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PubMed | Jiangsu University, Food Republic and Zhenjiang Kehua Aquaculture Development Company Ltd
Type: Journal Article | Journal: Journal of agricultural and food chemistry | Year: 2015

The bioavailability and bioavailable forms of collagen after oral administration to rats were investigated in this study. The relative and absolute bioavailability of collagen were 57.8% and 49.6%, respectively, which was indirectly evaluated by the bioavailability of Hyp in collagen using a pharmacokinetic method. The amino acid profile of plasma showed that more than 63.4% of the collagen was absorbed from the intestine in the form of peptide, and there was a good linear correlation between the absorbed amount of an amino acid and its content in collagen (R(2) = 0.9225). The collagen peptides in plasma were purified by Sephadex G10 and Eclipse XDB C18 chromatography and further indentified (Ala-Asn, Ala-Hyp-Gly, Asp-Glu, Glu-Asn, Glu-Asp, Glu-Met, Gly-Pro-Hyp, Leu-Hyp, Leu-Met, Phe-Gly-Asn, Pro-Gly-Leu, Pro-Leu, Ser-Gly-Met, Ser-Hyp, Ser-Pro-Gly, Tyr-Met) with UPLC-ESI-MS. These results may help to speculate about the molecular mechanism behind the physiological effects of collagen after oral administration.


Wang L.,Jiangsu University | Wang Q.,Jiangsu University | Qian J.,Jiangsu University | Liang Q.,Jiangsu University | And 4 more authors.
Journal of Agricultural and Food Chemistry | Year: 2015

The bioavailability and bioavailable forms of collagen after oral administration to rats were investigated in this study. The relative and absolute bioavailability of collagen were 57.8% and 49.6%, respectively, which was indirectly evaluated by the bioavailability of Hyp in collagen using a pharmacokinetic method. The amino acid profile of plasma showed that more than 63.4% of the collagen was absorbed from the intestine in the form of peptide, and there was a good linear correlation between the absorbed amount of an amino acid and its content in collagen (R2 = 0.9225). The collagen peptides in plasma were purified by Sephadex G10 and Eclipse XDB C18 chromatography and further indentified (Ala-Asn, Ala-Hyp-Gly, Asp-Glu, Glu-Asn, Glu-Asp, Glu-Met, Gly-Pro-Hyp, Leu-Hyp, Leu-Met, Phe-Gly-Asn, Pro-Gly-Leu, Pro-Leu, Ser-Gly-Met, Ser-Hyp, Ser-Pro-Gly, Tyr-Met) with UPLC-ESI-MS. These results may help to speculate about the molecular mechanism behind the physiological effects of collagen after oral administration. © 2015 American Chemical Society.


Wang L.,Jiangsu University | Liang Q.,Jiangsu University | Chen Q.,Jiangsu University | Xu J.,Zhenjiang Kehua Aquaculture Development Company Ltd | And 4 more authors.
Food Chemistry | Year: 2014

The hydrolysis kinetics and radical-scavenging activity of gelatin were investigated under simulated gastrointestinal digestion in this study. In the gastric phase, the degree of gelatin hydrolysis increased from 0.17% to 1.20%, while the DPPH radical-scavenging rate increased from 6.27% to 24.56%. Further digestion in the intestinal phase brought the degree of hydrolysis and radical-scavenging rate to 26.08% and 44.76%, respectively. After digestion, the gelatin hydrolysates were separated into two fractions by ultrafiltration. The fraction with an average molecular weight of 312.98 Da exhibited the higher yield (78.26%) and radical-scavenging activity (IC50 = 2.09 mg/ml), suggesting the high digestibility and bioactivity of gelatin after oral administration. The fraction was further purified with multi-step column chromatography and identified to be Gly-Pro-Met (303.38 Da) by UPLC-ESI-MS. These results may help us to better understand its physiological effects and to use it properly in foods and pharmaceuticals. © 2014 Elsevier Ltd. All rights reserved.


Wang L.,Jiangsu University | Liang Q.,Jiangsu University | Wang Z.,Jiangsu University | Xu J.,Zhenjiang Kehua Aquaculture Development Company Ltd | And 2 more authors.
Food Chemistry | Year: 2014

The collagen in Amur sturgeon was extracted by pepsin digestion and separated into two fractions, P2.4 (92.40%) and P4.0 (2.16%), by sodium chloride precipitation. SDS-PAGE and amino acid profile suggested that the P2.4 and P4.0 might be classified as type I collagen (PSC-I) and type V collagen (PSC-V), respectively. These collagens appeared to be dense sheet-like film linked by random-coiled filaments under SEM. The denaturation and melting temperatures of PSC-V (35.92 and 122.86 C) were significantly higher than PSC-I (32.52 and 116.01 C) assessed by CD and DSC, which could be attributed to its higher imino acid content (23.43%) and degree of hydroxylation (52.18%). FTIR confirmed their triple helical structure, and indicated more intermolecular crosslinks in PSC-I and more hydrogen bond in PSC-V. These results provide some basis for their large-scale production and further application as alternatives to mammalian collagen. © 2013 Elsevier Ltd. All rights reserved.


Wang L.,Jiangsu University | Wang Q.,Jiangsu University | Liang Q.,Jiangsu University | He Y.,Jiangsu University | And 4 more authors.
Journal of the Science of Food and Agriculture | Year: 2015

BACKGROUND: Gelatin has long been widely used in foods, pharmaceuticals, cosmetics, and other products. However, there are few reports on its bioavailability and bioavailable forms. In this study, the bioavailability of gelatin was indirectly evaluated by the determining the bioavailability of total hydroxyproline in gelatin using a pharmacokinetic method after oral administration to rats. RESULTS: The relative and absolute bioavailability of gelatin were 74.12% and 85.97%, respectively. The amino acid profile of plasma indicated that 41.91% of the digested gelatin was absorbed from the intestine in the form of peptide, and there was a good linear correlation between the absorbed amount of an amino acid and its content in gelatin (R2 = 0.9566). Moreover, 17 types of collagen peptide were purified by multi-step chromatography and identified with ultra-performance liquid chromatography-electrospray ionisation-mass spectrometry. CONCLUSION: Gelatin had high oral bioavailability. Nearly half of digested gelatin was absorbed from the intestine in the form of various collagen peptides. © 2015 Society of Chemical Industry.


PubMed | Jiangsu University, Zhenjiang Kehua Aquaculture Development Company Ltd and Lianyungang Haideyi Food Company Ltd
Type: Journal Article | Journal: Journal of the science of food and agriculture | Year: 2015

Gelatin has long been widely used in foods, pharmaceuticals, cosmetics, and other products. However, there are few reports on its bioavailability and bioavailable forms. In this study, the bioavailability of gelatin was indirectly evaluated by the determining the bioavailability of total hydroxyproline in gelatin using a pharmacokinetic method after oral administration to rats.The relative and absolute bioavailability of gelatin were 74.12% and 85.97%, respectively. The amino acid profile of plasma indicated that 41.91% of the digested gelatin was absorbed from the intestine in the form of peptide, and there was a good linear correlation between the absorbed amount of an amino acid and its content in gelatin (R(2) = 0.9566). Moreover, 17 types of collagen peptide were purified by multi-step chromatography and identified with ultra-performance liquid chromatography-electrospray ionisation-mass spectrometry.Gelatin had high oral bioavailability. Nearly half of digested gelatin was absorbed from the intestine in the form of various collagen peptides.


PubMed | Jiangsu University, Zhenjiang Entry Exit Inspection and Quarantine Burea and Zhenjiang Kehua Aquaculture Development Company Ltd
Type: | Journal: Food chemistry | Year: 2014

The hydrolysis kinetics and radical-scavenging activity of gelatin were investigated under simulated gastrointestinal digestion in this study. In the gastric phase, the degree of gelatin hydrolysis increased from 0.17% to 1.20%, while the DPPH radical-scavenging rate increased from 6.27% to 24.56%. Further digestion in the intestinal phase brought the degree of hydrolysis and radical-scavenging rate to 26.08% and 44.76%, respectively. After digestion, the gelatin hydrolysates were separated into two fractions by ultrafiltration. The fraction with an average molecular weight of 312.98 Da exhibited the higher yield (78.26%) and radical-scavenging activity (IC50=2.09 mg/ml), suggesting the high digestibility and bioactivity of gelatin after oral administration. The fraction was further purified with multi-step column chromatography and identified to be Gly-Pro-Met (303.38 Da) by UPLC-ESI-MS. These results may help us to better understand its physiological effects and to use it properly in foods and pharmaceuticals.


