Angiotensin converting enzyme inhibitory activity of soy protein subjected to selective hydrolysis and thermal processing

Wynnie Margatan, Kirsten Ruud, Qian Wang, Todd Markowski, Baraem Ismail

Research output: Contribution to journalArticle

20 Scopus citations

Abstract

Soy protein isolate (SPI) and β-conglycinin- and glycinin-rich fractions were hydrolyzed using papain and pepsin. Protein denaturation, profiling, and peptide identification were carried out following DSC, SDS-PAGE, and liquid chromatography-tandem mass spectrometry (LC-MS/MS) analysis. The in vitro antihypertensive activity of the hydrolysates was compared by determining the angiotensin converting enzyme (ACE) inhibitory activity. SDS-PAGE and LC-MS/MS analysis confirmed pepsin selectivity to glycinin and papain partial selectivity to β-conglycinin when the protein is least denatured. Both the papain-hydrolyzed SPI and the papain-hydrolyzed β-conglycinin-rich fraction had more than double the ACE inhibitory activity of that of pepsin-hydrolyzed SPI and pepsin-hydrolyzed glycinin-rich fraction. This observation indicated that β-conglycinin is a better precursor for antihypertensive peptides than glycinin. Additionally, the inhibitory activity of the papain-hydrolyzed SPI was thermally stable. This work demonstrated, for the first time, that selective hydrolysis to release peptides with ACE inhibitory activity can be accomplished without inducing extensive hydrolysis and performing unnecessary fractionation.

Original languageEnglish (US)
Pages (from-to)3460-3467
Number of pages8
JournalJournal of agricultural and food chemistry
Volume61
Issue number14
DOIs
StatePublished - Apr 10 2013

Keywords

  • angiotensin converting enzyme (ACE)
  • antihypertensive peptides
  • glycinin
  • soy protein hydrolysate
  • β-conglycinin

Fingerprint Dive into the research topics of 'Angiotensin converting enzyme inhibitory activity of soy protein subjected to selective hydrolysis and thermal processing'. Together they form a unique fingerprint.

  • Cite this