Absorption and Urinary Excretion of Peptides after Collagen Tripeptide Ingestion in Humans

Yamamoto, Shoko; Deguchi, Kisaburo; Onuma, Masamichi; Numata, Noriaki; Sakai, Yasuo

doi:10.1248/bpb.b15-00624

Cited by 74 publications

(63 citation statements)

References 26 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…From Table 1, MCPs from the skin of tilapia contained seven essential amino acids (16.18%) and ten nonessential amino acids (79.56%). Collagen hydrolysates usually contain a high concentration of collagen tripeptides with a Gly-X-Y sequence [30,31]. The contents of glycine, proline and hydroxyproline as the major amino acids in MCPs accounted for 20.92%, 11.32% and 10.28%, respectively.…”

Section: Resultsmentioning

confidence: 99%

Marine Collagen Peptides from the Skin of Nile Tilapia (Oreochromis niloticus): Characterization and Wound Healing Evaluation

et al. 2017

View full text Add to dashboard Cite

Burns can cause tremendous economic problems associated with irreparable harm to patients and their families. To characterize marine collagen peptides (MCPs) from the skin of Nile tilapia (Oreochromis niloticus), molecular weight distribution and amino acid composition of MCPs were determined, and Fourier transform infrared spectroscopy (FTIR) was used to analyze the chemical structure. Meanwhile, to evaluate the wound healing activity, in vitro and in vivo experiments were carried out. The results showed that MCPs prepared from the skin of Nile tilapia by composite enzymatic hydrolysis were composed of polypeptides with different molecular weights and the contents of polypeptides with molecular weights of less than 5 kDa accounted for 99.14%. From the amino acid composition, the majority of residues, accounting for over 58% of the total residues in MCPs, were hydrophilic. FTIR indicated that the main molecular conformations inside MCPs were random coil. In vitro scratch assay showed that there were significant effects on the scratch closure by the treatment of MCPs with the concentration of 50.0 μg/mL. In the experiments of deep partial-thickness scald wound in rabbits, MCPs could enhance the process of wound healing. Therefore, MCPs from the skin of Nile tilapia (O. niloticus) have promising applications in wound care.

show abstract

Section: Resultsmentioning

confidence: 99%

Marine Collagen Peptides from the Skin of Nile Tilapia (Oreochromis niloticus): Characterization and Wound Healing Evaluation

et al. 2017

View full text Add to dashboard Cite

show abstract

“…Of these, only Pro‐Hyp and one of the Ile/Leu‐Hyp isomers were further validated as BFIs for red meat. Pro‐Hyp is the main constituent of food‐derived collagen, while Ile/Leu‐Hyp and other Hyp‐peptides are less abundant . Although beef ribs and pork shoulders are considered rich sources of collagen, leaner meat, as that provided in Study‐D, is by no means free of connective tissue.…”

Section: Discussionmentioning

confidence: 99%

Combined Markers to Assess Meat Intake—Human Metabolomic Studies of Discovery and Validation

Cuparencu

Rinnan

Dragsted

2019

Molecular Nutrition Food Res

View full text Add to dashboard Cite

Scope Biomarkers of red meat may clarify the relationship between meat intake and health. This paper explores the discovery of biomarkers of intake for three types of meat with varying heme iron content. Candidate biomarkers for red and general meat are further evaluated based on defined validation criteria. Methods and results In a randomized cross‐over meal study, healthy volunteers consume a randomized sequence of four test meals: chicken, pork, beef, and a control made of egg white and pea. Fasting and postprandial urine samples are collected to cover 48 h and profiled by untargeted LC‐ESI‐qTOF‐MS metabolomics. The profiles following the meal challenges are explored by univariate and multivariate analyses. Nine red, four white, and eight general meat biomarkers are selected as putative biomarkers, originating from collagen degradation, flavour compounds, and amino acid metabolism. Heme‐related metabolites are masked by the chlorophyll content of the control meal. The candidate biomarkers are confirmed in an independent meal study and validated for plausibility, robustness, time‐response, and prediction performance. Combinations of biomarkers are more efficient than single markers in predicting meat intake. Conclusion New combinations of partially validated biomarkers are proposed to assess terrestrial meat intake and thus help disentangle the effects of meat consumption on human health.

