Interactions between β-Lactoglobulin and Pectins during in Vitro Gastric Hydrolysis
This paper deals with the influence of different levels of three pectins, low-methylated pectin (LMP), high-methylated pectin (HMP), and low-methylated and amidated pectin (LMA), on the in vitro gastric hydrolysis of β-lactoglobulin (β-lg). Proteolysis by pepsin consisted of a 2-h progressive reduct...
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| Veröffentlicht in: | Journal of agricultural and food chemistry 2004-01, Vol.52 (2), p.355-360 |
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| creator | Nacer S, Ahmed Sanchez, Christian Villaume, Christian Mejean, Luc Mouecoucou, Justine |
| description | This paper deals with the influence of different levels of three pectins, low-methylated pectin (LMP), high-methylated pectin (HMP), and low-methylated and amidated pectin (LMA), on the in vitro gastric hydrolysis of β-lactoglobulin (β-lg). Proteolysis by pepsin consisted of a 2-h progressive reduction of pH. A turbidity measurement of β-lg−pectin mixtures was carried out during the proteolysis. The influence of pectins on pepsin enzymatic activity was also evaluated. β-Lg was resistant to peptic digestion. The presence of each of the three pectins at a concentration of 50 wt % increased the N release at all pH values considered, despite a significant inhibition of the pepsin enzymatic activity with the pectins. The turbidity of β-lg solutions during proteolysis was reduced by the addition of pectins, because of the formation of electrostatic complexes between this protein and pectins. The increase of N release could be a false positive result due to the difficulty of precipitating protein by trichloroacetic acid because of the formation of electrostatic complexes demonstrated by the decrease of turbidity. Keywords: β-Lactoglobulin; pectin; pepsin; N release; turbidity; pepsin enzymatic activity |
| doi_str_mv | 10.1021/jf034584a |
| format | Article |
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Proteolysis by pepsin consisted of a 2-h progressive reduction of pH. A turbidity measurement of β-lg−pectin mixtures was carried out during the proteolysis. The influence of pectins on pepsin enzymatic activity was also evaluated. β-Lg was resistant to peptic digestion. The presence of each of the three pectins at a concentration of 50 wt % increased the N release at all pH values considered, despite a significant inhibition of the pepsin enzymatic activity with the pectins. The turbidity of β-lg solutions during proteolysis was reduced by the addition of pectins, because of the formation of electrostatic complexes between this protein and pectins. The increase of N release could be a false positive result due to the difficulty of precipitating protein by trichloroacetic acid because of the formation of electrostatic complexes demonstrated by the decrease of turbidity. Keywords: β-Lactoglobulin; pectin; pepsin; N release; turbidity; pepsin enzymatic activity</description><identifier>ISSN: 0021-8561</identifier><identifier>EISSN: 1520-5118</identifier><identifier>DOI: 10.1021/jf034584a</identifier><identifier>PMID: 14733521</identifier><identifier>CODEN: JAFCAU</identifier><language>eng</language><publisher>Washington, DC: American Chemical Society</publisher><subject>Analytical, structural and metabolic biochemistry ; Biological and medical sciences ; Food engineering ; Fundamental and applied biological sciences. Psychology ; Glycoproteins ; Hydrogen-Ion Concentration ; Hydrolysis ; Lactoglobulins - chemistry ; Lactoglobulins - metabolism ; Life Sciences ; Methylation ; Nephelometry and Turbidimetry ; Pectins - chemistry ; Pectins - pharmacology ; Pepsin A - antagonists & inhibitors ; Pepsin A - metabolism ; Proteins ; Static Electricity</subject><ispartof>Journal of agricultural and food chemistry, 2004-01, Vol.52 (2), p.355-360</ispartof><rights>Copyright © 2004 American Chemical Society</rights><rights>2004 