Relative quantitation analysis of the substrate specificity of glutamyl endopeptidase with bovine α-caseins

Yi Shen Zhu, Phanindra Kalyankar, Richard J. FitzGerald

Research output: Contribution to journalArticlepeer-review

Abstract

A bovine α-caseins' preparation digested with glutamyl endopeptidase (GE) at 37 and 50 °C was quantitatively analysed with the isobaric tag for relative and absolute quantification (iTRAQ) technique using nano-LC-ESI-QTOF-MS/MS. Incubation temperature was shown to affect protein digestion. MS analysis of the digestion products indicated that phosphorylated peptides were less sensitive than non-phosphorylated peptides according to the MS intensities. GE hydrolysed Glu(51)-Tyr(52) and Glu(50)-Glu(51) in Glu(49)-Glu(50)-Glu(51)-Tyr(52) of bovine αs1-casein. The results herein helped to confirm the precise process of α-caseins' hydrolysis with GE, which is significant for quantifying the release of bio- and techno-functional peptides.

Original languageEnglish
Pages (from-to)463-467
Number of pages5
JournalFood Chemistry
Volume167
DOIs
Publication statusPublished - 15 Jan 2015

Keywords

  • Bovine α-caseins' digest
  • Glutamyl endopeptidase
  • Isobaric tag for relative and absolute quantification
  • LC-MS/MS
  • Substrate specificity

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