Chromatographic Fractionation of α-Lactalbumin and β-Lactoglobulin with Polystyrenic Strongly Basic Anion Exchange Resins
Adsorption characteristics of α-lactalbumin (α-La) and β-lactoglobulin (β-Lg) onto 11 strongly basic anion exchange resins were evaluated by contacting the resins columnwise with sweet whey (pH 6.5), from which lipoproteins and caseinomacropeptides had been largely removed. The resins were based on...
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| Veröffentlicht in: | Food science & technology 1996, Vol.29 (4), p.340-343 |
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| creator | Outinen, M. Tossavainen, O. Syväoja, E.-L. |
| description | Adsorption characteristics of α-lactalbumin (α-La) and β-lactoglobulin (β-Lg) onto 11 strongly basic anion exchange resins were evaluated by contacting the resins columnwise with sweet whey (pH 6.5), from which lipoproteins and caseinomacropeptides had been largely removed. The resins were based on a polystyrene–divinylbenzene copolymer matrix. Two of the resins were gel-type, the rest were macroporous. The adsorption capacity of the gel-type resins was inferior compared to macroporous resins, of which two had a β-Lg adsorption capacity large enough to enable protein fractionation. Significant fractionation was obtained only with Diaion HPA 75 (α-La:β-Lg
=
1.9, when 9 and 82% of α-La and β-Lg were adsorbed, respectively). Optimum fractionation conditions (pH 6–7, β-Lg load of 16–20 mg/cm
3resin, degree of demineralization 0–50) were determined by batch experiments with Diaion HPA 75. Within these conditions, α-La:β-Lg (2.0-2.2) with 75–80% recovery of α-La was obtained. |
| doi_str_mv | 10.1006/fstl.1996.0051 |
| format | Article |
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=
1.9, when 9 and 82% of α-La and β-Lg were adsorbed, respectively). Optimum fractionation conditions (pH 6–7, β-Lg load of 16–20 mg/cm
3resin, degree of demineralization 0–50) were determined by batch experiments with Diaion HPA 75. Within these conditions, α-La:β-Lg (2.0-2.2) with 75–80% recovery of α-La was obtained.</description><identifier>ISSN: 0023-6438</identifier><identifier>EISSN: 1096-1127</identifier><identifier>DOI: 10.1006/fstl.1996.0051</identifier><identifier>CODEN: LBWTAP</identifier><language>eng</language><publisher>Oxford: Elsevier Ltd</publisher><subject>Animal, plant, fungal and microbial proteins, edible seaweeds and food yeasts ; anion exchange resins ; bases ; beta-lactoglobulin ; Biological and medical sciences ; chromatography ; Food industries ; fractionation ; Fundamental and applied biological sciences. Psychology ; gels ; lactalbumin ; whey protein</subject><ispartof>Food science & technology, 1996, Vol.29 (4), p.340-343</ispartof><rights>1996</rights><rights>1996 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c339t-8da39260a8febb728796053c216d888eefae4ef1ae92170813ee7cef5934d0763</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0023643896900511$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,4010,27900,27901,27902,65306</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=3126684$$DView record in Pascal Francis$$Hfree_for_read</backlink></links><search><creatorcontrib>Outinen, M.</creatorcontrib><creatorcontrib>Tossavainen, O.</creatorcontrib><creatorcontrib>Syväoja, E.-L.</creatorcontrib><title>Chromatographic Fractionation of α-Lactalbumin and β-Lactoglobulin with Polystyrenic Strongly Basic Anion Exchange Resins</title><title>Food science & technology</title><description>Adsorption characteristics of α-lactalbumin (α-La) and β-lactoglobulin (β-Lg) onto 11 strongly basic anion exchange resins were evaluated by contacting the resins columnwise with sweet whey (pH 6.5), from which lipoproteins and caseinomacropeptides had been largely removed. The resins were based on a polystyrene–divinylbenzene copolymer matrix. Two of the resins were gel-type, the rest were macroporous. The adsorption capacity of the gel-type resins was inferior compared to macroporous resins, of which two had a β-Lg adsorption capacity large enough to enable protein fractionation. Significant fractionation was obtained only with Diaion HPA 75 (α-La:β-Lg
=
1.9, when 9 and 82% of α-La and β-Lg were adsorbed, respectively). Optimum fractionation conditions (pH 6–7, β-Lg load of 16–20 mg/cm
