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Fractionation and Characterization of Glycomacropeptide from Caseinate and Skim Milk Hydrolysates
Author(s) -
MORR C.V.,
SEO A.
Publication year - 1988
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1988.tb10182.x
Subject(s) - chemistry , chromatography , size exclusion chromatography , sephadex , high performance liquid chromatography , hydrolysate , sodium dodecyl sulfate , skimmed milk , gel permeation chromatography , hydrolysis , fractionation , biochemistry , enzyme , food science , organic chemistry , polymer
Glycomacropeptide (GMP) was isolated from crystalline rennin and microbial rennet hydrolyzed caseinate and skim milk by Sephadex gel filtration, DEAE Sephadex ion exchange chromatography, Con A‐Sepharose affinity chromatography and exhaustive dialysis and characterized by size exclusion and reversed phase high performance liquid chromatography (HPLC) and sodium dodecyl sulfate gel electrophoresis (SDS PAGE). Size exclusion HPLC revealed one major GMP peak with a molecular weight of 33,000 daltons. SDS PAGE revealed a group of size‐heterogeneous peptides with molecular weights of < 18,000 daltons. Reversed phase HPLC revealed one major GMP peak with several minor peptides, indicating heterogeneity with respect to hydrophobicity/polarity.
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