ISSN:
1750-3841
Source:
Blackwell Publishing Journal Backfiles 1879-2005
Topics:
Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
,
Process Engineering, Biotechnology, Nutrition Technology
Notes:
Thirteen low-molecular-weight phosphopeptides were isolated from the water-soluble fraction of Comté cheese. The sample was fractionated and purified by gel permeation chromatography and reverse-phase HPLC. The peptide sequences were identified by Edman degradation and primary molecular structure was confirmed by mass spectrometry. The different peptides purified correspond to fragments of the sequence Val13-Lys 28 of β-casein and of the sequence Glu S-Lys 21 of α32 casein. These fragments probably originated from an initial proteolysis of the two caseins by plasmin, followed by further endopeptidase aminopeptidase and, possibly, carboxypeptidase digestions. Partial dephosphorylation of some β-casein fragments was observed. These peptides probably influence the flavor profile of comté cheese.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1111/j.1365-2621.1994.tb05558.x
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