size provide the best chelating activities. Thus sequential purification with affinity and gel filtration chromatography is a useful procedure for the purification of chickpea peptides with high chelating activity. These results show that a range of chelating peptides are generated during digestion of the chickpea proteins that, after metal chelation, may prevent the generation of reactive oxygen species (ROS) and favour metal absorption. (C) 2011 Elsevier Ltd. All rights reserved.
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