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  • Title: Characterization of a goat whey peptic hydrolysate produced by an ultrafiltration membrane enzymic reactor.
    Author: Bordenave BS, Sannier F, Ricart G, Piot JM.
    Journal: J Dairy Res; 2000 Nov; 67(4):551-9. PubMed ID: 11131068.
    Abstract:
    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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