show abstract

“…Collagen is an insoluble‐in‐water high‐molecular‐weight protein (Shoulders & Raines, ). Conversely, the mixture of peptides derived from the digestion of collagen are highly soluble in water, and active peptides can be detected in blood stream and skin a few minutes after oral administration (Osawa et al., ; Yamamoto, Deguchi, Onuma, Numata, & Sakai, ; Yazaki et al., ). The manufacturing process of collagen hydrolysate requires two main steps: first, the soluble fraction is obtained by chemical (acidic or basic) or enzymatic hydrolysis, then LMW peptides are isolated by filtration or ultrafiltration procedures (Mohammad et al., ).…”

Section: Introductionmentioning

confidence: 99%

Determination of Peptide Profile Consistency and Safety of Collagen Hydrolysates as Quality Attributes

López‐Morales

Vázquez-Leyva

Vallejo-Castillo

et al. 2019

Journal of Food Science

View full text Add to dashboard Cite

Collagen hydrolysates are dietary supplements used for nutritional and medical purposes. They are complex mixtures of low‐molecular‐weight peptides obtained from the enzymatic hydrolysis of collagen, which provide intrinsic batch‐to‐batch heterogeneity. In consequence, the quality of these products, which is related to the reproducibility of their mass distribution pattern, should be addressed. Here, we propose an analytical approach to determine the peptide pattern as a quality attribute of Colagenart®, a product containing collagen hydrolysate. In addition, we evaluated the safety by measuring the viability of two cell lines exposed to the product. The consistency of peptide distribution was determined using Size Exclusion Chromatography (SEC), Mass Spectrometry coupled to a reversed phase UPLC system (MS‐RP‐UPLC), and Shaped‐pulse off‐resonance water‐presaturation proton nuclear magnetic resonance spectrometry [ 1 Hwater_presat NMR]. The mass distribution pattern determined by SEC was in a range from 1.35 to 17 kDa, and from 2 to 14 kDa by MS‐RP‐UPLC. [ 1 Hwater_presat NMR] showed the detailed spin‐systems of the collagen hydrolysates components by global assignment of backbone Hα and NH, as well as side‐chain proton resonances. Additionally, short‐range intraresidue connectivity pathways of identified spin‐regions were obtained by a 2D homonuclear shift correlation Shaped‐pulse solvent suppression COSY scheme. Safety analysis of Colagenart® was evaluated in CaCo‐2 and HepG2 cells at 2.5 and 25 μg/mL and no negative effects were observed. The results demonstrated batch‐to‐batch reproducibility, which evinces the utility of this approach to establish the consistency of the quality attributes of collagen hydrolysates. Practical Application We propose state‐of‐the art analytical methodologies (SEC, MS, and NMR) to evaluate peptide profile and composition of collagen hydrolysates as quality attributes. These methodologies are suitable to be implemented for quality control purposes.

show abstract

Absorption and Urinary Excretion of Peptides after Collagen Tripeptide Ingestion in Humans

Cited by 74 publications

References 26 publications

Marine Collagen Peptides from the Skin of Nile Tilapia (Oreochromis niloticus): Characterization and Wound Healing Evaluation

Marine Collagen Peptides from the Skin of Nile Tilapia (Oreochromis niloticus): Characterization and Wound Healing Evaluation

Combined Markers to Assess Meat Intake—Human Metabolomic Studies of Discovery and Validation

Determination of Peptide Profile Consistency and Safety of Collagen Hydrolysates as Quality Attributes

Contact Info

Product

Resources

About