INIST-CNRS</rights><rights>Copyright</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a413t-b062b920b69e5ffea6c7811ab3bfdeb5892d04aceea75b27134151042f0cc3e43</citedby><cites>FETCH-LOGICAL-a413t-b062b920b69e5ffea6c7811ab3bfdeb5892d04aceea75b27134151042f0cc3e43</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/jf034584a$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/jf034584a$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>230,314,776,780,881,2751,27055,27903,27904,56716,56766</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=15410607$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/14733521$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.inrae.fr/hal-02682873$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Nacer S, Ahmed</creatorcontrib><creatorcontrib>Sanchez, Christian</creatorcontrib><creatorcontrib>Villaume, Christian</creatorcontrib><creatorcontrib>Mejean, Luc</creatorcontrib><creatorcontrib>Mouecoucou, Justine</creatorcontrib><title>Interactions between β-Lactoglobulin and Pectins during in Vitro Gastric Hydrolysis</title><title>Journal of agricultural and food chemistry</title><addtitle>J. Agric. Food Chem</addtitle><description>This paper deals with the influence of different levels of three pectins, low-methylated pectin (LMP), high-methylated pectin (HMP), and low-methylated and amidated pectin (LMA), on the in vitro gastric hydrolysis of β-lactoglobulin (β-lg). Proteolysis by pepsin consisted of a 2-h progressive reduction of pH. A turbidity measurement of β-lg−pectin mixtures was carried out during the proteolysis. The influence of pectins on pepsin enzymatic activity was also evaluated. β-Lg was resistant to peptic digestion. The presence of each of the three pectins at a concentration of 50 wt % increased the N release at all pH values considered, despite a significant inhibition of the pepsin enzymatic activity with the pectins. The turbidity of β-lg solutions during proteolysis was reduced by the addition of pectins, because of the formation of electrostatic complexes between this protein and pectins. The increase of N release could be a false positive result due to the difficulty of precipitating protein by trichloroacetic acid because of the formation of electrostatic complexes demonstrated by the decrease of turbidity. Keywords: β-Lactoglobulin; pectin; pepsin; N release; turbidity; pepsin enzymatic activity</description><subject>Analytical, structural and metabolic biochemistry</subject><subject>Biological and medical sciences</subject><subject>Food engineering</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Glycoproteins</subject><subject>Hydrogen-Ion Concentration</subject><subject>Hydrolysis</subject><subject>Lactoglobulins - chemistry</subject><subject>Lactoglobulins - metabolism</subject><subject>Life Sciences</subject><subject>Methylation</subject><subject>Nephelometry and Turbidimetry</subject><subject>Pectins - chemistry</subject><subject>Pectins - pharmacology</subject><subject>Pepsin A - antagonists & inhibitors</subject><subject>Pepsin A - metabolism</subject><subject>Proteins</subject><subject>Static Electricity</subject><issn>0021-8561</issn><issn>1520-5118</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpt0MFuEzEUBVALgWgoLPgBNBuQWAy8Z4_Hk2VVaFIpEhUEttazx1McJuPWngHyW3wI34SrRMmGlaX7jq6sy9hLhHcIHN9vOhCVbCp6xGYoOZQSsXnMZpCPZSNrPGPPUtoAQCMVPGVnWCkhJMcZW18Po4tkRx-GVBg3_nJuKP7-KVc5C7d9MFPvh4KGtrhxWWXUTtEPt0VOv_kxhmJBaYzeFstdG0O_Sz49Z0866pN7cXjP2derj-vLZbn6tLi-vFiVVKEYSwM1N3MOpp472XWOaqsaRDLCdK0zspnzFiqyzpGShisUFUqEindgrXCVOGdv973fqdd30W8p7nQgr5cXK_2QAa8b3ijxE7N9s7d3MdxPLo1665N1fU-DC1PSDSCoGupTqY0hpei6YzOCfphbH-fO9tWhdDJb157kYd8MXh8AJUt9F2mwPp2crBBqUNmVe-fT6H4f7xR_6FoJJfX65ou-wgWuPwDqz6desklvwhSHvPN_PvgPN5Gibw</recordid><startdate>20040128</startdate><enddate>20040128</enddate><creator>Nacer S, Ahmed</creator><creator>Sanchez, Christian</creator><creator>Villaume, Christian</creator><creator>Mejean, Luc</creator><creator>Mouecoucou, Justine</creator><general>American Chemical Society</general><scope>BSCLL</scope><scope>IQODW</scope><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><scope>1XC</scope></search><sort><creationdate>20040128</creationdate><title>Interactions between β-Lactoglobulin and Pectins during