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Article: Thermal analysis of flaxseed (Linum usitatissimum) proteins by differential scanning calorimetry

TitleThermal analysis of flaxseed (Linum usitatissimum) proteins by differential scanning calorimetry
Authors
LiChan, ECYMa, CY
KeywordsDifferential scanning calorimetry
Flaxseed
Linum usitatissiumum
Protein stability
Issue Date2002
PublisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/foodchem
Citation
Food Chemistry, 2002, v. 77 n. 4, p. 495-502 How to Cite?
DOI: http://dx.doi.org/10.1016/S0308-8146(01)00365-X
AbstractThe thermal properties of flaxseed (whole or dehulled), dehulled and delipidated meal, as well as proteins extracted and isolated from the meal, were investigated by differential scanning calorimetry (DSC). A high denaturation temperature (T d) of 114.7°C was observed for the major fraction of flaxseed protein isolated by anion-exchange chromatography, representing the 11-12 S storage globulin. Marked decreases in T d and enthalpy were observed at pH 3 compared with pH of 5 or higher, while the presence of high salt (1.0 M NaCl) resulted in higher thermal stability, enthalpy and greater cooperativity of the transition. Thermal analysis of the major fraction in the presence of chaotropic salts or protein structure perturbants (sodium dodecyl sulfate, urea, dithiothreitol, N-ethylmaleimide, ethylene glycol) suggested the contributions of hydrophobic and ionic interactions, hydrogen bonding as well as disulfide linkages or disulfide-sulfhydryl (SS-SH) interactions, to the thermal stability of flaxseed protein. Copyright © 2002 Elsevier Science Ltd.
Persistent Identifierhttp://hdl.handle.net/10722/68700
ISSN
0308-8146
2023 Impact Factor: 8.5
2023 SCImago Journal Rankings: 1.745
ISI Accession Number ID
WOS:000176619500014
References
References in Scopus

 

DC FieldValueLanguage
dc.contributor.authorLiChan, ECYen_HK
dc.contributor.authorMa, CYen_HK
dc.date.accessioned2010-09-06T06:06:52Z-
dc.date.available2010-09-06T06:06:52Z-
dc.date.issued2002en_HK
dc.identifier.citationFood Chemistry, 2002, v. 77 n. 4, p. 495-502en_HK
dc.identifier.issn0308-8146en_HK
dc.identifier.urihttp://hdl.handle.net/10722/68700-
dc.description.abstractThe thermal properties of flaxseed (whole or dehulled), dehulled and delipidated meal, as well as proteins extracted and isolated from the meal, were investigated by differential scanning calorimetry (DSC). A high denaturation temperature (T d) of 114.7°C was observed for the major fraction of flaxseed protein isolated by anion-exchange chromatography, representing the 11-12 S storage globulin. Marked decreases in T d and enthalpy were observed at pH 3 compared with pH of 5 or higher, while the presence of high salt (1.0 M NaCl) resulted in higher thermal stability, enthalpy and greater cooperativity of the transition. Thermal analysis of the major fraction in the presence of chaotropic salts or protein structure perturbants (sodium dodecyl sulfate, urea, dithiothreitol, N-ethylmaleimide, ethylene glycol) suggested the contributions of hydrophobic and ionic interactions, hydrogen bonding as well as disulfide linkages or disulfide-sulfhydryl (SS-SH) interactions, to the thermal stability of flaxseed protein. Copyright © 2002 Elsevier Science Ltd.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.subjectDifferential scanning calorimetryen_HK
dc.subjectFlaxseeden_HK
dc.subjectLinum usitatissiumumen_HK
dc.subjectProtein stabilityen_HK
dc.titleThermal analysis of flaxseed (Linum usitatissimum) proteins by differential scanning calorimetryen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0308-8146&volume=77&spage=495&epage=502&date=2002&atitle=Thermal+analysis+of+flaxseed+(Linum+usitatissimum)+proteins+by+differential+scanning+calorimetryen_HK
dc.identifier.emailMa, CY: macy@hkucc.hku.hken_HK
dc.identifier.authorityMa, CY=rp00759en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1016/S0308-8146(01)00365-Xen_HK
dc.identifier.scopuseid_2-s2.0-0036265114en_HK
dc.identifier.hkuros68443en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0036265114&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume77en_HK
dc.identifier.issue4en_HK
dc.identifier.spage495en_HK
dc.identifier.epage502en_HK
dc.identifier.isiWOS:000176619500014-
dc.publisher.placeNetherlandsen_HK
dc.identifier.scopusauthoridLiChan, ECY=7004388629en_HK
dc.identifier.scopusauthoridMa, CY=7402924944en_HK
dc.identifier.issnl0308-8146-

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