TY - JOUR
T1 - Fractionation and identification of Alaska pollock skin collagen-derived mineral chelating peptides
AU - Guo, Lidong
AU - Harnedy, Pádraigín A.
AU - O'Keeffe, Martina B.
AU - Zhang, Li
AU - Li, Bafang
AU - Hou, Hu
AU - Fitzgerald, Richard J.
N1 - Publisher Copyright:
© 2014 Elsevier Ltd. All rights reserved.
PY - 2015/4/15
Y1 - 2015/4/15
N2 - Peptides with the ability to chelate dietary minerals have been reported to have potential as functional food ingredients. A collagen tryptic hydrolysate (CTH), previously shown to chelate iron, was further investigated for the presence of Ca, Fe and Cu chelating peptides. Sequential purification steps, including immobilised metal affinity chromatography (IMAC) and gel permeation chromatography (GPC) were employed for the separation of chelating peptides. GPC analysis showed that the mineral chelating peptides were mainly between 500 and 2000 Da. Subsequent identification was carried out using UPLC-ESI-QTOF MS/MS. Overall, 10 sequences were identified as potential chelating peptides. The Ca, Fe and Cu chelating activity of GPAGPHGPPG was 11.52 ± 2.23 nmol/μmol, 1.71 ± 0.17 nmol/μmol and 0.43 ± 0.02 μmol/μmol, respectively. This study identifies collagen as a good source of peptides with potential applications as functional ingredients in the management of mineral deficiencies.
AB - Peptides with the ability to chelate dietary minerals have been reported to have potential as functional food ingredients. A collagen tryptic hydrolysate (CTH), previously shown to chelate iron, was further investigated for the presence of Ca, Fe and Cu chelating peptides. Sequential purification steps, including immobilised metal affinity chromatography (IMAC) and gel permeation chromatography (GPC) were employed for the separation of chelating peptides. GPC analysis showed that the mineral chelating peptides were mainly between 500 and 2000 Da. Subsequent identification was carried out using UPLC-ESI-QTOF MS/MS. Overall, 10 sequences were identified as potential chelating peptides. The Ca, Fe and Cu chelating activity of GPAGPHGPPG was 11.52 ± 2.23 nmol/μmol, 1.71 ± 0.17 nmol/μmol and 0.43 ± 0.02 μmol/μmol, respectively. This study identifies collagen as a good source of peptides with potential applications as functional ingredients in the management of mineral deficiencies.
KW - Chelating/binding peptides
KW - Collagen
KW - ESI-MS
KW - Functional food
KW - IMAC
UR - http://www.scopus.com/inward/record.url?scp=84908425943&partnerID=8YFLogxK
U2 - 10.1016/j.foodchem.2014.10.055
DO - 10.1016/j.foodchem.2014.10.055
M3 - Article
C2 - 25466056
AN - SCOPUS:84908425943
SN - 0308-8146
VL - 173
SP - 536
EP - 542
JO - Food Chemistry
JF - Food Chemistry
ER -