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Article: Effects of high pressure on the conformation of freeze-dried soy protein isolate: A FTIR spectroscopic study

TitleEffects of high pressure on the conformation of freeze-dried soy protein isolate: A FTIR spectroscopic study
Authors
KeywordsFourier Transform Infrared Spectroscopy (Ftir)
High Pressure
Protein Conformation
Soy Protein Isolates (Spi)
Issue Date2009
Citation
Guang Pu Xue Yu Guang Pu Fen Xi/Spectroscopy And Spectral Analysis, 2009, v. 29 n. 5, p. 1237-1240 How to Cite?
AbstractThe effect of high pressure (HP) treatment on the conformation of freeze-dried soy protein isolates (SPI) was investigated by Fourier transform infrared (FTIR) spectroscopy. Within the amide I′ region (1600-1700 cm -1) of the deconvoluted FTIR curve of SPI, more than 10 bands associated with protein conformation were distinctly observed, attributed to the CO stretching vibration and to a small extent to C-N stretching vibration of the peptide bonds, respectively. The secondary structure of native SPI is estimated to be composed of 15%-16% α-helix, 39%-44% extended strands, 17.5% random coils, and 21%-27% turns. The analyses of intensity and wavenumber of the bands showed that, HP treatment at pressures of 200-400 MPa resulted in the increases in intensity and a "red-shift" (about 2 cm -1) of these bands. HP treatment at 600 MPa further increased the band intensity of the amide I′ region. The analyses of amide II bands showed that HP treatment led to gradual increases in intensity and absolute area of amide II bands, in a pressure-dependent manner. Thus, it is suggested that HP treatment resulted in gradual unfolding of secondary and tertiary structure of SPI, while the structure of denatured proteins underwent a "rebuilding" process after the release of high pressure. These results confirm that the HP-induced modification of SPI is by means of the HP-induced conformational changes.
Persistent Identifierhttp://hdl.handle.net/10722/179128
ISSN
2015 Impact Factor: 0.275
2015 SCImago Journal Rankings: 0.199
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorTang, CHen_US
dc.contributor.authorMa, CYen_US
dc.date.accessioned2012-12-19T09:52:13Z-
dc.date.available2012-12-19T09:52:13Z-
dc.date.issued2009en_US
dc.identifier.citationGuang Pu Xue Yu Guang Pu Fen Xi/Spectroscopy And Spectral Analysis, 2009, v. 29 n. 5, p. 1237-1240en_US
dc.identifier.issn1000-0593en_US
dc.identifier.urihttp://hdl.handle.net/10722/179128-
dc.description.abstractThe effect of high pressure (HP) treatment on the conformation of freeze-dried soy protein isolates (SPI) was investigated by Fourier transform infrared (FTIR) spectroscopy. Within the amide I′ region (1600-1700 cm -1) of the deconvoluted FTIR curve of SPI, more than 10 bands associated with protein conformation were distinctly observed, attributed to the CO stretching vibration and to a small extent to C-N stretching vibration of the peptide bonds, respectively. The secondary structure of native SPI is estimated to be composed of 15%-16% α-helix, 39%-44% extended strands, 17.5% random coils, and 21%-27% turns. The analyses of intensity and wavenumber of the bands showed that, HP treatment at pressures of 200-400 MPa resulted in the increases in intensity and a "red-shift" (about 2 cm -1) of these bands. HP treatment at 600 MPa further increased the band intensity of the amide I′ region. The analyses of amide II bands showed that HP treatment led to gradual increases in intensity and absolute area of amide II bands, in a pressure-dependent manner. Thus, it is suggested that HP treatment resulted in gradual unfolding of secondary and tertiary structure of SPI, while the structure of denatured proteins underwent a "rebuilding" process after the release of high pressure. These results confirm that the HP-induced modification of SPI is by means of the HP-induced conformational changes.en_US
dc.languageengen_US
dc.relation.ispartofGuang Pu Xue Yu Guang Pu Fen Xi/Spectroscopy and Spectral Analysisen_US
dc.subjectFourier Transform Infrared Spectroscopy (Ftir)en_US
dc.subjectHigh Pressureen_US
dc.subjectProtein Conformationen_US
dc.subjectSoy Protein Isolates (Spi)en_US
dc.titleEffects of high pressure on the conformation of freeze-dried soy protein isolate: A FTIR spectroscopic studyen_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.doi10.3964/j.issn.1000-0593(2009)05-1237-04en_US
dc.identifier.scopuseid_2-s2.0-65149092099en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-65149092099&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume29en_US
dc.identifier.issue5en_US
dc.identifier.spage1237en_US
dc.identifier.epage1240en_US
dc.identifier.isiWOS:000265756100020-
dc.identifier.scopusauthoridTang, CH=35197262700en_US
dc.identifier.scopusauthoridMa, CY=7402924944en_US

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