Structural Characterization of Amaranth Protein Gels
: Gelation capacity of a native amaranth protein isolate was studied. Structural properties of gels prepared at different protein concentration and heating conditions were analyzed. Proteins present in amaranth isolates obtained by water extraction at pH 9.0 and subsequent isoelectric precipitation...
Ausführliche Beschreibung
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| Autor*in: |
Avanza, Maria V. [verfasserIn] Puppo, Maria C. [verfasserIn] Añón, Maria C. [verfasserIn] |
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| Format: |
E-Artikel |
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| Erschienen: |
Oxford, UK: Blackwell Publishing Ltd ; 2005 |
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Online-Ressource |
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| Reproduktion: |
2006 ; Blackwell Publishing Journal Backfiles 1879-2005 |
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| Übergeordnetes Werk: |
In: Journal of food science - Chicago, Ill. : Inst., 1990, 70(2005), 3, Seite 0 |
| Übergeordnetes Werk: |
volume:70 ; year:2005 ; number:3 ; pages:0 |
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| DOI / URN: |
10.1111/j.1365-2621.2005.tb07139.x |
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| 520 | |a : Gelation capacity of a native amaranth protein isolate was studied. Structural properties of gels prepared at different protein concentration and heating conditions were analyzed. Proteins present in amaranth isolates obtained by water extraction at pH 9.0 and subsequent isoelectric precipitation are able to form gels of yellowish appearance. Gel color intensity increased while luminosity decreased with increasing protein concentrations. High protein concentration allowed the formation of matrices with high water-holding capacity. In addition, increasing the heating temperature resulted in gels of high luminosity and low water-holding capacity. The increase of protein concentration (10% to 20% w/v) as well as the increase of heating temperature (70°C to 95°C) and heating time (10 to 30 min) resulted in the formation of a more ordered matrix with smaller pores, mainly stabilized by disulfide bonds and, at a lower extent, by noncovalent interactions (specially hydrogen bonds and hydrophobic interactions). Both amaranth globulin (11S globulin and P globulin) participated in gel structure via high-molecular-weight aggregates (>100 kD). Gel structure was stabilized via noncovalent bonds by monomer species of 42 kD and those of molecular mass lower than 20 kD localized in the interstitial spaces of gel matrix. | ||
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10.1111/j.1365-2621.2005.tb07139.x doi (DE-627)NLEJ243201958 DE-627 ger DE-627 rakwb Avanza, Maria V. verfasserin aut Structural Characterization of Amaranth Protein Gels Oxford, UK Blackwell Publishing Ltd 2005 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier : Gelation capacity of a native amaranth protein isolate was studied. Structural properties of gels prepared at different protein concentration and heating conditions were analyzed. Proteins present in amaranth isolates obtained by water extraction at pH 9.0 and subsequent isoelectric precipitation are able to form gels of yellowish appearance. Gel color intensity increased while luminosity decreased with increasing protein concentrations. High protein concentration allowed the formation of matrices with high water-holding capacity. In addition, increasing the heating temperature resulted in gels of high luminosity and low water-holding capacity. The increase of protein concentration (10% to 20% w/v) as well as the increase of heating temperature (70°C to 95°C) and heating time (10 to 30 min) resulted in the formation of a more ordered matrix with smaller pores, mainly stabilized by disulfide bonds and, at a lower extent, by noncovalent interactions (specially hydrogen bonds and hydrophobic interactions). Both amaranth globulin (11S globulin and P globulin) participated in gel structure via high-molecular-weight aggregates (>100 kD). Gel structure was stabilized via noncovalent bonds by monomer species of 42 kD and those of molecular mass lower than 20 kD localized in the interstitial spaces of gel matrix. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| amaranth proteins Puppo, Maria C. verfasserin aut Añón, Maria C. verfasserin aut In Journal of food science Chicago, Ill. : Inst., 1990 70(2005), 3, Seite 0 (DE-627)NLEJ243926316 (DE-600)2006705-7 1750-3841 nnns volume:70 year:2005 number:3 pages:0 http://dx.doi.org/10.1111/j.1365-2621.2005.tb07139.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 70 2005 3 0 |
