Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Jean-Claude van Ceunebroeck"'
Publikováno v:
Innovative Food Science & Emerging Technologies. 74:102830
The effect of pulsed electric field (PEF) and/or mild thermal processing at 60 °C (T60) on the cooking behaviour of potato tissue in media with different Ca2+ concentrations (0-0.5%) was investigated. The rate constant for texture degradation during
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::80d165dec371cce086961149141d8659
https://doi.org/10.1016/j.ifset.2021.102830
https://doi.org/10.1016/j.ifset.2021.102830
Autor:
Joséphine Van Wambeke, Peter Goos, Lucie G. Moens, Marc Hendrickx, Jean-Claude Van Ceunebroeck, Ann Van Loey, Elien De Laet
Publikováno v:
Innovative Food Science & Emerging Technologies. 74:102826
Pulsed electric field (PEF) and mild thermal pretreatments at 60 °C (T60) may help preserve texture of plant tissue during thermal processing through pectin modification. However, potato starch may counteract the adhesive role of pectin during therm
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c03b6a4e8d71fc3f16a4996b683438e3
https://doi.org/10.1016/j.ifset.2021.102826
https://doi.org/10.1016/j.ifset.2021.102826
Thermal inactivation of pectin methylesterase from different potato cultivars (Solanum tuberosum L.)
Publikováno v:
LWT. 138:110600
Pectin methylesterase (PME) is an important enzyme that can alter the texture of potato products during processing and storage. To manage the textural properties of potato based products, low and/or high temperature blanching can be used to promote o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::82cc70a53dd1d77207415f6b3369f867
https://doi.org/10.1016/j.lwt.2020.110600
https://doi.org/10.1016/j.lwt.2020.110600
Autor:
W. Herreman, Gisèle Préaux, Ignace Hanssens, Frans Van Cauwelaert, Constant Gielens, Hugo Dangreau, Jean-Claude van Ceunebroeck
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Biomembranes. 728:293-304
We investigated the interaction between alpha-lactalbumin and sonicated dimyristoylphosphatidylcholine at pH 4 and different temperatures. (1) At 23 degrees C and lipid-to-protein molar ratios below 170, the interaction results in a disruption of the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0e2fb813e04a52fc4f37b3ebe37d7f97
https://doi.org/10.1016/0005-2736(83)90498-4
https://doi.org/10.1016/0005-2736(83)90498-4
Publikováno v:
Physical Methods on Biological Membranes and Their Model Systems ISBN: 9781468475401
Bovine α-lactalbumin was used to study the influence of the protein conformation on its interaction with phosphatidylcholine liposomes. The isoionic point of α-lactalbumin is at pH 5, and it has been demonstrated that between pH 4 and 2, the protei
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1a4ae5e088843028f5f3f080d3e4aca8
https://doi.org/10.1007/978-1-4684-7538-8_25
https://doi.org/10.1007/978-1-4684-7538-8_25
