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 |
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creator | Feng, Mengmeng Betti, Mirko |
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) |
doi_str_mv | 10.1016/j.foodchem.2016.12.044 |
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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) <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. Hydrolysates from a dual enzyme mixture – the Alcalase/Flavourzyme combination – generated the greatest transport efficiency across Caco-2 cell monolayers (21.4%), two-fold more than that of the collagen control.</description><identifier>ISSN: 0308-8146</identifier><identifier>EISSN: 1873-7072</identifier><identifier>DOI: 10.1016/j.foodchem.2016.12.044</identifier><identifier>PMID: 28159262</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>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</subject><ispartof>Food chemistry, 2017-06, Vol.224, p.242-250</ispartof><rights>2016 Elsevier Ltd</rights><rights>Copyright © 2016 Elsevier Ltd. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c471t-9330be64b9098a1f654e36350ec017331ed36e28a0670db329a9dadd238b83683</citedby><cites>FETCH-LOGICAL-c471t-9330be64b9098a1f654e36350ec017331ed36e28a0670db329a9dadd238b83683</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.foodchem.2016.12.044$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3536,27903,27904,45974</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/28159262$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Feng, Mengmeng</creatorcontrib><creatorcontrib>Betti, Mirko</creatorcontrib><title>Transepithelial transport efficiency of bovine collagen hydrolysates in a human Caco-2 cell line model</title><title>Food chemistry</title><addtitle>Food Chem</addtitle><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) <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. Hydrolysates from a dual enzyme mixture – the Alcalase/Flavourzyme combination – generated the greatest transport efficiency across Caco-2 cell monolayers (21.4%), two-fold more than that of the collagen control.</description><subject>Alcalase</subject><subject>Amino Acids - metabolism</subject><subject>Animals</subject><subject>Bioavailability</subject><subject>Biological Transport</subject><subject>Bovine collagen hydrolysates</subject><subject>Caco-2 cell</subject><subject>Caco-2 Cells</subject><subject>Cattle</subject><subject>Collagen - metabolism</subject><subject>Digestion</subject><subject>Endopeptidases - metabolism</subject><subject>Epithelium - metabolism</subject><subject>Flavourzyme</subject><subject>Humans</subject><subject>Hydrolysis</subject><subject>Low molecular weight peptides</subject><subject>Molecular Weight</subject><subject>Subtilisins - metabolism</subject><subject>Trypsin</subject><subject>Trypsin - metabolism</subject><issn>0308-8146</issn><issn>1873-7072</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkMlOwzAQhi0EomV5BeQjlwQviePcQBWbVIlLOVuOPaGunLjYKVLfnoRSrpxGI33_LB9CN5TklFBxt8nbEKxZQ5ezsc8py0lRnKA5lRXPKlKxUzQnnMhM0kLM0EVKG0LIyMpzNGOSljUTbI7aVdR9gq0b1uCd9niY-m2IA4a2dcZBb_Y4tLgJX64HbIL3-gN6vN7bGPw-6QESdj3WeL3rdI8X2oSMYQPeYz8lumDBX6GzVvsE17_1Er0_Pa4WL9ny7fl18bDMTFHRIas5Jw2IoqlJLTVtRVkAF7wkYAitOKdguQAmNREVsQ1nta6ttpZx2UguJL9Et4e52xg-d5AG1bk03aJ7CLukqBRlOdKsGFFxQE0MKUVo1Ta6Tse9okRNjtVGHR2rybGiTI2Ox-DN745d04H9ix2ljsD9AYDx0y8HUaUfj2BdBDMoG9x_O74BZ1eQ9Q</recordid><startdate>20170601</startdate><enddate>20170601</enddate><creator>Feng, Mengmeng</creator><creator>Betti, Mirko</creator><general>Elsevier Ltd</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>20170601</creationdate><title>Transepithelial transport efficiency of bovine collagen hydrolysates in a human Caco-2 cell line model</title><author>Feng, Mengmeng ; Betti, Mirko</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c471t-9330be64b9098a1f654e36350ec017331ed36e28a0670db329a9dadd238b83683</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><topic>Alcalase</topic><topic>Amino Acids - metabolism</topic><topic>Animals</topic><topic>Bioavailability</topic><topic>Biological Transport</topic><topic>Bovine collagen hydrolysates</topic><topic>Caco-2 cell</topic><topic>Caco-2 Cells</topic><topic>Cattle</topic><topic>Collagen - metabolism</topic><topic>Digestion</topic><topic>Endopeptidases - metabolism</topic><topic>Epithelium - metabolism</topic><topic>Flavourzyme</topic><topic>Humans</topic><topic>Hydrolysis</topic><topic>Low molecular weight peptides</topic><topic>Molecular Weight</topic><topic>Subtilisins - metabolism</topic><topic>Trypsin</topic><topic>Trypsin - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Feng, Mengmeng</creatorcontrib><creatorcontrib>Betti, Mirko</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Food chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Feng, Mengmeng</au><au>Betti, Mirko</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Transepithelial transport efficiency of bovine collagen hydrolysates in a human Caco-2 cell line model</atitle><jtitle>Food chemistry</jtitle><addtitle>Food Chem</addtitle><date>2017-06-01</date><risdate>2017</risdate><volume>224</volume><spage>242</spage><epage>250</epage><pages>242-250</pages><issn>0308-8146</issn><eissn>1873-7072</eissn><abstract>•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) <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. Hydrolysates from a dual enzyme mixture – the Alcalase/Flavourzyme combination – generated the greatest transport efficiency across Caco-2 cell monolayers (21.4%), two-fold more than that of the collagen control.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>28159262</pmid><doi>10.1016/j.foodchem.2016.12.044</doi><tpages>9</tpages></addata></record> |
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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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