Stability to thermal treatment of dipeptidyl peptidase IV (DPP-IV) inhibitory activity of a boarfish (Capros aper) protein hydrolysate when incorporated into tomato-based products
| Autor: | Richard J. FitzGerald, William Crowe, Philip J. Allsopp, Chris M. McLaughlin, Finbarr O'Harte, Vadivel Parthsarathy, Jason Whooley, Emeir M. McSorley, Brian McGovern, Martin Devaney, Pádraigín A. Harnedy-Rothwell |
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| Přispěvatelé: | Department of Agriculture, Food and the Marine, Ireland |
| Jazyk: | angličtina |
| Rok vydání: | 2020 |
| Předmět: |
chemistry.chemical_classification
functional food ingredient antidiabetic Peptide Thermal treatment boarfish stability Inhibitory postsynaptic potential Industrial and Manufacturing Engineering Dipeptidyl peptidase Hydrolysate peptide dipeptidyl peptidase IV inhibition simulated gastrointestinal digestion Biochemistry chemistry thermal treatment Food Science protein hydrolysate |
| Popis: | peer-reviewed The full text of this article will not be available in ULIR until the embargo expires on the 07/05/2021 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 x 1 min and 121°C x 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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