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Article: Raman spectroscopic study of deamidated food proteins

TitleRaman spectroscopic study of deamidated food proteins
Authors
KeywordsDeamidation
Raman spectroscopy
Soy proteins isolates
Spray-dried egg white
Whey protein isolates
Issue Date2009
PublisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/foodchem
Citation
Food Chemistry, 2009, v. 113 n. 2, p. 363-370 How to Cite?
AbstractThree food protein products, soy and whey protein isolates and spray-dried egg white powder, were deamidated to various levels by 0.04 N hydrochloric acid. The extents of deamidation were determined using an ammonia electrode. Raman spectra of the modified proteins were obtained and analyzed. A new C{double bond, long}O stretching vibration band was observed at 1780 cm -1, attributed to γ-carboxyl groups of aspartic and glutamic acids. Calibration curves were constructed by plotting the intensity ratio of the 1780 cm -1 band to the 1003 cm -1 phenylalanine stretching band (as an internal standard) against the extent of deamidation. Linear fits were obtained with high correlation coefficients r > 0.987. Effect of deamidation on the conformation of these proteins was also studied by monitoring changes in Raman spectral characteristics, including a transition from ordered to disordered structures, exposure of tryptophan residues from a buried, hydrophobic microenvironment, and probable conformational changes of the aliphatic residues. © 2008 Elsevier Ltd. All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/159284
ISSN
2015 Impact Factor: 4.052
2015 SCImago Journal Rankings: 1.620
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorWong, HWen_HK
dc.contributor.authorChoi, SMen_HK
dc.contributor.authorPhillips, DLen_HK
dc.contributor.authorMa, CYen_HK
dc.date.accessioned2012-08-16T05:48:11Z-
dc.date.available2012-08-16T05:48:11Z-
dc.date.issued2009en_HK
dc.identifier.citationFood Chemistry, 2009, v. 113 n. 2, p. 363-370en_HK
dc.identifier.issn0308-8146en_HK
dc.identifier.urihttp://hdl.handle.net/10722/159284-
dc.description.abstractThree food protein products, soy and whey protein isolates and spray-dried egg white powder, were deamidated to various levels by 0.04 N hydrochloric acid. The extents of deamidation were determined using an ammonia electrode. Raman spectra of the modified proteins were obtained and analyzed. A new C{double bond, long}O stretching vibration band was observed at 1780 cm -1, attributed to γ-carboxyl groups of aspartic and glutamic acids. Calibration curves were constructed by plotting the intensity ratio of the 1780 cm -1 band to the 1003 cm -1 phenylalanine stretching band (as an internal standard) against the extent of deamidation. Linear fits were obtained with high correlation coefficients r > 0.987. Effect of deamidation on the conformation of these proteins was also studied by monitoring changes in Raman spectral characteristics, including a transition from ordered to disordered structures, exposure of tryptophan residues from a buried, hydrophobic microenvironment, and probable conformational changes of the aliphatic residues. © 2008 Elsevier Ltd. All rights reserved.en_HK
dc.languageengen_US
dc.publisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/foodchemen_HK
dc.relation.ispartofFood Chemistryen_HK
dc.subjectDeamidationen_HK
dc.subjectRaman spectroscopyen_HK
dc.subjectSoy proteins isolatesen_HK
dc.subjectSpray-dried egg whiteen_HK
dc.subjectWhey protein isolatesen_HK
dc.titleRaman spectroscopic study of deamidated food proteinsen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0308-8146&volume=113&spage=363&epage=&date=2009&atitle=Raman+spectroscopic+study+of+deamidated+food+proteinsen_US
dc.identifier.emailPhillips, DL: phillips@hku.hken_HK
dc.identifier.emailMa, CY: macy@hkucc.hku.hken_HK
dc.identifier.authorityPhillips, DL=rp00770en_HK
dc.identifier.authorityMa, CY=rp00759en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1016/j.foodchem.2008.09.027en_HK
dc.identifier.scopuseid_2-s2.0-53949124105en_HK
dc.identifier.hkuros204227en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-53949124105&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume113en_HK
dc.identifier.issue2en_HK
dc.identifier.spage363en_HK
dc.identifier.epage370en_HK
dc.identifier.isiWOS:000261084600001-
dc.publisher.placeNetherlandsen_HK
dc.identifier.scopusauthoridWong, HW=36920238800en_HK
dc.identifier.scopusauthoridChoi, SM=8873744400en_HK
dc.identifier.scopusauthoridPhillips, DL=7404519365en_HK
dc.identifier.scopusauthoridMa, CY=7402924944en_HK

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