Liang Q.,Jiangsu University | Wang L.,Jiangsu University | Sun W.,Jiangsu University | Wang Z.,Jiangsu University | And 2 more authors.
Process Biochemistry | Year: 2014

The collagen in Amur sturgeon cartilage was isolated using sodium chloride (salt-solubilized collagen, SSC, 2.18%), followed by acetic acid (acid-solubilized collagen, ASC, 27.04%) and then pepsin (pepsin-solubilized collagen, PSC, 55.92%). These collagens appeared to be dense sheet-like film linked by random-coiled filaments under SEM. The denaturation and melting temperatures of PSC (35.71 and 123.90 °C) were significantly higher than SSC (32.64 and 114.51 °C) and ASC (32.98 and 120.72 °C) assessed by circular dichroism and differential scanning calorimetry, which could be attributed to its high imino acid content (22.57%) and degree of hydroxylation (47.29%). Electrophoresis pattern showed that the SSC and ASC were type I collagen, while PSC was predominantly type II collagen along with other minor types. Infrared spectra confirmed their triple helical structure, and indicated more hydrogen bonding in ASC and more intermolecular crosslinks in PSC. These results provide some basis for their large-scale production and further application as alternatives to mammalian collagen. © 2013 Elsevier Ltd. All rights reserved.


Wang L.,Jiangsu University | Liang Q.,Jiangsu University | Chen T.,Jiangsu University | Wang Z.,Jiangsu University | And 2 more authors.
Food Hydrocolloids | Year: 2014

The collagen in Amur sturgeon skin was isolated using sodium chloride (SSC, 4.55%), acetic acid (ASC, 37.42%) and pepsin (PSC, 52.80%), respectively. The collagens appeared to be dense sheet-like film linked by random-coiled filaments under SEM. The denaturation and melting temperature were 32.15°C and 116.62°C for SSC, 32.78°C and 120.66°C for ASC, 32.46°C and 115.42°C for PSC, assessed by CD and DSC. SDS-PAGE showed that the collagens were mainly type I with two different α chains. The amino acid profiles of them was similar to each other with high imino acid content and hydroxylation degree. FTIR confirmed the triple helical structure of the collagens, and indicated more hydrogen bond in PSC and more intermolecular crosslinks in ASC. These results suggested that the collagens have potential in commercial applications as alternatives to mammalian collagen. © 2013 Elsevier Ltd.


Liang Q.,Jiangsu University | Wang L.,Jiangsu University | He Y.,Jiangsu University | Wang Z.,Jiangsu University | And 2 more authors.
Journal of Functional Foods | Year: 2014

The hydrolysis kinetics and antioxidant activity of collagen from Nile tilapia were investigated under simulated gastrointestinal digestion in this study. From gastric to intestinal phase, degree of hydrolysis increased from 1.15% to 16.74%, while surface hydrophobicity decreased from 21.46% to 2.06%; DPPH radical scavenging increased from 18.22% to 31.79%, but inhibition rate of linoleic acid peroxidation reached 34.63% in 40 min and then kept stability. After digestion, the collagen hydrolysates were separated into three fractions by ultrafiltration. The fraction (86.70%) with average molecular weight of 436.80 Da exhibited the highest antioxidant activity, suggesting the high digestibility and bioactivity of collagen. The fraction was further purified with multi-step chromatography and identified to be Gly-Pro-Met (303.38 Da) by UPLC-ESI-MS with IC50 value being 25.64 μg/mL for DPPH radical. These results may help better understanding its physiological effects and utilize it in foods and pharmaceuticals. © 2014 Elsevier Ltd. All rights reserved.

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