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Article: Raman spectroscopic study of amidated food proteins

TitleRaman spectroscopic study of amidated food proteins
Authors
KeywordsAmidation
Gluten
Raman spectroscopy
Soy proteins isolates
Spray-dried egg white
Issue Date2007
PublisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/foodchem
Citation
Food Chemistry, 2007, v. 105 n. 2, p. 784-792 How to Cite?
AbstractVarious amounts of tryptophan were attached to three food protein products: soy protein isolates, spray-dried egg white and gluten, using a water-soluble carbodiimide method. The extent of amidation was determined by a spectrophotometric method. Raman spectra (600-2000 cm -1) of the modified proteins were obtained and analyzed. The phenyl stretching vibration at 1552 cm -1, directly attributed to the attached tryptophan, was used as a marker band, and increases in band intensity were observed in the modified protein samples. Calibration curves were constructed by plotting the intensity ratio of the 1552 cm -1 band to the 1003 cm -1 phenylalanine stretching band (used as an internal standard) against the amount of tryptophan attached. High correlation coefficients, (r) ≥ 0.99, were obtained from these calibration curves. The Raman spectral data showed a transition from ordered conformation to random coil structures in the amidated food protein products. © 2007 Elsevier Ltd. All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/68627
ISSN
2023 Impact Factor: 8.5
2023 SCImago Journal Rankings: 1.745
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorWong, HWen_HK
dc.contributor.authorPhillips, DLen_HK
dc.contributor.authorMa, CYen_HK
dc.date.accessioned2010-09-06T06:06:16Z-
dc.date.available2010-09-06T06:06:16Z-
dc.date.issued2007en_HK
dc.identifier.citationFood Chemistry, 2007, v. 105 n. 2, p. 784-792en_HK
dc.identifier.issn0308-8146en_HK
dc.identifier.urihttp://hdl.handle.net/10722/68627-
dc.description.abstractVarious amounts of tryptophan were attached to three food protein products: soy protein isolates, spray-dried egg white and gluten, using a water-soluble carbodiimide method. The extent of amidation was determined by a spectrophotometric method. Raman spectra (600-2000 cm -1) of the modified proteins were obtained and analyzed. The phenyl stretching vibration at 1552 cm -1, directly attributed to the attached tryptophan, was used as a marker band, and increases in band intensity were observed in the modified protein samples. Calibration curves were constructed by plotting the intensity ratio of the 1552 cm -1 band to the 1003 cm -1 phenylalanine stretching band (used as an internal standard) against the amount of tryptophan attached. High correlation coefficients, (r) ≥ 0.99, were obtained from these calibration curves. The Raman spectral data showed a transition from ordered conformation to random coil structures in the amidated food protein products. © 2007 Elsevier Ltd. All rights reserved.en_HK
dc.languageengen_HK
dc.publisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/foodchemen_HK
dc.relation.ispartofFood Chemistryen_HK
dc.rightsFood Chemistry. Copyright © Elsevier BV.en_HK
dc.subjectAmidationen_HK
dc.subjectGlutenen_HK
dc.subjectRaman spectroscopyen_HK
dc.subjectSoy proteins isolatesen_HK
dc.subjectSpray-dried egg whiteen_HK
dc.titleRaman spectroscopic study of amidated food proteinsen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0308-8146&volume=105&spage=784&epage=792&date=2007&atitle=Raman+spectroscopic+study+of+amidated+food+proteinsen_HK
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.2007.01.040en_HK
dc.identifier.scopuseid_2-s2.0-34447257943en_HK
dc.identifier.hkuros145322en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-34447257943&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume105en_HK
dc.identifier.issue2en_HK
dc.identifier.spage784en_HK
dc.identifier.epage792en_HK
dc.identifier.isiWOS:000249001700045-
dc.publisher.placeNetherlandsen_HK
dc.identifier.scopusauthoridWong, HW=36920238800en_HK
dc.identifier.scopusauthoridPhillips, DL=7404519365en_HK
dc.identifier.scopusauthoridMa, CY=7402924944en_HK
dc.identifier.issnl0308-8146-

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