posted on 2013-03-27, 12:49authored byDavid Spellman, Gerard O'Cuinn, Richard J. Fitzgerald
Whey protein hydrolysates were generated at different total solids (TS) levels (50–300 g/l) using
the commercially available proteolytic preparation DebitraseTM HYW20, while enzyme to
substrate ratio, pH and temperature were maintained constant. Hydrolysis proceeded at a faster
rate at lower TS reaching a degree of hydrolysis (DH) of 16.6% at 300 g TS/l, compared with a
DH of 22.7% at 50 g TS/l after 6 h hydrolysis. The slower breakdown of intact whey proteins at
high TS was quantified by gel-permeation HPLC. Reversed-phase (RP) HPLC of hydrolysate
samples of equivalent DH (y15%) generated at different TS levels indicated that certain hydrophobic
peptide peaks were present at higher levels in hydrolysates generated at low TS. Sensory
evaluation showed that hydrolysates with equivalent DH values were significantly (P<0.0005)
less bitter when generated at 300 g TS/l (mean bitterness score=25.4%) than hydrolysates
generated at 50 g TS/l (mean bitterness score=39.9%). A specific hydrophobic peptide peak present
at higher concentrations in hydrolysates generated at low TS was isolated and identified as
b-lactoglobulin f(43–57), a fragment having the physical and chemical characteristics of a bitter
peptide.
History
Publication
Journal of Dairy Research;72 (2), pp. 138-143
Publisher
Cambridge University Press
Note
peer-reviewed
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