ISSN:
1750-3841
Source:
Blackwell Publishing Journal Backfiles 1879-2005
Topics:
Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
,
Process Engineering, Biotechnology, Nutrition Technology
Notes:
The pH 4.6-soluble fraction of the peptic hydrolyzate of as 1-casein contained the 23 N-terminal residues, αsl-CN(fl-23), as a major pep-tide. Reversed-phase HPLC indicated that small amounts of other peptides such as αsl-CN(f154-199) were also contained in this fraction. By removing of these peptides, the emulsifying activity (EA) of the αsl-CN(fl-23) fraction was markedly decreased. However, when the removed peptide fraction was added to the purified αsl-CN(fl-23), the EA was increased. Some synergistic effect in the emulsification seemed to exist between αsl-CN(fl-23) and the other peptides. Although the purified αsl-CN(fl-23) had low EA values at neutral pH levels, it showed high emulsifying and surface activities in the acidic pH region.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1111/j.1365-2621.1986.tb13097.x
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