Continuous Hydrolysis of Goat Whey in an Ultrafiltration Reactor: Generation of Alpha-Lactorphin
Bovine whey hydrolysate has been developed and applied to areas such as nutrition, culture media, and isolation of bioactive peptides. In order to produce such a type of hydrolysate, it is possible to use goat whey which constitutes also a food processing by-product. Enzymatic hydrolysis of goat whe...
Ausführliche Beschreibung
Autor*in: |
Bordenave, S. [verfasserIn] Sannier, F. [verfasserIn] Piot, J. M. [verfasserIn] Ricart, G. [verfasserIn] |
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Format: |
E-Artikel |
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Sprache: |
Englisch |
Erschienen: |
2011 |
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Übergeordnetes Werk: |
Enthalten in: Preparative biochemistry & biotechnology - Philadelphia, PA : Taylor & Francis, 1996, 29(1999), 2, Seite 189-202 |
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Übergeordnetes Werk: |
number:2 ; volume:29 ; year:1999 ; pages:189-202 |
Links: |
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DOI / URN: |
10.1080/10826069908544890 |
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10.1080/10826069908544890 doi (DE-627)NLEJ253600936 (TFO)791189505 DE-627 ger DE-627 rda eng Bordenave, S. verfasserin aut Continuous Hydrolysis of Goat Whey in an Ultrafiltration Reactor: Generation of Alpha-Lactorphin 2011 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Bovine whey hydrolysate has been developed and applied to areas such as nutrition, culture media, and isolation of bioactive peptides. In order to produce such a type of hydrolysate, it is possible to use goat whey which constitutes also a food processing by-product. Enzymatic hydrolysis of goat whey by pepsin was carried out in a continuous ultrafiltration reactor. The permeate contained peptide hydrolysate that was resolved by RP-HPLC. Second order derivative spectroscopy, amino acid analysis, and mass spectrometry revealed the presence of a biologically active peptide called alpha-lactorphin. This constitutes preliminary information about goat whey enzymatic degradation for future applications. Sannier, F. verfasserin aut Piot, J. M. verfasserin aut Ricart, G. verfasserin aut Enthalten in Preparative biochemistry & biotechnology Philadelphia, PA : Taylor & Francis, 1996 29(1999), 2, Seite 189-202 Online-Ressource (DE-627)NLEJ253593913 (DE-600)2057441-1 (DE-576)263254100 1532-2297 nnns number:2 volume:29 year:1999 pages:189-202 https://www.tib.eu/de/suchen/id/tandf%3Adcc33564e783b14b1bd6f55745c4ba8ae057d4b3 Digitalisierung Deutschlandweit zugänglich ZDB-1-TFO GBV_NL_ARTICLE AR 2 29 1999 189-202 |
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10.1080/10826069908544890 doi (DE-627)NLEJ253600936 (TFO)791189505 DE-627 ger DE-627 rda eng Bordenave, S. verfasserin aut Continuous Hydrolysis of Goat Whey in an Ultrafiltration Reactor: Generation of Alpha-Lactorphin 2011 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Bovine whey hydrolysate has been developed and applied to areas such as nutrition, culture media, and isolation of bioactive peptides. In order to produce such a type of hydrolysate, it is possible to use goat whey which constitutes also a food processing by-product. Enzymatic hydrolysis of goat whey by pepsin was carried out in a continuous ultrafiltration reactor. The permeate contained peptide hydrolysate that was resolved by RP-HPLC. Second order derivative spectroscopy, amino acid analysis, and mass spectrometry revealed the presence of a biologically active peptide called alpha-lactorphin. This constitutes preliminary information about goat whey enzymatic degradation for future applications. Sannier, F. verfasserin aut Piot, J. M. verfasserin aut Ricart, G. verfasserin aut Enthalten in Preparative biochemistry & biotechnology Philadelphia, PA : Taylor & Francis, 1996 29(1999), 2, Seite 189-202 Online-Ressource (DE-627)NLEJ253593913 (DE-600)2057441-1 (DE-576)263254100 1532-2297 nnns number:2 volume:29 year:1999 pages:189-202 https://www.tib.eu/de/suchen/id/tandf%3Adcc33564e783b14b1bd6f55745c4ba8ae057d4b3 Digitalisierung Deutschlandweit zugänglich ZDB-1-TFO GBV_NL_ARTICLE AR 2 29 1999 189-202 |
