Transepithelial transport efficiency of bovine collagen hydrolysates in a human Caco-2 cell line model

•Collagen hydrolysates were produced by Alcalase, Flavouzyme, and trypsin.•Transepithelial transport was studied in a Caco-2 cell line.•Alcalase-Flavourzyme (AF) treatment yielded very low molecular weight peptides.•The transepithelial transport efficiency was the greatest for the AF treatment. Coll...

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Veröffentlicht in:Food chemistry 2017-06, Vol.224, p.242-250
Hauptverfasser: Feng, Mengmeng, Betti, Mirko
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description •Collagen hydrolysates were produced by Alcalase, Flavouzyme, and trypsin.•Transepithelial transport was studied in a Caco-2 cell line.•Alcalase-Flavourzyme (AF) treatment yielded very low molecular weight peptides.•The transepithelial transport efficiency was the greatest for the AF treatment. Collagen was extracted from raw bovine hide and hydrolyzed by one of three enzymes – Alcalase, Flavourzyme, or trypsin – or by using a combination of two or three of these enzymes. The Alcalase-containing enzymatic hydrolysis treatments generated a greater proportion of hydrolysates with molecular weight (MW)
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Collagen was extracted from raw bovine hide and hydrolyzed by one of three enzymes – Alcalase, Flavourzyme, or trypsin – or by using a combination of two or three of these enzymes. The Alcalase-containing enzymatic hydrolysis treatments generated a greater proportion of hydrolysates with molecular weight (MW) &lt;2kDa (79.8–82.7%). Flavourzyme-containing hydrolysis treatments exhibited the greatest proportion of free amino acids (686–740nmol/mg). The hydrolysates were then subjected to a simulated gastrointestinal (GI) digestion, and transport studies were conducted using a Caco-2 cell model. Due to the lower MW profile, the hydrolyzed collagen showed greater resistance to GI digestion and greater transport efficiency than the unhydrolyzed collagen control. 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Collagen was extracted from raw bovine hide and hydrolyzed by one of three enzymes – Alcalase, Flavourzyme, or trypsin – or by using a combination of two or three of these enzymes. The Alcalase-containing enzymatic hydrolysis treatments generated a greater proportion of hydrolysates with molecular weight (MW) &lt;2kDa (79.8–82.7%). Flavourzyme-containing hydrolysis treatments exhibited the greatest proportion of free amino acids (686–740nmol/mg). The hydrolysates were then subjected to a simulated gastrointestinal (GI) digestion, and transport studies were conducted using a Caco-2 cell model. Due to the lower MW profile, the hydrolyzed collagen showed greater resistance to GI digestion and greater transport efficiency than the unhydrolyzed collagen control. 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subjects Alcalase
Amino Acids - metabolism
Animals
Bioavailability
Biological Transport
Bovine collagen hydrolysates
Caco-2 cell
Caco-2 Cells
Cattle
Collagen - metabolism
Digestion
Endopeptidases - metabolism
Epithelium - metabolism
Flavourzyme
Humans
Hydrolysis
Low molecular weight peptides
Molecular Weight
Subtilisins - metabolism
Trypsin
Trypsin - metabolism
title Transepithelial transport efficiency of bovine collagen hydrolysates in a human Caco-2 cell line model
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