Effects of high-pressure processing and enzymatic dephosphorylation on phosvitin properties

Stephanie P. Volk, Dong U. Ahn, Michael Zeece, Stephanie Jung

Research output: Contribution to journalArticle

5 Scopus citations

Abstract

Background: Egg phosvitin could be a good source of functional peptides. Enzymatic dephosphorylation and high-pressure processing combined with thermal treatment applied before proteolysis could produce phosvitin hydrolysates with different properties compared to its native form. Results: Phosvitin structure was maintained overall during high-pressure treatment of 600 MPa applied at an initial temperature of 65 °C regardless of the pH and duration of treatment, confirming the high structural stability of this phosphoprotein. Treatment of phosvitin with phosphatase increased the degree of dephosphorylation from 24% to 63%, after 2 and 18 h, respectively. Moderate dephosphorylation of phosvitin prior to proteolytic digestion improved its hydrolysis, allowing formation of peptides with a molecular weight lower than 17,000 kDa as determined by size exclusion chromatography. Angiotensin-converting enzyme (ACE) inhibition and antioxidant activity of dephosphorylated and protease-treated phosvitin was increased by 52% and 39%, respectively, as compared to protease-digested native phosvitin. Conclusion: Enzymatic dephosphorylation before proteolysis mimicking in vivo gut conditions improved ACE inhibition and antioxidant activity of phosvitin hydrolysates.

Original languageEnglish (US)
Pages (from-to)3095-3098
Number of pages4
JournalJournal of the Science of Food and Agriculture
Volume92
Issue number15
DOIs
StatePublished - Dec 2012

Keywords

  • Enzymatic dephosphorylation
  • High-pressure processing
  • Phosvitin

ASJC Scopus subject areas

  • Biotechnology
  • Food Science
  • Agronomy and Crop Science
  • Nutrition and Dietetics

Fingerprint Dive into the research topics of 'Effects of high-pressure processing and enzymatic dephosphorylation on phosvitin properties'. Together they form a unique fingerprint.

Cite this