Reference : Influence of drying temperature on the solubility, the purity of isolates and the ele...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
Life sciences : Food science
http://hdl.handle.net/2268/4066
Influence of drying temperature on the solubility, the purity of isolates and the electrophoretic patterns of corn proteins
English
Malumba Kamba, Paul mailto [Université de Liège - ULg > > Gembloux Agro-Bio Tech >]
Vanderghem, Caroline mailto [Université de Liège - ULg > Gembloux Agro-Bio Tech > Gembloux Agro-Bio Tech >]
Deroanne, Claude [Université de Liège - ULg > Gembloux Agro-Bio Tech > Gembloux Agro-Bio Tech >]
Bera, François mailto [Université de Liège - ULg > Gembloux Agro-Bio Tech > Gembloux Agro-Bio Tech >]
2008
Food Chemistry
Elsevier Science
111
3
564-572
Yes (verified by ORBi)
International
0308-8146
Oxford
United Kingdom
[en] corn ; protein ; denaturation ; drying ; electrophoresis ; isolate ; zein ; albumin ; globulin ; glutelin ; solubility
[en] A sequential extraction of proteins from whole corn kernels dried between 54 and 130 degrees C was performed in order to elucidate the effect of the drying temperature on the solubility, the purity and the electrophoretic patterns of the different classes of corn proteins. It was observed that albumin, globulin and zein solubilities dropped significantly when the drying temperature increased, while fractions solubilised as glutelin-G(2) and glutelin-G3 increased until 110 degrees C before dropping slightly at 130 degrees C. The analysis of the solubility of different protein groups indicated that mechanisms other than the creation of new disulfide bonds between proteins occurred during the high temperature drying of corn. Except for glutelin-G1 and zein isolates, which were highly pure, the purities of albumin, globulin, glutelin-G2 and glutelin-G3 isolates after dialysis were influenced by the drying temperature. Sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) showed the disappearance of some water and salt-soluble poly-peptides at high drying temperatures. The electrophoretic patterns of zein and glutelin-G, were not significantly modified, although the solubility of zein was affected by the drying temperature. (c) 2008 Elsevier Ltd. All rights reserved.
Researchers ; Professionals ; Students ; General public ; Others
http://hdl.handle.net/2268/4066
also: http://hdl.handle.net/2268/65753
10.1016/j.foodchem.2008.04.030
http://www.sciencedirect.com/science?_ob=ArticleURL&_udi=B6T8J-4WDNKP9-2&_user=532081&_coverDate=12%2F31%2F2009&_alid=1264973234&_rdoc=1&_fmt=high&_orig=search&_cdi=5088&_sort=r&_docanchor=&view=c&_ct=4&_acct=C000026700&_version=1&_urlVersion=0&_userid=532081&md5=031e81ecf40a19858d86bf5513455c87

File(s) associated to this reference

Fulltext file(s):

FileCommentaryVersionSizeAccess
Open access
Corn proteins.pdfPublisher postprint512.94 kBView/Open

Bookmark and Share SFX Query

All documents in ORBi are protected by a user license.