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10.1111/j.1365-2621.2005.tb07139.x doi (DE-627)NLEJ243201958 DE-627 ger DE-627 rakwb Avanza, Maria V. verfasserin aut Structural Characterization of Amaranth Protein Gels Oxford, UK Blackwell Publishing Ltd 2005 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier : Gelation capacity of a native amaranth protein isolate was studied. Structural properties of gels prepared at different protein concentration and heating conditions were analyzed. Proteins present in amaranth isolates obtained by water extraction at pH 9.0 and subsequent isoelectric precipitation are able to form gels of yellowish appearance. Gel color intensity increased while luminosity decreased with increasing protein concentrations. High protein concentration allowed the formation of matrices with high water-holding capacity. In addition, increasing the heating temperature resulted in gels of high luminosity and low water-holding capacity. The increase of protein concentration (10% to 20% w/v) as well as the increase of heating temperature (70°C to 95°C) and heating time (10 to 30 min) resulted in the formation of a more ordered matrix with smaller pores, mainly stabilized by disulfide bonds and, at a lower extent, by noncovalent interactions (specially hydrogen bonds and hydrophobic interactions). Both amaranth globulin (11S globulin and P globulin) participated in gel structure via high-molecular-weight aggregates (>100 kD). Gel structure was stabilized via noncovalent bonds by monomer species of 42 kD and those of molecular mass lower than 20 kD localized in the interstitial spaces of gel matrix. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| amaranth proteins Puppo, Maria C. verfasserin aut Añón, Maria C. verfasserin aut In Journal of food science Chicago, Ill. : Inst., 1990 70(2005), 3, Seite 0 (DE-627)NLEJ243926316 (DE-600)2006705-7 1750-3841 nnns volume:70 year:2005 number:3 pages:0 http://dx.doi.org/10.1111/j.1365-2621.2005.tb07139.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 70 2005 3 0 |
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10.1111/j.1365-2621.2005.tb07139.x doi (DE-627)NLEJ243201958 DE-627 ger DE-627 rakwb Avanza, Maria V. verfasserin aut Structural Characterization of Amaranth Protein Gels Oxford, UK Blackwell Publishing Ltd 2005 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier : Gelation capacity of a native amaranth protein isolate was studied. Structural properties of gels prepared at different protein concentration and heating conditions were analyzed. Proteins present in amaranth isolates obtained by water extraction at pH 9.0 and subsequent isoelectric precipitation are able to form gels of yellowish appearance. Gel color intensity increased while luminosity decreased with increasing protein concentrations. High protein concentration allowed the formation of matrices with high water-holding capacity. In addition, increasing the heating temperature resulted in gels of high luminosity and low water-holding capacity. The increase of protein concentration (10% to 20% w/v) as well as the increase of heating temperature (70°C to 95°C) and heating time (10 to 30 min) resulted in the formation of a more ordered matrix with smaller pores, mainly stabilized by disulfide bonds and, at a lower extent, by noncovalent interactions (specially hydrogen bonds and hydrophobic interactions). Both amaranth globulin (11S globulin and P globulin) participated in gel structure via high-molecular-weight aggregates (>100 kD). Gel structure was stabilized via noncovalent bonds by monomer species of 42 kD and those of molecular mass lower than 20 kD localized in the interstitial spaces of gel matrix. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| amaranth proteins Puppo, Maria C. verfasserin aut Añón, Maria C. verfasserin aut In Journal of food science Chicago, Ill. : Inst., 1990 70(2005), 3, Seite 0 (DE-627)NLEJ243926316 (DE-600)2006705-7 1750-3841 nnns volume:70 year:2005 number:3 pages:0 http://dx.doi.org/10.1111/j.1365-2621.2005.tb07139.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 70 2005 3 0 |
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10.1111/j.1365-2621.2005.tb07139.x doi (DE-627)NLEJ243201958 DE-627 ger DE-627 rakwb Avanza, Maria V. verfasserin aut Structural Characterization of Amaranth Protein Gels Oxford, UK Blackwell Publishing Ltd 2005 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier : Gelation capacity of a native amaranth protein isolate was studied. Structural properties of gels prepared at different protein concentration and heating conditions were analyzed. Proteins present in amaranth isolates obtained by water extraction at pH 9.0 and subsequent isoelectric precipitation are able to form gels of yellowish appearance. Gel color intensity increased while luminosity decreased with increasing protein concentrations. High protein concentration allowed the formation of matrices with high water-holding capacity. In addition, increasing the heating temperature resulted in gels of high luminosity and low water-holding capacity. The increase of protein concentration (10% to 20% w/v) as well as the increase of heating temperature (70°C to 95°C) and heating time (10 to 30 min) resulted in the formation of a more ordered matrix with smaller pores, mainly stabilized by disulfide bonds and, at a lower extent, by noncovalent interactions (specially hydrogen bonds and hydrophobic interactions). Both amaranth globulin (11S globulin and P globulin) participated in gel structure via high-molecular-weight aggregates (>100 kD). Gel structure was stabilized via noncovalent bonds by monomer species of 42 kD and those of molecular mass lower than 20 kD localized in the interstitial spaces of gel matrix. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| amaranth proteins Puppo, Maria C. verfasserin aut Añón, Maria C. verfasserin aut In Journal of food science Chicago, Ill. : Inst., 1990 70(2005), 3, Seite 0 (DE-627)NLEJ243926316 (DE-600)2006705-7 1750-3841 nnns volume:70 year:2005 number:3 pages:0 http://dx.doi.org/10.1111/j.1365-2621.2005.tb07139.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 70 2005 3 0 |
