The browser you are using is not supported by this website. All versions of Internet Explorer are no longer supported, either by us or Microsoft (read more here: https://www.microsoft.com/en-us/microsoft-365/windows/end-of-ie-support).

Please use a modern browser to fully experience our website, such as the newest versions of Edge, Chrome, Firefox or Safari etc.

Effects of ionic strength and denaturation time on polyethyleneglycol self-diffusion in whey protein solutions and gels visualized by nuclear magnetic resonance

Author

Summary, in English

Pulsed field gradient NMR spectroscopy was used to determine the poly(ethylene glycol) (PEG) self-diffusion coefficient (D-PEG) as a function of NaCl concentration (C-NaCl) and denaturation time (t(D)) in whey protein solutions and gels. D-PEG in the gel decreased with increasing C-NaCl concentrations and increased with increasing t(D); the increase ceased for all PEGs when the gel was fixed. This increase was more pronounced for the 82250 g/mol PEG than the 1080 g/mol PEG. Moreover, the diffusion coefficient of nonaggregated whey protein was measured and an increase for longer t(D) was also observed. Scanning electron microscopy images and H-1 spectra demonstrated that D-PEG were related to the structure changes and to the percentage of beta-lactoglobulin denaturation.

Department/s

Publishing year

2006

Language

English

Pages

5105-5112

Publication/Series

Journal of Agricultural and Food Chemistry

Volume

54

Issue

14

Document type

Journal article

Publisher

The American Chemical Society (ACS)

Topic

  • Agricultural Science, Forestry and Fisheries

Keywords

  • diffusion
  • NMR
  • whey proteins
  • denaturation time
  • gels
  • SEM
  • ionic strength

Status

Published

ISBN/ISSN/Other

  • ISSN: 0021-8561