3resin, degree of demineralization 0–50) were determined by batch experiments with Diaion HPA 75. Within these conditions, α-La:β-Lg (2.0-2.2) with 75–80% recovery of α-La was obtained.</description><subject>Animal, plant, fungal and microbial proteins, edible seaweeds and food yeasts</subject><subject>anion exchange resins</subject><subject>bases</subject><subject>beta-lactoglobulin</subject><subject>Biological and medical sciences</subject><subject>chromatography</subject><subject>Food industries</subject><subject>fractionation</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>gels</subject><subject>lactalbumin</subject><subject>whey protein</subject><issn>0023-6438</issn><issn>1096-1127</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1996</creationdate><recordtype>article</recordtype><recordid>eNp1kEtvGyEUhVHVSnXTbLvtLLIdl8eYgWVq5VHJUqo81uiauYypxmDBpImVX5X-kPymMnXUXVhcxNF3jriHkC-Mzhml8pvL4zBnWss5pQv2jswY1bJmjLfvyYxSLmrZCPWRfMr5Fy2n4WpGnpabFLcwxj7BbuNtdZ7Ajj4GmEYVXfXyXK-KBMP6futDBaGrXv78k2I_xPX9UMQHP26qn3HY53GfMJSYmzHF0A_76jvk8jwNU9rZo91A6LG6xuxD_kw-OBgyHr_eR-Tu_Ox2eVmvri5-LE9XtRVCj7XqQGguKSiH63XLVaslXQjLmeyUUogOsEHHADVnLVVMILYW3UKLpqOtFEdkfsi1Keac0Jld8ltIe8OomaozU3Vmqs5M1RXDycGwg2xhcAmC9fm_SzAupWoK9vWAOYgG-lSQuxtOmaBswXSBCqEOBJb1fntMJluPwWLnE9rRdNG_9Ye_7lqPeA</recordid><startdate>1996</startdate><enddate>1996</enddate><creator>Outinen, M.</creator><creator>Tossavainen, O.</creator><creator>Syväoja, E.-L.</creator><general>Elsevier Ltd</general><general>Elsevier</general><scope>FBQ</scope><scope>IQODW</scope><scope>AAYXX</scope><scope>CITATION</scope></search><sort><creationdate>1996</creationdate><title>Chromatographic Fractionation of α-Lactalbumin and β-Lactoglobulin with Polystyrenic Strongly Basic Anion Exchange Resins</title><author>Outinen, M. ; Tossavainen, O. ; Syväoja, E.-L.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c339t-8da39260a8febb728796053c216d888eefae4ef1ae92170813ee7cef5934d0763</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1996</creationdate><topic>Animal, plant, fungal and microbial proteins, edible seaweeds and food yeasts</topic><topic>anion exchange resins</topic><topic>bases</topic><topic>beta-lactoglobulin</topic><topic>Biological and medical sciences</topic><topic>chromatography</topic><topic>Food industries</topic><topic>fractionation</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>gels</topic><topic>lactalbumin</topic><topic>whey protein</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Outinen, M.</creatorcontrib><creatorcontrib>Tossavainen, O.</creatorcontrib><creatorcontrib>Syväoja, E.-L.</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>CrossRef</collection><jtitle>Food science & technology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Outinen, M.</au><au>Tossavainen, O.</au><au>Syväoja, E.-L.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Chromatographic Fractionation of α-Lactalbumin and β-Lactoglobulin with Polystyrenic Strongly Basic Anion Exchange Resins</atitle><jtitle>Food science & technology</jtitle><date>1996</date><risdate>1996</risdate><volume>29</volume><issue>4</issue><spage>340</spage><epage>343</epage><pages>340-343</pages><issn>0023-6438</issn><eissn>1096-1127</eissn><coden>LBWTAP</coden><abstract>Adsorption characteristics of α-lactalbumin (α-La) and β-lactoglobulin (β-Lg) onto 11 strongly basic anion exchange resins were evaluated by contacting the resins columnwise with sweet whey (pH 6.5), from which lipoproteins and caseinomacropeptides had been largely removed. The resins were based on a polystyrene–divinylbenzene copolymer matrix. Two of the resins were gel-type, the rest were macroporous. The adsorption capacity of the gel-type resins was inferior compared to macroporous resins, of which two had a β-Lg adsorption capacity large enough to enable protein fractionation. Significant fractionation was obtained only with Diaion HPA 75 (α-La:β-Lg
=
1.9, when 9 and 82% of α-La and β-Lg were adsorbed, respectively). Optimum fractionation conditions (pH 6–7, β-Lg load of 16–20 mg/cm
3resin, degree of demineralization 0–50) were determined by batch experiments with Diaion HPA 75. Within these conditions, α-La:β-Lg (2.0-2.2) with 75–80% recovery of α-La was obtained.</abstract><cop>Oxford</cop><pub>Elsevier Ltd</pub><doi>10.1006/fstl.1996.0051</doi><tpages>4</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0023-6438 |
| ispartof | Food science & technology, 1996, Vol.29 (4), p.340-343 |
| issn | 0023-6438 1096-1127 |
| language | eng |
| recordid | cdi_crossref_primary_10_1006_fstl_1996_0051 |
| source | Elsevier ScienceDirect Journals |
| subjects | Animal, plant, fungal and microbial proteins, edible seaweeds and food yeasts anion exchange resins bases beta-lactoglobulin Biological and medical sciences chromatography Food industries fractionation Fundamental and applied biological sciences. Psychology gels lactalbumin whey protein |
| title | Chromatographic Fractionation of α-Lactalbumin and β-Lactoglobulin with Polystyrenic Strongly Basic Anion Exchange Resins |
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