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10.1080/10826069908544890 doi (DE-627)NLEJ253600936 (TFO)791189505 DE-627 ger DE-627 rda eng Bordenave, S. verfasserin aut Continuous Hydrolysis of Goat Whey in an Ultrafiltration Reactor: Generation of Alpha-Lactorphin 2011 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Bovine whey hydrolysate has been developed and applied to areas such as nutrition, culture media, and isolation of bioactive peptides. In order to produce such a type of hydrolysate, it is possible to use goat whey which constitutes also a food processing by-product. Enzymatic hydrolysis of goat whey by pepsin was carried out in a continuous ultrafiltration reactor. The permeate contained peptide hydrolysate that was resolved by RP-HPLC. Second order derivative spectroscopy, amino acid analysis, and mass spectrometry revealed the presence of a biologically active peptide called alpha-lactorphin. This constitutes preliminary information about goat whey enzymatic degradation for future applications. Sannier, F. verfasserin aut Piot, J. M. verfasserin aut Ricart, G. verfasserin aut Enthalten in Preparative biochemistry & biotechnology Philadelphia, PA : Taylor & Francis, 1996 29(1999), 2, Seite 189-202 Online-Ressource (DE-627)NLEJ253593913 (DE-600)2057441-1 (DE-576)263254100 1532-2297 nnns number:2 volume:29 year:1999 pages:189-202 https://www.tib.eu/de/suchen/id/tandf%3Adcc33564e783b14b1bd6f55745c4ba8ae057d4b3 Digitalisierung Deutschlandweit zugänglich ZDB-1-TFO GBV_NL_ARTICLE AR 2 29 1999 189-202 |
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10.1080/10826069908544890 doi (DE-627)NLEJ253600936 (TFO)791189505 DE-627 ger DE-627 rda eng Bordenave, S. verfasserin aut Continuous Hydrolysis of Goat Whey in an Ultrafiltration Reactor: Generation of Alpha-Lactorphin 2011 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Bovine whey hydrolysate has been developed and applied to areas such as nutrition, culture media, and isolation of bioactive peptides. In order to produce such a type of hydrolysate, it is possible to use goat whey which constitutes also a food processing by-product. Enzymatic hydrolysis of goat whey by pepsin was carried out in a continuous ultrafiltration reactor. The permeate contained peptide hydrolysate that was resolved by RP-HPLC. Second order derivative spectroscopy, amino acid analysis, and mass spectrometry revealed the presence of a biologically active peptide called alpha-lactorphin. This constitutes preliminary information about goat whey enzymatic degradation for future applications. Sannier, F. verfasserin aut Piot, J. M. verfasserin aut Ricart, G. verfasserin aut Enthalten in Preparative biochemistry & biotechnology Philadelphia, PA : Taylor & Francis, 1996 29(1999), 2, Seite 189-202 Online-Ressource (DE-627)NLEJ253593913 (DE-600)2057441-1 (DE-576)263254100 1532-2297 nnns number:2 volume:29 year:1999 pages:189-202 https://www.tib.eu/de/suchen/id/tandf%3Adcc33564e783b14b1bd6f55745c4ba8ae057d4b3 Digitalisierung Deutschlandweit zugänglich ZDB-1-TFO GBV_NL_ARTICLE AR 2 29 1999 189-202 |
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Continuous Hydrolysis of Goat Whey in an Ultrafiltration Reactor: Generation of Alpha-Lactorphin |
abstract |
Bovine whey hydrolysate has been developed and applied to areas such as nutrition, culture media, and isolation of bioactive peptides. In order to produce such a type of hydrolysate, it is possible to use goat whey which constitutes also a food processing by-product. Enzymatic hydrolysis of goat whey by pepsin was carried out in a continuous ultrafiltration reactor. The permeate contained peptide hydrolysate that was resolved by RP-HPLC. Second order derivative spectroscopy, amino acid analysis, and mass spectrometry revealed the presence of a biologically active peptide called alpha-lactorphin. This constitutes preliminary information about goat whey enzymatic degradation for future applications. |
abstractGer |
Bovine whey hydrolysate has been developed and applied to areas such as nutrition, culture media, and isolation of bioactive peptides. In order to produce such a type of hydrolysate, it is possible to use goat whey which constitutes also a food processing by-product. Enzymatic hydrolysis of goat whey by pepsin was carried out in a continuous ultrafiltration reactor. The permeate contained peptide hydrolysate that was resolved by RP-HPLC. Second order derivative spectroscopy, amino acid analysis, and mass spectrometry revealed the presence of a biologically active peptide called alpha-lactorphin. This constitutes preliminary information about goat whey enzymatic degradation for future applications. |
