کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
7596253 | 1492124 | 2015 | 5 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Relative quantitation analysis of the substrate specificity of glutamyl endopeptidase with bovine α-caseins
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کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه
شیمی
شیمی آنالیزی یا شیمی تجزیه
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Relative quantitation analysis of the substrate specificity of glutamyl endopeptidase with bovine α-caseins Relative quantitation analysis of the substrate specificity of glutamyl endopeptidase with bovine α-caseins](/preview/png/7596253.png)
چکیده انگلیسی
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.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Food Chemistry - Volume 167, 15 January 2015, Pages 463-467
Journal: Food Chemistry - Volume 167, 15 January 2015, Pages 463-467
نویسندگان
Yi-shen Zhu, Phanindra Kalyankar, Richard J. FitzGerald,