Rheokinetic Analysis of Protein Films at the Air−Aqueous Subphase Interface. 2. Bovine Serum Albumin Adsorption from Sucrose Aqueous Solutions
In this paper surface dynamic properties (surface tension and surface dilational properties) of bovine serum albumin (BSA) films adsorbed on the air−aqueous sucrose solution interface are presented, as a function of adsorption time. The experiments were performed using a superficial, sinusoidal osci...
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| Veröffentlicht in: | Journal of agricultural and food chemistry 1997-08, Vol.45 (8), p.3016-3021 |
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| creator | Rodríguez Niño, M. Rosario Wilde, Peter J Clark, David C Husband, Fiona A Rodríguez Patino, Juan M |
| description | In this paper surface dynamic properties (surface tension and surface dilational properties) of bovine serum albumin (BSA) films adsorbed on the air−aqueous sucrose solution interface are presented, as a function of adsorption time. The experiments were performed using a superficial, sinusoidal oscillatory rheometer (ring trough), at constant temperature (20 °C). The surface rheological parameters (i.e. surface dilational modulus, elastic and viscous component, and loss tangent angle) and the surface tension were measured as a function of sucrose concentration (0, 0.25, 0.5, and 1 M) and on a mixture of ethanol (1.0 M) and sucrose (0.5 M) in the aqueous phase. The films displayed a viscoelastic behavior, which was practically elastic. At low sucrose concentration ( |
| doi_str_mv | 10.1021/jf970115v |
| format | Article |
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Bovine Serum Albumin Adsorption from Sucrose Aqueous Solutions</title><source>American Chemical Society Journals</source><creator>Rodríguez Niño, M. Rosario ; Wilde, Peter J ; Clark, David C ; Husband, Fiona A ; Rodríguez Patino, Juan M</creator><creatorcontrib>Rodríguez Niño, M. Rosario ; Wilde, Peter J ; Clark, David C ; Husband, Fiona A ; Rodríguez Patino, Juan M</creatorcontrib><description>In this paper surface dynamic properties (surface tension and surface dilational properties) of bovine serum albumin (BSA) films adsorbed on the air−aqueous sucrose solution interface are presented, as a function of adsorption time. The experiments were performed using a superficial, sinusoidal oscillatory rheometer (ring trough), at constant temperature (20 °C). The surface rheological parameters (i.e. surface dilational modulus, elastic and viscous component, and loss tangent angle) and the surface tension were measured as a function of sucrose concentration (0, 0.25, 0.5, and 1 M) and on a mixture of ethanol (1.0 M) and sucrose (0.5 M) in the aqueous phase. The films displayed a viscoelastic behavior, which was practically elastic. At low sucrose concentration (<0.5 M) the surface rheological properties were similar to those on water, whereas at the highest sucrose concentration (1 M) these properties decreased significantly. The transient surface dynamic properties also depend on sucrose concentration in the aqueous phase. A first-order kinetic model is a satisfactory mathematical description of the BSA adsorption and unfolding at the interface. These phenomena have been related to the protein unfolding and/or protein−protein interactions in the presence of solutes (ethanol or sucrose) in the aqueous phase. Keywords: Superficial dilational rheology; adsorption; surface properties; bovine serum albumin; air−water interface</description><identifier>ISSN: 0021-8561</identifier><identifier>EISSN: 1520-5118</identifier><identifier>DOI: 10.1021/jf970115v</identifier><identifier>CODEN: JAFCAU</identifier><language>eng</language><publisher>Washington, DC: American Chemical Society</publisher><subject>AIR WATER INTERFACE ; ALBUMINAS ; ALBUMINE ; ALBUMINS ; Animal, plant, fungal and microbial proteins, edible seaweeds and food yeasts ; Biological and medical sciences ; BLOOD SERUM ; EMULSION ; EMULSIONS ; ESPUMA ; FOAMS ; Food industries ; Fundamental and applied biological sciences. Psychology ; INTERFACE AIR EAU ; INTERFASE AIRE-AGUA ; Molecular biophysics ; MOUSSE ; PROTEINAS ; PROTEINE ; PROTEINS ; SERUM SANGUIN ; SUERO SANGUINEO ; Surface properties. Adsorption</subject><ispartof>Journal of agricultural and food chemistry, 1997-08, Vol.45 (8), p.3016-3021</ispartof><rights>Copyright © 1997 American Chemical Society</rights><rights>1997 