Zobrazeno 1 - 10
of 21
pro vyhledávání: '"Solène Le Maux"'
Publikováno v:
International Journal of Food Science & Technology. 53:219-227
peer-reviewed The thermal inactivation conditions (75 degrees Cx35min, 80 degrees Cx10min, 85 degrees Cx5min and 90 degrees Cx5min) for Protamex following bovine whey protein concentrate (WPC) hydrolysis was studied with the view to limiting WPC hydr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::af9fec2cdcda75f032bb0e6f0a126a4c
https://doi.org/10.1111/ijfs.13576
https://doi.org/10.1111/ijfs.13576
Publikováno v:
Food Research International. 99:84-90
β-Lactoglobulin hydrolysates (βlgHs) were generated using elastase at enzyme-to-substrate ratios (E:S) of 0.5, 1.0 and 1.5% in order to reach target degree of hydrolysis (DH) values of 9 and 13%. The impact of different E:S during manufacture on hy
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d76bf5cb31a24d2fc6f6c2fa377f0bbc
https://doi.org/10.1016/j.foodres.2017.05.012
https://doi.org/10.1016/j.foodres.2017.05.012
Publikováno v:
Journal of the Science of Food and Agriculture. 97:1093-1101
Background: Hydrolysis parameters affecting the release of dipeptidyl peptidase IV (DPP-IV) inhibitory and antioxidant peptides from milk proteins have not been extensively studied. Therefore, a multifactorial (i.e. pH, temperature and hydrolysis tim
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b9f13cd384ef8fea249b81089d8afd03
https://doi.org/10.1002/jsfa.7834
https://doi.org/10.1002/jsfa.7834
Publikováno v:
Food Chemistry. 199:246-251
Enzymatic hydrolysis of whey protein (WP) was carried out under pH-controlled and non pH-controlled conditions using papain and a microbial-derived alternative (papain-like activity). The impact of such conditions on physicochemical and bioactive pro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c2a481bb4e1b078595ae75154f7a6eac
https://doi.org/10.1016/j.foodchem.2015.12.021
https://doi.org/10.1016/j.foodchem.2015.12.021
Publikováno v:
Food & Function. 7:3437-3443
Bovine α-lactalbumin (α-La) contains numerous dipeptidyl peptidase IV (DPP-IV) inhibitory peptide sequences within its primary structure. In silico analysis indicated that the targeted hydrolysis of α-La with elastase should release DPP-IV inhibit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b11f69ed744fc056de0a557f5f52b8ad
https://doi.org/10.1039/c6fo00239k
https://doi.org/10.1039/c6fo00239k
Autor:
Katy Horner, Victoria O’Sullivan, Richard J. FitzGerald, Alice B. Nongonierma, Aoife M. Curran, Lorraine Brennan, Eoin G. Murphy, Phil M. Kelly, Solène Le Maux
Background Dietary modifications can contribute to improved pancreatic β cell function and enhance glycemic control. Objectives The objectives of this study were as follows: 1) to investigate the potential of milk protein hydrolysates to modulate po
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0c061c0278a1f6315832444080215693
Publikováno v:
Journal of Cereal Science. 65:112-118
peer-reviewed The potential of quinoa to act as a source of dipeptidyl peptidase IV (DPP-IV) inhibitory and antioxidant peptides was studied. A quinoa protein isolate (QPI) with a purity of 40.73 ± 0.90% was prepared. The QPI was hydrolysed at 50 °
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e45f99d45b223781fd9d8b6ae54c0084
https://doi.org/10.1016/j.jcs.2015.07.004
https://doi.org/10.1016/j.jcs.2015.07.004
Publikováno v:
Journal of the science of food and agriculture. 97(4)
Hydrolysis parameters affecting the release of dipeptidyl peptidase IV (DPP-IV) inhibitory and antioxidant peptides from milk proteins have not been extensively studied. Therefore, a multifactorial (i.e. pH, temperature and hydrolysis time) composite
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::8d40dd5252f2ba0d537fea38902d0ea8
https://pubmed.ncbi.nlm.nih.gov/27271791
https://pubmed.ncbi.nlm.nih.gov/27271791
Publikováno v:
Journal of Agricultural and Food Chemistry
Journal of Agricultural and Food Chemistry, American Chemical Society, 2012, 60 (37), pp.9476-9483. ⟨10.1021/jf3028396⟩
Journal of Agricultural and Food Chemistry 37 (60), 9476-9483. (2012)
Journal of Agricultural and Food Chemistry, American Chemical Society, 2012, 60 (37), pp.9476-9483. ⟨10.1021/jf3028396⟩
Journal of Agricultural and Food Chemistry 37 (60), 9476-9483. (2012)
S. Le Maux is currently supported by a Teagasc Walsh Fellowship and the Department of Agriculture, Fisheries and Food (FIRM project 08/RD/TMFRC/650). We also acknowledge funding from IRCSET-Ulysses Travel Grant. peer-reviewed The dairy protein β-lac
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::595a6deb36458f007224f19d970e4fe8
https://doi.org/10.1021/jf3028396
https://doi.org/10.1021/jf3028396
Autor:
Phillip M. Kelly, Alice B. Nongonierma, Solène Le Maux, Brian A. Murray, Richard J. FitzGerald
The work described herein was supported by Enterprise Ireland under Grant Number TC2013-0001. The research was part funded by the Science Foundation Ireland Research Infrastructure Fund. peer-reviewed Short peptides in food protein hydrolysates are o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dddd4909f85a1f7d4de9cbef65a6d75a