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10.1111/j.1365-2621.2005.tb07139.x doi (DE-627)NLEJ243201958 DE-627 ger DE-627 rakwb Avanza, Maria V. verfasserin aut Structural Characterization of Amaranth Protein Gels Oxford, UK Blackwell Publishing Ltd 2005 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier : Gelation capacity of a native amaranth protein isolate was studied. Structural properties of gels prepared at different protein concentration and heating conditions were analyzed. Proteins present in amaranth isolates obtained by water extraction at pH 9.0 and subsequent isoelectric precipitation are able to form gels of yellowish appearance. Gel color intensity increased while luminosity decreased with increasing protein concentrations. High protein concentration allowed the formation of matrices with high water-holding capacity. In addition, increasing the heating temperature resulted in gels of high luminosity and low water-holding capacity. The increase of protein concentration (10% to 20% w/v) as well as the increase of heating temperature (70°C to 95°C) and heating time (10 to 30 min) resulted in the formation of a more ordered matrix with smaller pores, mainly stabilized by disulfide bonds and, at a lower extent, by noncovalent interactions (specially hydrogen bonds and hydrophobic interactions). Both amaranth globulin (11S globulin and P globulin) participated in gel structure via high-molecular-weight aggregates (>100 kD). Gel structure was stabilized via noncovalent bonds by monomer species of 42 kD and those of molecular mass lower than 20 kD localized in the interstitial spaces of gel matrix. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| amaranth proteins Puppo, Maria C. verfasserin aut Añón, Maria C. verfasserin aut In Journal of food science Chicago, Ill. : Inst., 1990 70(2005), 3, Seite 0 (DE-627)NLEJ243926316 (DE-600)2006705-7 1750-3841 nnns volume:70 year:2005 number:3 pages:0 http://dx.doi.org/10.1111/j.1365-2621.2005.tb07139.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 70 2005 3 0 |
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: Gelation capacity of a native amaranth protein isolate was studied. Structural properties of gels prepared at different protein concentration and heating conditions were analyzed. Proteins present in amaranth isolates obtained by water extraction at pH 9.0 and subsequent isoelectric precipitation are able to form gels of yellowish appearance. Gel color intensity increased while luminosity decreased with increasing protein concentrations. High protein concentration allowed the formation of matrices with high water-holding capacity. In addition, increasing the heating temperature resulted in gels of high luminosity and low water-holding capacity. The increase of protein concentration (10% to 20% w/v) as well as the increase of heating temperature (70°C to 95°C) and heating time (10 to 30 min) resulted in the formation of a more ordered matrix with smaller pores, mainly stabilized by disulfide bonds and, at a lower extent, by noncovalent interactions (specially hydrogen bonds and hydrophobic interactions). Both amaranth globulin (11S globulin and P globulin) participated in gel structure via high-molecular-weight aggregates (>100 kD). Gel structure was stabilized via noncovalent bonds by monomer species of 42 kD and those of molecular mass lower than 20 kD localized in the interstitial spaces of gel matrix. |
| abstractGer |
: Gelation capacity of a native amaranth protein isolate was studied. Structural properties of gels prepared at different protein concentration and heating conditions were analyzed. Proteins present in amaranth isolates obtained by water extraction at pH 9.0 and subsequent isoelectric precipitation are able to form gels of yellowish appearance. Gel color intensity increased while luminosity decreased with increasing protein concentrations. High protein concentration allowed the formation of matrices with high water-holding capacity. In addition, increasing the heating temperature resulted in gels of high luminosity and low water-holding capacity. The increase of protein concentration (10% to 20% w/v) as well as the increase of heating temperature (70°C to 95°C) and heating time (10 to 30 min) resulted in the formation of a more ordered matrix with smaller pores, mainly stabilized by disulfide bonds and, at a lower extent, by noncovalent interactions (specially hydrogen bonds and hydrophobic interactions). Both amaranth globulin (11S globulin and P globulin) participated in gel structure via high-molecular-weight aggregates (>100 kD). Gel structure was stabilized via noncovalent bonds by monomer species of 42 kD and those of molecular mass lower than 20 kD localized in the interstitial spaces of gel matrix. |
| abstract_unstemmed |
