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Article: Effect of high pressure treatment on aggregation and structural properties of soy protein isolate

TitleEffect of high pressure treatment on aggregation and structural properties of soy protein isolate
Authors
KeywordsFourier Transform Infrared (Ftir) Spectroscopy
High Pressure
Laser Scattering
Protein Conformation
Soy Protein Isolate (Spi)
Issue Date2009
PublisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/locate/lwt
Citation
Lwt - Food Science And Technology, 2009, v. 42 n. 2, p. 606-611 How to Cite?
AbstractThe aggregation and structural properties of soy protein isolate (SPI), induced by high pressure (HP) treatment at 200-600 MPa were investigated by size-exclusion chromatography combined with multi-angle laser scattering (SEC-MALLS) and fourier transform infrared (FTIR) spectroscopy. HP treatment at lower pressure level (e.g., 200 MPa) resulted in formation of marked insoluble aggregate of SPI, while the treatment at higher pressure level (e.g., 600 MPa) led to transformation of insoluble aggregate to soluble one. The soluble aggregate formed at 400 or 600 MPa had much less mean molecular weight (MW) (about 5.2 × 106 g/mol) than that at 200 MPa (about 1.6 × 107 g/mol), and was also much more homogenous in MW distribution. FTIR analyses confirmed changes in secondary and tertiary structures, induced by HP treatment. These results can provide direct evidence or explanation for HP-induced modification of soy proteins. © 2008 Swiss Society of Food Science and Technology.
Persistent Identifierhttp://hdl.handle.net/10722/179097
ISSN
2015 Impact Factor: 2.711
2015 SCImago Journal Rankings: 1.300
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorTang, CHen_US
dc.contributor.authorMa, CYen_US
dc.date.accessioned2012-12-19T09:51:57Z-
dc.date.available2012-12-19T09:51:57Z-
dc.date.issued2009en_US
dc.identifier.citationLwt - Food Science And Technology, 2009, v. 42 n. 2, p. 606-611en_US
dc.identifier.issn0023-6438en_US
dc.identifier.urihttp://hdl.handle.net/10722/179097-
dc.description.abstractThe aggregation and structural properties of soy protein isolate (SPI), induced by high pressure (HP) treatment at 200-600 MPa were investigated by size-exclusion chromatography combined with multi-angle laser scattering (SEC-MALLS) and fourier transform infrared (FTIR) spectroscopy. HP treatment at lower pressure level (e.g., 200 MPa) resulted in formation of marked insoluble aggregate of SPI, while the treatment at higher pressure level (e.g., 600 MPa) led to transformation of insoluble aggregate to soluble one. The soluble aggregate formed at 400 or 600 MPa had much less mean molecular weight (MW) (about 5.2 × 106 g/mol) than that at 200 MPa (about 1.6 × 107 g/mol), and was also much more homogenous in MW distribution. FTIR analyses confirmed changes in secondary and tertiary structures, induced by HP treatment. These results can provide direct evidence or explanation for HP-induced modification of soy proteins. © 2008 Swiss Society of Food Science and Technology.en_US
dc.languageengen_US
dc.publisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/locate/lwten_US
dc.relation.ispartofLWT - Food Science and Technologyen_US
dc.subjectFourier Transform Infrared (Ftir) Spectroscopyen_US
dc.subjectHigh Pressureen_US
dc.subjectLaser Scatteringen_US
dc.subjectProtein Conformationen_US
dc.subjectSoy Protein Isolate (Spi)en_US
dc.titleEffect of high pressure treatment on aggregation and structural properties of soy protein isolateen_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.doi10.1016/j.lwt.2008.07.012en_US
dc.identifier.scopuseid_2-s2.0-55549102634en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-55549102634&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume42en_US
dc.identifier.issue2en_US
dc.identifier.spage606en_US
dc.identifier.epage611en_US
dc.identifier.isiWOS:000261505600027-
dc.publisher.placeUnited Kingdomen_US
dc.identifier.scopusauthoridTang, CH=35197262700en_US
dc.identifier.scopusauthoridMa, CY=7402924944en_US

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