Zobrazeno 1 - 10
of 21
pro vyhledávání: '"Seronei Chelulei Cheison"'
Publikováno v:
Journal of Dairy Research. 86:114-119
The experiments reported in this research paper examine the potential of digestion using acidic enzymes Protease A and Protease M to selectively hydrolyse α-lactalbumin (α-La) whilst leaving β-lactoglobulin (β-Lg) relatively intact. Both enzymes
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3850028c2deae55835d43fca285ba95a
https://doi.org/10.1017/s0022029919000086
https://doi.org/10.1017/s0022029919000086
Autor:
Elena Leeb, Jörg Hinrichs, Ulrich Kulozik, Thomas Letzel, Seronei Chelulei Cheison, Aline Holder
Publikováno v:
International Dairy Journal. 38:116-123
Two food grade fractionation processes using ion-exchange membrane adsorption chromatography (IE-MAC) and cross-flow electro membrane filtration (CFEMF) were successfully developed for the fractionation of complex peptide mixtures. Feed solutions for
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e2d58597b3a90fc046bb8e991e729a25
https://doi.org/10.1016/j.idairyj.2013.12.006
https://doi.org/10.1016/j.idairyj.2013.12.006
Publikováno v:
Journal of Food Engineering. 116:176-183
Maillard reaction is influenced by protein and sugar properties, water activity (aw) as well as the glycosylation time and temperature. The aim of this work was to investigate the influence of environmental parameters on the glycosylation reaction ki
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::22a687ded30ad6e38707b03e8c2259ec
https://doi.org/10.1016/j.jfoodeng.2012.11.003
https://doi.org/10.1016/j.jfoodeng.2012.11.003
Publikováno v:
Critical reviews in food science and nutrition. 57(2)
Proteins in solution are subject to myriad forces stemming from interactions with each other as well as with the solvent media. The role of the environmental conditions, namely pH, temperature, ionic strength remains under-estimated yet it impacts pr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::10a437bac9aab9ad20c39d2d4884c405
https://pubmed.ncbi.nlm.nih.gov/25976220
https://pubmed.ncbi.nlm.nih.gov/25976220
Publikováno v:
LWT. 49:117-122
Whey protein (WP) purification exploits selective heat and salt stabilities. Proteins are denatured. WP α-lactalbumin (α-La) and β-lactoglobulin (β-Lg) are resistant to trypsin (EC 3.4.21.4) and pepsin (EC 3.4.23.1), respectively. This work was t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ed92435b30ef6ef00ad2592a195d8e9e
https://doi.org/10.1016/j.lwt.2012.03.022
https://doi.org/10.1016/j.lwt.2012.03.022
Publikováno v:
Food Chemistry. 125:1241-1248
Trypsin (EC 3.4.21.4) hydrolysis of food proteins are done at the optimum pH (7.8) and temperature (37 °C). Little information is available on the effect of sub-optimal conditions on hydrolysis. Bovine β-lactoglobulin (β-Lg) was hydrolysed by tryp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8979702a4fa345d222ca88e0f057a948
https://doi.org/10.1016/j.foodchem.2010.10.042
https://doi.org/10.1016/j.foodchem.2010.10.042
Publikováno v:
International Dairy Journal. 21:166-171
Whey protein isolate (93.84% protein) was hydrolysed using bovine trypsin (EC 3.4.21.4) at an enzyme-to-substrate ratio of 1.0% (w w −1 ) over a range of temperatures and pH. Residual protein was quantified using reversed-phase high performance liq
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::88d1d3661d019a070d8e26edc79396de
https://doi.org/10.1016/j.idairyj.2010.09.008
https://doi.org/10.1016/j.idairyj.2010.09.008
Publikováno v:
Food Chemistry. 125:121-127
Proteins acquire conformation in aqueous media due to the influence of the buffer salt composition and concentration. Such influence may have impact on the enzyme–substrate interaction and somehow steer the enzyme attack properties, leading to rele
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::63c1157e94861d38e4fe2e2378dc07de
https://doi.org/10.1016/j.foodchem.2010.08.047
https://doi.org/10.1016/j.foodchem.2010.08.047
Publikováno v:
Journal of Agricultural and Food Chemistry. 59:1572-1581
Temperature and pH influence the conformation of the whey protein β-lactoglobulin (β-Lg) monomer, dimer, and octamer formation, its denaturation, and solubility. Most hydrolyses have been reported at trypsin (EC 3.4.21.4) optimum conditions (pH 7.8
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e11105dee1e59bb6c529d56708ed9270
https://doi.org/10.1021/jf1039876
https://doi.org/10.1021/jf1039876
Publikováno v:
Procedia Food Science. 1:1540-1546
Tryptic hydrolysis of β-Lactoglobulin (β-Lg) has been shown as an excellent way to produce several functional peptides. However enzymatic hydrolysis results in a mixture of numerous different peptides, which is problematic regarding the enrichment
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::24ec2802019e2044a12f826dcec8af22