Staff Publications

Staff Publications

  • external user (warningwarning)
  • Log in as
  • language uk
  • About

    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

    We have a manual that explains all the features 

Record number 407961
Title Rheological properties of patatin gels compared with ß-lactoglobulin, ovalbumin, and glycinin
Author(s) Creusot, N.P.; Wierenga, P.A.; Laus, M.C.; Giuseppin, M.L.F.; Gruppen, H.
Source Journal of the Science of Food and Agriculture 91 (2011)2. - ISSN 0022-5142 - p. 253 - 261.
DOI http://dx.doi.org/10.1002/jsfa.4178
Department(s) Food Chemistry Group
VLAG
Publication type Refereed Article in a scientific journal
Publication year 2011
Keyword(s) heat-induced gelation - sunflower helianthus-annuus - potato-tuber protein - ionic-strength - whey proteins - egg-white - soy glycinin - physicochemical properties - interchange reactions - induced denaturation
Abstract BACKGROUND: The thermal unfolding and rheological properties of patatin gels were compared with those of commonly used proteins (ß-lactoglobulin, ovalbumin, glycinin). RESULTS: A significant difference between these proteins was observed in both the denaturation temperature (59 °C for patatin; about 20 °C lower than the other proteins) and the onset temperature of gel formation (50–60 °C, compared to 70–85 °C for the other proteins). At low ionic strength the minimal concentration was only 6% (w/v) for patatin, compared to 8–11% for the other proteins. This effect was attributed to the relatively high exposed hydrophobicity of patatin as determined by hydrophobic interaction chromatography. For gels compared at ‘iso-strength’, the frequency dependence was found to be close to identical, while small differences were observed in the strain at fracture. CONCLUSIONS: Patatin was found to form gels with comparable small-deformational rheological properties as typical food proteins. In addition, at concentrations where the elastic modulus was similar for all proteins, the frequency and strain dependence were also comparable. From this it is concluded that patatin is a promising protein to be used in food applications as a gelling agent.
Comments
There are no comments yet. You can post the first one!
Post a comment
 
Please log in to use this service. Login as Wageningen University & Research user or guest user in upper right hand corner of this page.