Zobrazeno 1 - 10
of 77
pro vyhledávání: '"Alice B. Nongonierma"'
Publikováno v:
Journal of Functional Foods, Vol 34, Iss , Pp 49-58 (2017)
Dipeptidyl peptidase IV (DPP-IV) inhibitory peptides were identified in silico within camel milk proteins. Camel milk was hydrolysed with trypsin using a design of experiments (DOE, temperature (40–60 °C), enzyme to substrate (E:S) ratio (0.50–2
Externí odkaz:
https://doaj.org/article/2299601a9f2c42719c6bfae923301045
Autor:
Alice B. Nongonierma, Luca Dellafiora, Sara Paolella, Gianni Galaverna, Pietro Cozzini, Richard J. FitzGerald
Publikováno v:
Frontiers in Endocrinology, Vol 9 (2018)
Inhibition of dipeptidyl peptidase IV (DPP-IV) may be exploited to maintain the incretin effect during the postprandial phase. As a result, glycemic regulation and energy homeostasis may be improved. Food protein-derived peptides have been identified
Externí odkaz:
https://doaj.org/article/f23bc7c3906d4d21a86c1c869847d51b
Publikováno v:
Journal of Functional Foods, Vol 17, Iss , Pp 640-656 (2015)
Milk proteins are a good source of bioactive peptides (BAPs). BAPs can positively affect various health biomarkers in vitro. The role of milk protein-derived BAPs in humans was reviewed herein. To date, a limited number of BAPs have been identified i
Externí odkaz:
https://doaj.org/article/6bdc33b6f6de4bf3b3898e0ddfd72f3c
Publikováno v:
Journal of Functional Foods, Vol 5, Iss 4, Pp 1909-1917 (2013)
Dipeptides with a C terminal Pro inhibit dipeptidyl peptidase IV (DPP-IV), a key enzyme in incretin hormone processing. It was hypothesised that tri- and tetrapeptides with a proline at the C-terminus may also be DPP-IV inhibitors. Therefore, an in s
Externí odkaz:
https://doaj.org/article/3657681d54864f3dbbe316edd271d01a
Autor:
Léa Fleury, Barbara Deracinois, Camille Dugardin, Alice B. Nongonierma, Richard J. FitzGerald, Christophe Flahaut, Benoit Cudennec, Rozenn Ravallec
Publikováno v:
International Journal of Molecular Sciences; Volume 23; Issue 15; Pages: 8365
Dipeptidyl-peptidase IV (DPP-IV) plays an essential role in glucose metabolism by inactivating incretins. In this context, food-protein-derived DPP-IV inhibitors are promising glycemic regulators which may act by preventing the onset of type 2 diabet
Publikováno v:
International Dairy Journal. 81:113-121
peer-reviewed The nitrogen solubility (pH 2.0–8.0), heat stability (pH 6.2–7.4) and viscosity (pH 6.2–7.4) properties of bovine milk protein isolate (MPI) and its Flavourzyme™, Neutrase™ and Protamex™ enzymatic hydrolysates were studied.
Publikováno v:
Food Chemistry. 244:340-348
peer-reviewed Nine novel dipeptidyl peptidase IV (DPP-IV) inhibitory peptides (FLQY, FQLGASPY, ILDKEGIDY, ILELA, LLQLEAIR, LPVP, LQALHQGQIV, MPVQA and SPVVPF) were identified in camel milk proteins hydrolysed with trypsin. This was achieved using a s
Publikováno v:
Food & Function. 9:407-416
Tropical banded crickets (Gryllodes sigillatus) were studied for their ability to yield hydrolysates with dipeptidyl peptidase IV (DPP-IV) inhibitory properties. A cricket protein isolate (CPI) was prepared following extraction of the water soluble p
Strategies for the discovery and identification of food protein-derived biologically active peptides
Publikováno v:
Trends in Food Science & Technology. 69:289-305
peer-reviewed Background: The widespread application of protein-derived bioactive peptides (BAPs) with health promoting properties in human nutrition is currently limited. This may be due to the fact that several challenges exist in the discovery and
Publikováno v:
Innovative Food Science & Emerging Technologies. 43:239-252
This review, focusing on studies published between 2005 and 2017, analysed the literature on the generation of bioactive peptides (BAPs) from edible insect proteins following enzymatic hydrolysis. The protein extraction and quantification methodologi