Isolation and Structural Identification of Iron (II)-Chelated Oligopeptides from Black-Bone Silky Fowl
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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% of peptides 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.
