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Dynamic rheological properties of native and cross-linked gliadin proteins.

Abstract：

:A comparison of cross-linked and native gliadin suspensions, with respect to the state of protein globular structure was carried out using small-angle X-ray scattering (SAXS), dynamic light scattering (DLS) and rheological analysis. Gliadin suspensions were also analyzed in the presence and absence of glycerol. DLS analysis showed that R(h) increased only with gliadin/EDC/NHS suspensions. However, Kratky plots revealed that gliadin and gliadin/L-cysteine maintained their globular shape even in absence or presence of glycerol. Rheological experiments revealed that gliadin and gliadin/L-cysteine suspension exhibited a similar profile with three main domains, and a sol-gel transition. Gliadin/EDC/NHS did not present any sol-gel transition, and this fact corroborates with DLS results and the hypothesis of lower protein-protein interaction, which are in agreement with G″ > G'.

journal_name

Int J Biol Macromol

journal_title

International journal of biological macromolecules

authors

Soares RM,Lionzo MI,Da Silveira NP,Rayas-Duarte P,Soldi V

doi

10.1016/j.ijbiomac.2012.06.041

subject

Has Abstract

pub_date

2012-11-01 00:00:00

pages

640-6

issue

4

eissn

0141-8130

issn

1879-0003

pii

S0141-8130(12)00273-5

journal_volume

51

pub_type

杂志文章

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