abstract_unstemmed |
Bovine whey hydrolysate has been developed and applied to areas such as nutrition, culture media, and isolation of bioactive peptides. In order to produce such a type of hydrolysate, it is possible to use goat whey which constitutes also a food processing by-product. Enzymatic hydrolysis of goat whey by pepsin was carried out in a continuous ultrafiltration reactor. The permeate contained peptide hydrolysate that was resolved by RP-HPLC. Second order derivative spectroscopy, amino acid analysis, and mass spectrometry revealed the presence of a biologically active peptide called alpha-lactorphin. This constitutes preliminary information about goat whey enzymatic degradation for future applications. |
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<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000naa a22002652 4500</leader><controlfield tag="001">NLEJ253600936</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20231206145912.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">231206s2011 xx |||||o 00| ||eng c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1080/10826069908544890</subfield><subfield code="2">doi</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ253600936</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(TFO)791189505</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">rda</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="100" ind1="1" ind2=" "><subfield code="a">Bordenave, S.</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Continuous Hydrolysis of Goat Whey in an Ultrafiltration Reactor: Generation of Alpha-Lactorphin</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">2011</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">Text</subfield><subfield code="b">txt</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">Computermedien</subfield><subfield code="b">c</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">Online-Ressource</subfield><subfield code="b">cr</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Bovine whey hydrolysate has been developed and applied to areas such as nutrition, culture media, and isolation of bioactive peptides. In order to produce such a type of hydrolysate, it is possible to use goat whey which constitutes also a food processing by-product. Enzymatic hydrolysis of goat whey by pepsin was carried out in a continuous ultrafiltration reactor. The permeate contained peptide hydrolysate that was resolved by RP-HPLC. Second order derivative spectroscopy, amino acid analysis, and mass spectrometry revealed the presence of a biologically active peptide called alpha-lactorphin. This constitutes preliminary information about goat whey enzymatic degradation for future applications.</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Sannier, F.</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Piot, J. M.</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Ricart, G.</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">Enthalten in</subfield><subfield code="t">Preparative biochemistry & biotechnology</subfield><subfield code="d">Philadelphia, PA : Taylor & Francis, 1996</subfield><subfield code="g">29(1999), 2, Seite 189-202</subfield><subfield code="h">Online-Ressource</subfield><subfield code="w">(DE-627)NLEJ253593913</subfield><subfield code="w">(DE-600)2057441-1</subfield><subfield code="w">(DE-576)263254100</subfield><subfield code="x">1532-2297</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">number:2</subfield><subfield code="g">volume:29</subfield><subfield code="g">year:1999</subfield><subfield code="g">pages:189-202</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">https://www.tib.eu/de/suchen/id/tandf%3Adcc33564e783b14b1bd6f55745c4ba8ae057d4b3</subfield><subfield code="x">Digitalisierung</subfield><subfield code="z">Deutschlandweit zugänglich</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">ZDB-1-TFO</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="e">2</subfield><subfield code="d">29</subfield><subfield code="j">1999</subfield><subfield code="h">189-202</subfield></datafield></record></collection>
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