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Stability to thermal treatment of dipeptidyl peptidase‐IV inhibitory activity of a boarfish ( Capros aper ) protein hydrolysate when incorporated into tomato‐based products
Author(s) -
HarnedyRothwell Pádraigín A.,
McLaughlin Chris M.,
Crowe William,
Allsopp Philip J.,
McSorley Emeir M.,
Devaney Martin,
Whooley Jason,
McGovern Brian,
Parthsarathy Vadivel,
O'Harte Finbarr P.M.,
FitzGerald Richard J.
Publication year - 2021
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.14615
Subject(s) - hydrolysate , peptide , chemistry , dipeptidyl peptidase , food science , digestion (alchemy) , biochemistry , enzyme , chromatography , hydrolysis
Summary Biofunctional peptide ingredients should retain their stability following standard processing operations in food‐based delivery vehicles. A boarfish protein hydrolysate, exhibiting anti‐diabetic activity, was subjected to a range of thermal treatments following incorporation into tomato‐based soup and juice products. The dipeptidyl peptidase‐IV (DPP‐IV) inhibitory activity and peptide profile of the hydrolysate within the products were assessed before and after thermal treatment. The treatments applied had no effect on the DPP‐IV inhibitory activity or peptide profile of the protein hydrolysate. The heat‐treated (90 °C × 1 min and 121 °C × 42 s) juice‐fortified beverage had microbial counts within the acceptable limits for consumption when stored at 4 °C for 30 days. Furthermore, the hydrolysate within the beverage products was resistant to simulated gastrointestinal digestion (SGID) regardless of whether it was heat‐ or non‐heat‐treated, or stored for 30 days at 4 °C. Therefore, tomato‐based beverages are suitable delivery vehicles for biofunctional peptide ingredients.