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a346t-ec19792e57928b2619a57708615de09d5c5a3763af4640330192e2ba48e957cf3</citedby><cites>FETCH-LOGICAL-a346t-ec19792e57928b2619a57708615de09d5c5a3763af4640330192e2ba48e957cf3</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/jf970115v$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/jf970115v$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,780,784,2763,27074,27922,27923,56736,56786</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=2797133$$DView record in Pascal Francis$$Hfree_for_read</backlink></links><search><creatorcontrib>Rodríguez Niño, M. Rosario</creatorcontrib><creatorcontrib>Wilde, Peter J</creatorcontrib><creatorcontrib>Clark, David C</creatorcontrib><creatorcontrib>Husband, Fiona A</creatorcontrib><creatorcontrib>Rodríguez Patino, Juan M</creatorcontrib><title>Rheokinetic Analysis of Protein Films at the Air−Aqueous Subphase Interface. 2. Bovine Serum Albumin Adsorption from Sucrose Aqueous Solutions</title><title>Journal of agricultural and food chemistry</title><addtitle>J. Agric. Food Chem</addtitle><description>In this paper surface dynamic properties (surface tension and surface dilational properties) of bovine serum albumin (BSA) films adsorbed on the air−aqueous sucrose solution interface are presented, as a function of adsorption time. The experiments were performed using a superficial, sinusoidal oscillatory rheometer (ring trough), at constant temperature (20 °C). The surface rheological parameters (i.e. surface dilational modulus, elastic and viscous component, and loss tangent angle) and the surface tension were measured as a function of sucrose concentration (0, 0.25, 0.5, and 1 M) and on a mixture of ethanol (1.0 M) and sucrose (0.5 M) in the aqueous phase. The films displayed a viscoelastic behavior, which was practically elastic. At low sucrose concentration (<0.5 M) the surface rheological properties were similar to those on water, whereas at the highest sucrose concentration (1 M) these properties decreased significantly. The transient surface dynamic properties also depend on sucrose concentration in the aqueous phase. A first-order kinetic model is a satisfactory mathematical description of the BSA adsorption and unfolding at the interface. These phenomena have been related to the protein unfolding and/or protein−protein interactions in the presence of solutes (ethanol or sucrose) in the aqueous phase. Keywords: Superficial dilational rheology; adsorption; surface properties; bovine serum albumin; air−water interface</description><subject>AIR WATER INTERFACE</subject><subject>ALBUMINAS</subject><subject>ALBUMINE</subject><subject>ALBUMINS</subject><subject>Animal, plant, fungal and microbial proteins, edible seaweeds and food yeasts</subject><subject>Biological and medical sciences</subject><subject>BLOOD SERUM</subject><subject>EMULSION</subject><subject>EMULSIONS</subject><subject>ESPUMA</subject><subject>FOAMS</subject><subject>Food industries</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>INTERFACE AIR EAU</subject><subject>INTERFASE AIRE-AGUA</subject><subject>Molecular biophysics</subject><subject>MOUSSE</subject><subject>PROTEINAS</subject><subject>PROTEINE</subject><subject>PROTEINS</subject><subject>SERUM SANGUIN</subject><subject>SUERO SANGUINEO</subject><subject>Surface properties. Adsorption</subject><issn>0021-8561</issn><issn>1520-5118</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1997</creationdate><recordtype>article</recordtype><recordid>eNptkUFP2zAYhq0JpBXYYT9gkg_ssEOKHcdxcsyqFRBsQ2s5W19de3VJ4mAnCP4BR8RP3C_BVVBPu9iH53lff_qM0GdKppSk9GxrSkEo5Q8f0ITylCSc0uIATUiEScFz-hEdhbAlhBRckAl6-bPR7s62urcKVy3UT8EG7Ay-8a7XtsVzWzcBQ4_7jcaV9f-eX6v7Qbsh4MWw6jYQNL5se-0NKD3F6RR_dw-xDy-0Hxpc1auhiTXVOjjf9da12HjXxKzyLkb3Xa4edjScoEMDddCf3u9jdDv_sZxdJNe_zy9n1XUCLMv7RCtaijLVPB7FKs1pCVwIUuSUrzUp11xxYCJnYLI8I4wRGuV0BVmhSy6UYcfo29i7myN4bWTnbQP-SVIid6uU-1VG93R0OwgKauOhVTbsA6koBWUsasmo2dDrxz0GfydzwQSXy5uF_EX41fKqyOXP6H8ZfQNOwl8fK28XtIyvioykWeRfRw4qyK0bfPye8J_x3gDfhZjt</recordid><startdate>19970801</startdate><enddate>19970801</enddate><creator>Rodríguez Niño, M. Rosario</creator><creator>Wilde, Peter J</creator><creator>Clark, David C</creator><creator>Husband, Fiona A</creator><creator>Rodríguez Patino, Juan M</creator><general>American Chemical Society</general><scope>FBQ</scope><scope>BSCLL</scope><scope>IQODW</scope><scope>AAYXX</scope><scope>CITATION</scope></search><sort><creationdate>19970801</creationdate><title>Rheokinetic Analysis of Protein Films at the Air−Aqueous Subphase Interface. 