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 497010
Title Rheological properties of dispersions of enzymatically cross-linked apo-α-lactalbumin
Author(s) Saricay, Yunus; Wierenga, Peter A.; Vries, Renko de
Source Food Hydrocolloids 56 (2016). - ISSN 0268-005X - p. 344 - 351.
DOI https://doi.org/10.1016/j.foodhyd.2015.12.039
Department(s) Physical Chemistry and Soft Matter
Food Chemistry Group
VLAG
Publication type Refereed Article in a scientific journal
Publication year 2016
Keyword(s) Enzymatic cross-linking - Gelation - Oxidative enzymes - Protein aggregates - Rheology
Abstract

The enzymatic cross-linking of apo-α-lactalbumin (α-LA) with horseradish peroxidase (HRP) leads to the formation of hydrophilic protein aggregates with controlled size and architecture. We explore the rheological properties of dispersions of these HRP-cross-linked α-LA aggregates with a hydrodynamic radius (RH) of 100 nm as a function of protein concentration. Above approximately 4% (w/v) of protein, the dispersions exhibit a sol-to-gel transition due to jamming of the densely packed protein aggregates. The storage modulus (G') and apparent viscosity (η) increase exponentially with protein concentration. At a fixed concentration, the modulus G' and viscosity η of the dispersions show a power law increase with increasing particle concentration. All jammed dispersions are highly, and reversibly, shear thinning, and have an apparent viscosity that increases without bounds as the shear rate approaches zero. Our results confirm that the enzymatically cross-linked α-LA aggregates are highly swollen and hydrophilic. As a consequence, their interaction remains purely repulsive even when compressed. Horseradish peroxidase-catalyzed cross-linking of apo-α-lactalbumin thus allows for creating reversibly shear thinning protein hydrogels at rather low protein concentrations, which may be important for precisely tailoring structuring by proteins in novel food formulations.

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.