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Impact of enzyme inactivation conditions during the generation of whey protein hydrolysates on their physicochemical and bioactive properties
Author(s) -
Le Maux Solène,
gonierma Alice B.,
Lardeux Claire,
FitzGerald Richard J.
Publication year - 2018
Publication title -
international journal of food science and technology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.831
H-Index - 96
eISSN - 1365-2621
pISSN - 0950-5423
DOI - 10.1111/ijfs.13576
Subject(s) - hydrolysate , chemistry , oxygen radical absorbance capacity , whey protein , hydrolysis , antioxidant , food science , chromatography , enzymatic hydrolysis , enzyme , limiting , biochemistry , antioxidant capacity , mechanical engineering , engineering
Summary The thermal inactivation conditions (75 °C × 35 min, 80 °C × 10 min, 85 °C × 5 min and 90 °C × 5 min) for Protamex™ following bovine whey protein concentrate ( WPC ) hydrolysis was studied with the view to limiting WPC hydrolysate ( WPH ) aggregation while maintaining bioactivity. A decrease in the amount of large WPH aggregates formed was observed at inactivation temperatures ≤85 °C. However, the WPC appeared to be more hydrolysed on heating at 75 °C × 35 min, as Protamex™ was active for longer under these heating conditions. Significantly ( P  <   0.05), higher WPH antioxidant (oxygen radical absorbance capacity – ORAC ) activity was obtained on inactivation at temperatures ≤80 °C. In contrast, the dipeptidyl peptidase IV (DPP‐IV) inhibitory properties of all WPH samples were similar ( P  >   0.05). A reduction in thermal treatment from 90 °C × 5 min to 85 °C × 5 min was sufficient to decrease the amount of large aggregates formed in the hydrolysate without altering its bioactive properties.

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