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

Yi Shen Zhu; Phanindra Kalyankar; Richard J. FitzGerald

doi:10.1016/j.foodchem.2014.07.017

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 journal › Article › peer-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 α_s1-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 language	English
Pages (from-to)	463-467
Number of pages	5
Journal	Food Chemistry
Volume	167
DOIs	https://doi.org/10.1016/j.foodchem.2014.07.017
Publication status	Published - 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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10.1016/j.foodchem.2014.07.017

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title = "Relative quantitation analysis of the substrate specificity of glutamyl endopeptidase with bovine α-caseins",

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.",

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year = "2015",

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doi = "10.1016/j.foodchem.2014.07.017",

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AU - Zhu, Yi Shen

AU - Kalyankar, Phanindra

AU - FitzGerald, Richard J.

PY - 2015/1/15

Y1 - 2015/1/15

N2 - 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.

AB - 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.

KW - Bovine α-caseins' digest

KW - Glutamyl endopeptidase

KW - Isobaric tag for relative and absolute quantification

KW - LC-MS/MS

KW - Substrate specificity

UR - https://www.scopus.com/pages/publications/84904989443

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DO - 10.1016/j.foodchem.2014.07.017

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AN - SCOPUS:84904989443

SN - 0308-8146

VL - 167

SP - 463

EP - 467

JO - Food Chemistry

JF - Food Chemistry

ER -

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

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Keywords

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