2. Bovine Serum Albumin Adsorption from Sucrose Aqueous Solutions</title><author>Rodríguez Niño, M. Rosario ; Wilde, Peter J ; Clark, David C ; Husband, Fiona A ; Rodríguez Patino, Juan M</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a346t-ec19792e57928b2619a57708615de09d5c5a3763af4640330192e2ba48e957cf3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1997</creationdate><topic>AIR WATER INTERFACE</topic><topic>ALBUMINAS</topic><topic>ALBUMINE</topic><topic>ALBUMINS</topic><topic>Animal, plant, fungal and microbial proteins, edible seaweeds and food yeasts</topic><topic>Biological and medical sciences</topic><topic>BLOOD SERUM</topic><topic>EMULSION</topic><topic>EMULSIONS</topic><topic>ESPUMA</topic><topic>FOAMS</topic><topic>Food industries</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>INTERFACE AIR EAU</topic><topic>INTERFASE AIRE-AGUA</topic><topic>Molecular biophysics</topic><topic>MOUSSE</topic><topic>PROTEINAS</topic><topic>PROTEINE</topic><topic>PROTEINS</topic><topic>SERUM SANGUIN</topic><topic>SUERO SANGUINEO</topic><topic>Surface properties. Adsorption</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Rodríguez Niño, M. Rosario</creatorcontrib><creatorcontrib>Wilde, Peter J</creatorcontrib><creatorcontrib>Clark, David C</creatorcontrib><creatorcontrib>Husband, Fiona A</creatorcontrib><creatorcontrib>Rodríguez Patino, Juan M</creatorcontrib><collection>AGRIS</collection><collection>Istex</collection><collection>Pascal-Francis</collection><collection>CrossRef</collection><jtitle>Journal of agricultural and food chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Rodríguez Niño, M. Rosario</au><au>Wilde, Peter J</au><au>Clark, David C</au><au>Husband, Fiona A</au><au>Rodríguez Patino, Juan M</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Rheokinetic Analysis of Protein Films at the Air−Aqueous Subphase Interface. 2. Bovine Serum Albumin Adsorption from Sucrose Aqueous Solutions</atitle><jtitle>Journal of agricultural and food chemistry</jtitle><addtitle>J. Agric. Food Chem</addtitle><date>1997-08-01</date><risdate>1997</risdate><volume>45</volume><issue>8</issue><spage>3016</spage><epage>3021</epage><pages>3016-3021</pages><issn>0021-8561</issn><eissn>1520-5118</eissn><coden>JAFCAU</coden><abstract>In this paper surface dynamic properties (surface tension and surface dilational properties) of bovine serum albumin (BSA) films adsorbed on the air−aqueous sucrose solution interface are presented, as a function of adsorption time. The experiments were performed using a superficial, sinusoidal oscillatory rheometer (ring trough), at constant temperature (20 °C). The surface rheological parameters (i.e. surface dilational modulus, elastic and viscous component, and loss tangent angle) and the surface tension were measured as a function of sucrose concentration (0, 0.25, 0.5, and 1 M) and on a mixture of ethanol (1.0 M) and sucrose (0.5 M) in the aqueous phase. The films displayed a viscoelastic behavior, which was practically elastic. At low sucrose concentration (<0.5 M) the surface rheological properties were similar to those on water, whereas at the highest sucrose concentration (1 M) these properties decreased significantly. The transient surface dynamic properties also depend on sucrose concentration in the aqueous phase. A first-order kinetic model is a satisfactory mathematical description of the BSA adsorption and unfolding at the interface. These phenomena have been related to the protein unfolding and/or protein−protein interactions in the presence of solutes (ethanol or sucrose) in the aqueous phase. Keywords: Superficial dilational rheology; adsorption; surface properties; bovine serum albumin; air−water interface</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><doi>10.1021/jf970115v</doi><tpages>6</tpages></addata></record> |
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| ispartof | Journal of agricultural and food chemistry, 1997-08, Vol.45 (8), p.3016-3021 |
| issn | 0021-8561 1520-5118 |
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| source | American Chemical Society Journals |
| subjects | AIR WATER INTERFACE ALBUMINAS ALBUMINE ALBUMINS Animal, plant, fungal and microbial proteins, edible seaweeds and food yeasts Biological and medical sciences BLOOD SERUM EMULSION EMULSIONS ESPUMA FOAMS Food industries Fundamental and applied biological sciences. Psychology INTERFACE AIR EAU INTERFASE AIRE-AGUA Molecular biophysics MOUSSE PROTEINAS PROTEINE PROTEINS SERUM SANGUIN SUERO SANGUINEO Surface properties. Adsorption |
| title | Rheokinetic Analysis of Protein Films at the Air−Aqueous Subphase Interface. 2. Bovine Serum Albumin Adsorption from Sucrose Aqueous Solutions |
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