in Vitro Gastric Hydrolysis</title><author>Nacer S, Ahmed ; Sanchez, Christian ; Villaume, Christian ; Mejean, Luc ; Mouecoucou, Justine</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a413t-b062b920b69e5ffea6c7811ab3bfdeb5892d04aceea75b27134151042f0cc3e43</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Analytical, structural and metabolic biochemistry</topic><topic>Biological and medical sciences</topic><topic>Food engineering</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Glycoproteins</topic><topic>Hydrogen-Ion Concentration</topic><topic>Hydrolysis</topic><topic>Lactoglobulins - chemistry</topic><topic>Lactoglobulins - metabolism</topic><topic>Life Sciences</topic><topic>Methylation</topic><topic>Nephelometry and Turbidimetry</topic><topic>Pectins - chemistry</topic><topic>Pectins - pharmacology</topic><topic>Pepsin A - antagonists & inhibitors</topic><topic>Pepsin A - metabolism</topic><topic>Proteins</topic><topic>Static Electricity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Nacer S, Ahmed</creatorcontrib><creatorcontrib>Sanchez, Christian</creatorcontrib><creatorcontrib>Villaume, Christian</creatorcontrib><creatorcontrib>Mejean, Luc</creatorcontrib><creatorcontrib>Mouecoucou, Justine</creatorcontrib><collection>Istex</collection><collection>Pascal-Francis</collection><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><collection>Hyper Article en Ligne (HAL)</collection><jtitle>Journal of agricultural and food chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Nacer S, Ahmed</au><au>Sanchez, Christian</au><au>Villaume, Christian</au><au>Mejean, Luc</au><au>Mouecoucou, Justine</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Interactions between β-Lactoglobulin and Pectins during in Vitro Gastric Hydrolysis</atitle><jtitle>Journal of agricultural and food chemistry</jtitle><addtitle>J. Agric. Food Chem</addtitle><date>2004-01-28</date><risdate>2004</risdate><volume>52</volume><issue>2</issue><spage>355</spage><epage>360</epage><pages>355-360</pages><issn>0021-8561</issn><eissn>1520-5118</eissn><coden>JAFCAU</coden><abstract>This paper deals with the influence of different levels of three pectins, low-methylated pectin (LMP), high-methylated pectin (HMP), and low-methylated and amidated pectin (LMA), on the in vitro gastric hydrolysis of β-lactoglobulin (β-lg). Proteolysis by pepsin consisted of a 2-h progressive reduction of pH. A turbidity measurement of β-lg−pectin mixtures was carried out during the proteolysis. The influence of pectins on pepsin enzymatic activity was also evaluated. β-Lg was resistant to peptic digestion. The presence of each of the three pectins at a concentration of 50 wt % increased the N release at all pH values considered, despite a significant inhibition of the pepsin enzymatic activity with the pectins. The turbidity of β-lg solutions during proteolysis was reduced by the addition of pectins, because of the formation of electrostatic complexes between this protein and pectins. The increase of N release could be a false positive result due to the difficulty of precipitating protein by trichloroacetic acid because of the formation of electrostatic complexes demonstrated by the decrease of turbidity. Keywords: β-Lactoglobulin; pectin; pepsin; N release; turbidity; pepsin enzymatic activity</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><pmid>14733521</pmid><doi>10.1021/jf034584a</doi><tpages>6</tpages></addata></record> |
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| subjects | Analytical, structural and metabolic biochemistry Biological and medical sciences Food engineering Fundamental and applied biological sciences. Psychology Glycoproteins Hydrogen-Ion Concentration Hydrolysis Lactoglobulins - chemistry Lactoglobulins - metabolism Life Sciences Methylation Nephelometry and Turbidimetry Pectins - chemistry Pectins - pharmacology Pepsin A - antagonists & inhibitors Pepsin A - metabolism Proteins Static Electricity |
| title | Interactions between β-Lactoglobulin and Pectins during in Vitro Gastric Hydrolysis |
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