Isolation and Structural Identification of Iron (Ⅱ)-Chelated Oligopeptides from Black-Bone Silky Fowl
LIU Wen-ying
LU Jun
SONG Sha-sha
GU Rui-zeng
REN Di-feng
CAI Mu-yi
Abstract：Black-bone silky fowl oligopeptides (BSFOP) were prepared by enzymatic hydrolysis of muscle from black-bone silky fowls and then reacted with iron (II) to yield iron (II)-chelated black-bone silky fowl oligopeptides (BSFOP-Fe).The iron-chelating capacity of BSFOP was 84.76±0.12％.BSFOP-Fe had a high protein content (54.64 ± 1.03％) and low molecular weight;85.50％ ofpeptides were less than 1000 u.Scanning electron microscopy,ultraviolet (UV) wavelength scanning,and infrared spectra were used to analyze the structure of BSFOP-Fe,and the results showed that BSFOP-Fe was a new type of iron-chelated compound.An in vitro stability study indicated that BSFOP-Fe maintained certain stability against temperature,pH,and in vitro gastric protease digestion.BSFOP-Fe was separated and purified by reverse-phase high performance liquid chromatography.One main fraction was collected and analyzed by mass spectrometry.One pentapeptide was identified from the main fraction of BSFOP-FE,and its amino acid sequence was Thr-Ser-Gly-Met-Pro.BSFOP-Fe could be applied as a food additive,to dietary nutrients,and to pharmaceutical products as an iron supplement.
Keywords：black-bone silky fowlcharacteristiclow-molecular-weight peptidesiron-chelated peptidesstructure identification
Publication Date：2017-01-01
Online Publishing Date：2025-08-15(First online date of this platform, not the publication date of the document)
Pages：9( 95-102,79 )