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JOURNAL ARTICLE
RESEARCH SUPPORT, NON-U.S. GOV'T
Characterization of a goat whey peptic hydrolysate produced by an ultrafiltration membrane enzymic reactor.
Journal of Dairy Research 2000 November
Goat whey was hydrolysed by pepsin in an ultrafiltration membrane enzymic reactor coupled with a 30 kDa mineral membrane. Peptides collected in the permeate were resolved using reversed-phase HPLC. Their sequences were determined by amino acid analysis, second order derivative spectra analysis and mass spectrometry. Owing to the resistance of beta-lactoglobulin (beta-lg) towards pepsin, the majority of peptides identified were derived from alpha-lactalbumin (alpha-la). Pepsin showed a broad specificity of hydrolysis sites and generated a wide range of products from dipeptides to very large peptides containing disulphide bridges. The molecular masses of peptides resulting from alpha-la degradation were between 150 and 6900 Da: 36% were < 600 Da. 24% were 600-2000 Da and 40% were > 2000 Da.
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