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Article: Study of Succinylated Food Proteins by Raman Spectroscopy

TitleStudy of Succinylated Food Proteins by Raman Spectroscopy
Authors
KeywordsEgg white
Proteins
Raman spectroscopy
Soy protein isolates
Succinylation
Whey protein isolates
Issue Date2004
PublisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/journal/jafcau
Citation
Journal Of Agricultural And Food Chemistry, 2004, v. 52 n. 7, p. 1815-1823 How to Cite?
AbstractThree food protein products, soy protein isolates, spray-dried egg white, and whey protein isolates, were chemically modified to varying levels with succinic anhydride, and the extent of modification of these proteins were determined by standard wet chemistry methods. Raman spectra (500-2000 cm -1) of the modified proteins were obtained. New C=O stretching vibrations were observed at 1420 and 1737 cm-1 and were attributed to the carboxylate (COO-) and ester carbonyl (RCOO-) groups, respectively, which were appended to the proteins during succinylation. Two series of calibration curves were obtained by plotting the intensity ratio of the 1420 and 1737 cm-1 to 1003 cm-1 phenylalanine stretching band (used as an internal standard) against the extent of substituted ε-amino (and α-amino) groups and aliphatic hydroxyl groups, respectively. Linear fits were obtained with correlation coefficient r > 0.988. The Raman spectral data were also analyzed to study the effect of succinylation on the conformation of the three proteins. Some conformational changes were observed, including a transition from ordered to disordered structures, an exposure of tryptophan residues from a buried, hydrophobic microenvironment, and probably conformational shift of cystine residues.
Persistent Identifierhttp://hdl.handle.net/10722/68746
ISSN
2023 Impact Factor: 5.7
2023 SCImago Journal Rankings: 1.114
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorZhao, Yen_HK
dc.contributor.authorMa, CYen_HK
dc.contributor.authorYuen, SNen_HK
dc.contributor.authorPhillips, DLen_HK
dc.date.accessioned2010-09-06T06:07:16Z-
dc.date.available2010-09-06T06:07:16Z-
dc.date.issued2004en_HK
dc.identifier.citationJournal Of Agricultural And Food Chemistry, 2004, v. 52 n. 7, p. 1815-1823en_HK
dc.identifier.issn0021-8561en_HK
dc.identifier.urihttp://hdl.handle.net/10722/68746-
dc.description.abstractThree food protein products, soy protein isolates, spray-dried egg white, and whey protein isolates, were chemically modified to varying levels with succinic anhydride, and the extent of modification of these proteins were determined by standard wet chemistry methods. Raman spectra (500-2000 cm -1) of the modified proteins were obtained. New C=O stretching vibrations were observed at 1420 and 1737 cm-1 and were attributed to the carboxylate (COO-) and ester carbonyl (RCOO-) groups, respectively, which were appended to the proteins during succinylation. Two series of calibration curves were obtained by plotting the intensity ratio of the 1420 and 1737 cm-1 to 1003 cm-1 phenylalanine stretching band (used as an internal standard) against the extent of substituted ε-amino (and α-amino) groups and aliphatic hydroxyl groups, respectively. Linear fits were obtained with correlation coefficient r > 0.988. The Raman spectral data were also analyzed to study the effect of succinylation on the conformation of the three proteins. Some conformational changes were observed, including a transition from ordered to disordered structures, an exposure of tryptophan residues from a buried, hydrophobic microenvironment, and probably conformational shift of cystine residues.en_HK
dc.languageengen_HK
dc.publisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/journal/jafcauen_HK
dc.relation.ispartofJournal of Agricultural and Food Chemistryen_HK
dc.subjectEgg whiteen_HK
dc.subjectProteinsen_HK
dc.subjectRaman spectroscopyen_HK
dc.subjectSoy protein isolatesen_HK
dc.subjectSuccinylationen_HK
dc.subjectWhey protein isolatesen_HK
dc.titleStudy of Succinylated Food Proteins by Raman Spectroscopyen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0021-8561&volume=52&spage=1815&epage=1823&date=2004&atitle=Study+of+succinylated+food+proteins+by+raman+spectroscopy+en_HK
dc.identifier.emailMa, CY: macy@hkucc.hku.hken_HK
dc.identifier.emailPhillips, DL: phillips@hku.hken_HK
dc.identifier.authorityMa, CY=rp00759en_HK
dc.identifier.authorityPhillips, DL=rp00770en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1021/jf030577aen_HK
dc.identifier.pmid15053515-
dc.identifier.scopuseid_2-s2.0-1842431424en_HK
dc.identifier.hkuros92411en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-1842431424&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume52en_HK
dc.identifier.issue7en_HK
dc.identifier.spage1815en_HK
dc.identifier.epage1823en_HK
dc.identifier.isiWOS:000220636900006-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridZhao, Y=14059361400en_HK
dc.identifier.scopusauthoridMa, CY=7402924944en_HK
dc.identifier.scopusauthoridYuen, SN=7103160942en_HK
dc.identifier.scopusauthoridPhillips, DL=7404519365en_HK
dc.identifier.issnl0021-8561-

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