Oxidation promotes cross-linking but impairs film-forming properties of whey proteins

Research output: Contribution to journalArticlepeer-review

54 Scopus citations


The objective of the study was to investigate the impact of oxidation on the film-forming properties of whey protein isolate (WPI). Sequential heating (70-90 °C) then oxidation (0.1 mM FeCl3/1 mM ascorbate/0-20 mM H2O2) (H → O) or vice versa (O → H) were conducted to oxidize/unfold WPI at pH 6.8 and 8.0 before casting. The resulting films were characterized through mechanical, microstructural, and protein electrophoretic analyses. Oxidation promoted protein cross-linking mainly through disulfide bonds. Tensile strength (TS) and elongation at break (EAB) of films decreased for WPI oxidized by higher concentrations of H2O 2. Film solubility (protein leachability) at pH 3-7, ranging from 20 to 40%, was unaffected by H2O2 up to 5 mM but reached almost 100% at above 5 mM H2O2 except at pH 4-5. β-Lactoglobulin dimers and its complex with α-lactalbumin were abundant in O → H WPI films and polymers of WPI dominated in H → O films. Microstructural images confirmed that oxidation promoted crumbly structures thereby explaining the reduced film-forming capability.

Original languageEnglish
Pages (from-to)11-19
Number of pages9
JournalJournal of Food Engineering
Issue number1
StatePublished - Mar 2013

Bibliographical note

Funding Information:
Funding provided by the US Department of Agriculture , NRI/CSREES (Grant 20083550318790) and the US Department of Homeland Security, Science & Technology Directorate , through a technology development and deployment program managed by The National Institute For Hometown Security (Grant 200902160810).


  • Edible films
  • Oxidation
  • Physical properties
  • Whey protein isolate

ASJC Scopus subject areas

  • Food Science


Dive into the research topics of 'Oxidation promotes cross-linking but impairs film-forming properties of whey proteins'. Together they form a unique fingerprint.

Cite this