Titre du document / Document title
Partially carboxymethylated feather keratins. 1. Properties in aqueous systems
Auteur(s) / Author(s)
SCHROOYEN Peter M. M. (1) ;
DIJKSTRA Piet J. (1) ;
OBERTHÜR Radulf C. (1) ;
BANTJES Adriaan (1) ;
FEIJEN Jan (1) ;
Affiliation(s) du ou des auteurs / Author(s) Affiliation(s)
(1) Department of Chemical Technology, University of Twente, P.O. Box 217, 7500 AE Enschede, PAYS-BAS
Résumé / Abstract
Feather keratins were extracted from chicken feathers with an aqueous solution of urea and 2-mercaptoethanol. The keratin solution obtained was dialyzed to remove the reagents. Upon dialysis, extensive protein aggregation occurred. To obtain stable solutions or dispersions in water, cysteine residues were modified prior to dialysis with iodoacetamide, iodoacetic acid, or bromosuccinic acid, thereby blocking free thiol groups and introducing hydrophilic groups. For the development of biodegradable materials with good mechanical properties from these biopolymers, disulfide bonds between the keratin molecules are needed. Therefore, cysteine residues were only partially modified by using different reagent/cysteine molar ratios. The reaction rate constants of iodoacetate with glutathione and 2-mercaptoethanol were successfully used to predict the degree of modification of keratin cysteine. It was shown that, for carboxymethylated keratin, fewer aggregates were formed for higher degrees of cysteine modification, while more protein was present as oligomers. Aggregates and oligomers were stabilized through intermolecular disulfide bonds.
Revue / Journal Title
Journal of agricultural and food chemistry
ISSN
0021-8561
CODEN JAFCAU
Source / Source
2000, vol. 48, n
o9, pp. 4326-4334 (1 p.1/4)
Langue / Language
Anglais
Editeur / Publisher
American Chemical Society, Washington, DC, ETATS-UNIS
(1953)
(Revue)
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Localisation / Location
INIST-CNRS, Cote INIST : 7332, 35400009110314.0930
Nº notice refdoc (ud4) : 825033
