2. Academic Validation
  3. Identification of a novel food-derived collagen peptide, hydroxyprolyl-glycine, in human peripheral blood by pre-column derivatisation with phenyl isothiocyanate

Identification of a novel food-derived collagen peptide, hydroxyprolyl-glycine, in human peripheral blood by pre-column derivatisation with phenyl isothiocyanate

  • Food Chem. 2011 Dec 1;129(3):1019-24. doi: 10.1016/j.foodchem.2011.05.066.
Yasutaka Shigemura 1,  Saeko Akaba 2,  Eriko Kawashima 3,  Eun Young Park 2,  Yasushi Nakamura 2,  Kenji Sato 4
Affiliations

Affiliations

  • 1 Osaka Yuhigaoka Gakuen Junior College, 7-72 Ikutamadera-cho, Tennoji, Osaka 543-0073, Japan; Division of Applied Life Sciences, Graduate School of Life and Environment Sciences, Kyoto Prefectural University, 1-5 Shimogamo, Kyoto 606-8522, Japan.
  • 2 Division of Applied Life Sciences, Graduate School of Life and Environment Sciences, Kyoto Prefectural University, 1-5 Shimogamo, Kyoto 606-8522, Japan.
  • 3 Yokohama Research Center, Chisso Corporation, 5-1, Okawa, Kanazawa-ku, Yokohama 236-8605, Japan.
  • 4 Division of Applied Life Sciences, Graduate School of Life and Environment Sciences, Kyoto Prefectural University, 1-5 Shimogamo, Kyoto 606-8522, Japan. Electronic address: [email protected].
PMID: 25212331 DOI: 10.1016/j.foodchem.2011.05.066
Abstract

Peptides in the blood of subjects before and after collagen hydrolysate ingestion were fractionated by ion exchange and size-exclusion chromatographies and then derivatised with phenyl isothiocyanate. The derivatives were characterised by reserved phase (RP)-HPLC. Prolyl-hydroxyproline (Pro-Hyp), which has been identified in the previous studies, was detected as a major food-derived collagen peptide in the blood of all subjects (n=5). Another major peptide was identified as hydroxyprolyl-glycine (Hyp-Gly) in the blood of four subjects, which has not been detected in previous studies. The ratio of Hyp-Gly to Pro-Hyp depended on subjects and ranged from 0.00 to 5.04. Hyp-Gly was less susceptible to human serum peptidase than Pro-Hyp. Hyp-Gly enhanced the growth of mouse primary fibroblasts on collagen gels in a higher extent than Pro-Hyp. These findings suggest that Hyp-Gly plays a significant role in exerting the biological effects by ingestion of collagen hydrolysate.

Keywords

Collagen; Collagen hydrolysate; Fibroblasts; Hyp; Hyp-Gly; Peptide; Plasma; Pro-Hyp; Skin.

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