: Gelation capacity of a native amaranth protein isolate was studied. Structural properties of gels prepared at different protein concentration and heating conditions were analyzed. Proteins present in amaranth isolates obtained by water extraction at pH 9.0 and subsequent isoelectric precipitation are able to form gels of yellowish appearance. Gel color intensity increased while luminosity decreased with increasing protein concentrations. High protein concentration allowed the formation of matrices with high water-holding capacity. In addition, increasing the heating temperature resulted in gels of high luminosity and low water-holding capacity. The increase of protein concentration (10% to 20% w/v) as well as the increase of heating temperature (70°C to 95°C) and heating time (10 to 30 min) resulted in the formation of a more ordered matrix with smaller pores, mainly stabilized by disulfide bonds and, at a lower extent, by noncovalent interactions (specially hydrogen bonds and hydrophobic interactions). Both amaranth globulin (11S globulin and P globulin) participated in gel structure via high-molecular-weight aggregates (>100 kD). Gel structure was stabilized via noncovalent bonds by monomer species of 42 kD and those of molecular mass lower than 20 kD localized in the interstitial spaces of gel matrix. |
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<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">NLEJ243201958</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210707173922.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">120427s2005 xx |||||o 00| ||und c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1111/j.1365-2621.2005.tb07139.x</subfield><subfield code="2">doi</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ243201958</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="100" ind1="1" ind2=" "><subfield code="a">Avanza, Maria V.</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Structural Characterization of Amaranth Protein Gels</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="a">Oxford, UK</subfield><subfield code="b">Blackwell Publishing Ltd</subfield><subfield code="c">2005</subfield></datafield><datafield tag="300" ind1=" " ind2=" "><subfield code="a">Online-Ressource</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zzz</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">z</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zu</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">: Gelation capacity of a native amaranth protein isolate was studied. Structural properties of gels prepared at different protein concentration and heating conditions were analyzed. Proteins present in amaranth isolates obtained by water extraction at pH 9.0 and subsequent isoelectric precipitation are able to form gels of yellowish appearance. Gel color intensity increased while luminosity decreased with increasing protein concentrations. High protein concentration allowed the formation of matrices with high water-holding capacity. In addition, increasing the heating temperature resulted in gels of high luminosity and low water-holding capacity. The increase of protein concentration (10% to 20% w/v) as well as the increase of heating temperature (70°C to 95°C) and heating time (10 to 30 min) resulted in the formation of a more ordered matrix with smaller pores, mainly stabilized by disulfide bonds and, at a lower extent, by noncovalent interactions (specially hydrogen bonds and hydrophobic interactions). Both amaranth globulin (11S globulin and P globulin) participated in gel structure via high-molecular-weight aggregates (>100 kD). Gel structure was stabilized via noncovalent bonds by monomer species of 42 kD and those of molecular mass lower than 20 kD localized in the interstitial spaces of gel matrix.</subfield></datafield><datafield tag="533" ind1=" " ind2=" "><subfield code="d">2006</subfield><subfield code="f">Blackwell Publishing Journal Backfiles 1879-2005</subfield><subfield code="7">|2006||||||||||</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">amaranth proteins</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Puppo, Maria C.</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Añón, Maria C.</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">In</subfield><subfield code="t">Journal of food science</subfield><subfield code="d">Chicago, Ill. : Inst., 1990</subfield><subfield code="g">70(2005), 3, Seite 0</subfield><subfield code="w">(DE-627)NLEJ243926316</subfield><subfield code="w">(DE-600)2006705-7</subfield><subfield code="x">1750-3841</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:70</subfield><subfield code="g">year:2005</subfield><subfield code="g">number:3</subfield><subfield code="g">pages:0</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://dx.doi.org/10.1111/j.1365-2621.2005.tb07139.x</subfield><subfield code="q">text/html</subfield><subfield code="x">Verlag</subfield><subfield code="z">Deutschlandweit zugänglich</subfield><subfield code="3">Volltext</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_U</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">ZDB-1-DJB</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_NL_ARTICLE</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">70</subfield><subfield code="j">2005</subfield><subfield code="e">3</subfield><subfield code="h">0</subfield></datafield></record></collection>
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7.399081 |