File Download

There are no files associated with this item.

  Links for fulltext
     (May Require Subscription)
Supplementary

Article: Racemization assessment in alkali treated dietary proteins using high-performance liquid chromatography

TitleRacemization assessment in alkali treated dietary proteins using high-performance liquid chromatography
Authors
Issue Date1989
PublisherElsevier Inc. The Journal's web site is located at http://www.elsevier.com/locate/nutres
Citation
Nutrition Research, 1989, v. 9 n. 9, p. 1053-1065 How to Cite?
AbstractRacemization of amino acids was studied in alkali treated β-casein, oat protein (Avena sativa) and rapeseed protein (Brasica napus). Amino acid hydrolyzates containing enantiomeric amino acids, L-Xxx and D-Xxx, were converted into mixtures of N-ethoxycarbonyl-(Eoc-) derivatized diastereomeric dipeptide pairs, Eoc-Phe-L-Xxx, Eoc-Phe-D-Xxx and Eoc-Val-L-Xxx, Eoc-Val-D-Xxx upon the reaction with ethoxycarbonylphenylalanine N-hydroxysuccinimide ester (Eoc-Phe-ONSU) and ethoxycarbonylvaline N-hydroxysuccinimide ester (Eoc-Val-ONSU), respectively. The epimeric products were separated and determined by reversed phase high-performance liquid chromatography and the content of D-isomers was calculated. Racemization of β-casein using this method was in agreement with gas chromatography-mass spectrometry techniques described in the literature. In oat and rapeseed proteins exposed to alkaline conditions for 3 and 24 hours in 0.1 N NaOH at 65°C, the extend of racemization followed the sequence Ser>Asp>Phe>Glu>Val in most of the samples. In preliminar experiments, alkali-treated sunflower seed protein (Helian-thus annuus) samples were examined for the content of D-Phe. The reported HPLC technique represents a simple method for a practical assessment of racemization in dietary proteins.
Persistent Identifierhttp://hdl.handle.net/10722/178469
ISSN
2015 Impact Factor: 2.523
2015 SCImago Journal Rankings: 1.171

 

DC FieldValueLanguage
dc.contributor.authorPaquet, Aen_US
dc.contributor.authorMa, CYen_US
dc.date.accessioned2012-12-19T09:47:52Z-
dc.date.available2012-12-19T09:47:52Z-
dc.date.issued1989en_US
dc.identifier.citationNutrition Research, 1989, v. 9 n. 9, p. 1053-1065en_US
dc.identifier.issn0271-5317en_US
dc.identifier.urihttp://hdl.handle.net/10722/178469-
dc.description.abstractRacemization of amino acids was studied in alkali treated β-casein, oat protein (Avena sativa) and rapeseed protein (Brasica napus). Amino acid hydrolyzates containing enantiomeric amino acids, L-Xxx and D-Xxx, were converted into mixtures of N-ethoxycarbonyl-(Eoc-) derivatized diastereomeric dipeptide pairs, Eoc-Phe-L-Xxx, Eoc-Phe-D-Xxx and Eoc-Val-L-Xxx, Eoc-Val-D-Xxx upon the reaction with ethoxycarbonylphenylalanine N-hydroxysuccinimide ester (Eoc-Phe-ONSU) and ethoxycarbonylvaline N-hydroxysuccinimide ester (Eoc-Val-ONSU), respectively. The epimeric products were separated and determined by reversed phase high-performance liquid chromatography and the content of D-isomers was calculated. Racemization of β-casein using this method was in agreement with gas chromatography-mass spectrometry techniques described in the literature. In oat and rapeseed proteins exposed to alkaline conditions for 3 and 24 hours in 0.1 N NaOH at 65°C, the extend of racemization followed the sequence Ser>Asp>Phe>Glu>Val in most of the samples. In preliminar experiments, alkali-treated sunflower seed protein (Helian-thus annuus) samples were examined for the content of D-Phe. The reported HPLC technique represents a simple method for a practical assessment of racemization in dietary proteins.en_US
dc.languageengen_US
dc.publisherElsevier Inc. The Journal's web site is located at http://www.elsevier.com/locate/nutresen_US
dc.relation.ispartofNutrition Researchen_US
dc.titleRacemization assessment in alkali treated dietary proteins using high-performance liquid chromatographyen_US
dc.typeArticleen_US
dc.identifier.emailMa, CY: macy@hkucc.hku.hken_US
dc.identifier.authorityMa, CY=rp00759en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.scopuseid_2-s2.0-0024386971en_US
dc.identifier.volume9en_US
dc.identifier.issue9en_US
dc.identifier.spage1053en_US
dc.identifier.epage1065en_US
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridPaquet, A=7003782027en_US
dc.identifier.scopusauthoridMa, CY=7402924944en_US

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats