Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Patrizia, Rasmussen"'
Publikováno v:
Journal of Cereal Science. 53:319-327
Formation of a gluten protein network is fundamental for the texture and the overall quality of pasta. Replacement of the gluten network in gluten-free pasta is a major technological challenge, and the conventional technological processes have to be
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3cec4a8c82df131da777423169c2e17b
https://doi.org/10.1016/j.jcs.2011.02.001
https://doi.org/10.1016/j.jcs.2011.02.001
Autor:
Patrizia Rasmussen, Carolina Pepe, Gianluca Picariello, Stefania Iametti, Sergio Lilla, Pasquale Ferranti, Francesco Bonomi
Publikováno v:
Food Chemistry. 124:1718-1726
In this study, the protein and peptide fractions of two commercial Italian barley malt beers, made with different processes by the same producer, have been analysed with a combined immunochemical and mass spectrometry approach. The “gluten” conte
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eb2e9b222827648f4d167f19557cf52a
https://doi.org/10.1016/j.foodchem.2010.07.111
https://doi.org/10.1016/j.foodchem.2010.07.111
Autor:
Patrizia Rasmussen, Hanne Frøkiær, Pasquale Ferranti, Francesco Addeo, Francesco Bonomi, Stefania Iametti
Publikováno v:
European Journal of Biochemistry. 269:1362-1372
Bovine β-lactoglobulin was hydrolyzed with trypsin or chymotrypsin in the course of heat treatment at 55, 60 and 65 °C at neutral pH. At these temperatures β-lactoglobulin undergoes significant but reversible structural changes. In the conditions
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::84f27b587479a34d18c9e841dae7dbd3
https://doi.org/10.1046/j.1432-1033.2002.02769.x
https://doi.org/10.1046/j.1432-1033.2002.02769.x
Autor:
Stefania Iametti, Pasquale Ferranti, Patrizia Rasmussen, Alberto Barbiroli, Dimitrios Fessas, Francesco Bonomi, Antonella Nasi
Fatty acids are the natural ligands associated with the bovine milk lipocalin, β-lactoglobulin (BLG), and were identified by means of mass spectrometry. The naturally bound ligands were found to contribute to the stability of the proteins toward den
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4399d825205eb3b56493a1d8f8f4b1aa
http://hdl.handle.net/11588/409670
http://hdl.handle.net/11588/409670
Autor:
Monica Galliano, Patrizia Rasmussen, Francesco Bonomi, Pasquale Ferranti, Daniela Maggioni, Stefania Iametti, Daniela Donghi, Alberto Barbiroli, Sandra Scanu, Maria Caterina Vilardo, Tiziana Beringhelli
Publikováno v:
Biological chemistry. 391(1)
Binding of fluorine-containing drugs to bovine β-lactoglobulin, the most abundant whey protein in bovine milk, was investigated by means of 19F NMR and mass spectrometry. The stoichiometry of the binding and its stability in acidic medium, where β-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::31d99930d56c19c15daf03d81de4813c
https://pubmed.ncbi.nlm.nih.gov/19919177
https://pubmed.ncbi.nlm.nih.gov/19919177
Autor:
Patrizia Rasmussen, Marcello Duranti, Gabriella Tedeschi, Alessio Scarafoni, Valerio Galbusera, Chiara Magni, Alessandro Consonni, Armando Negri
Publikováno v:
Phytochemistry. 69(9)
The paper describes the purification, structural characterization and inhibitory properties of a trypsin inhibitor from Lupinus albus L., a leguminous plant believed to be devoid of any protease inhibitor. The protein has been isolated by a newly set
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::015b031b244aa4a1d8566dc2020d12a3
https://pubmed.ncbi.nlm.nih.gov/18474386
https://pubmed.ncbi.nlm.nih.gov/18474386
Autor:
Francesco Bonomi, Patrizia Rasmussen, Giovanni Maria Mura, Alessio Coi, Maria Luisa Ganadu, Anna Maria Paola Bianucci
Publikováno v:
International journal of biological macromolecules. 42(3)
alphaB-crystallin is a small heat shock protein that shows chaperone-like activity, as it protects the aggregation of denatured proteins. In this work, the possible relationships between structural characteristics and the biological activity of alpha
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4ac5b583722000748bf050345ab17aea
https://pubmed.ncbi.nlm.nih.gov/18048095
https://pubmed.ncbi.nlm.nih.gov/18048095
Autor:
Pasquale Ferranti, Alberto Barbiroli, Patrizia Rasmussen, Stefania Iametti, Franco Faoro, Gianluca Picariello, Marcello Iriti, Franco Bonomi
Publikováno v:
Biopolymers
(2007): 57–72.
info:cnr-pdr/source/autori:Rasmussen P, Barbiroli A, Bonomi F, Faoro F, Ferranti P, Iriti M, Picariello G, Iametti S./titolo:Formation of structured polymers upon controlled denaturation of beta-lactoglobulin with different chaotropes./doi:/rivista:Biopolymers (Print)/anno:2007/pagina_da:57/pagina_a:72/intervallo_pagine:57–72/volume
(2007): 57–72.
info:cnr-pdr/source/autori:Rasmussen P, Barbiroli A, Bonomi F, Faoro F, Ferranti P, Iriti M, Picariello G, Iametti S./titolo:Formation of structured polymers upon controlled denaturation of beta-lactoglobulin with different chaotropes./doi:/rivista:Biopolymers (Print)/anno:2007/pagina_da:57/pagina_a:72/intervallo_pagine:57–72/volume
Prolonged exposure (>90 days) of bovine β-lactoglobulin (BLG) to subdenaturing concentrations of either urea or potassium thiocyanate resulted in the formation of ordered polymers in the form of fibrils. The fibrils obtained with each chaotrope show
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b00a6421f400e18fbe863ae0f59d3b9d
https://publications.cnr.it/doc/45740
https://publications.cnr.it/doc/45740
Autor:
Hanne Frøkiær, Patrizia Rasmussen, Pierpaolo Rovere, Francesco Bonomi, Alessandro Fiocchi, Claudio Poiesi, Stefania Iametti, A. Gaiaschi, Patrizia Restani
Publikováno v:
The Journal of dairy research. 70(1)
Bovine beta-lactoglobulin was hydrolyzed with trypsin or chymotrypsin before, during and after treatment at 600 MPa and pH 6.8 for 10 min at 30, 37 and 44 degrees C. The extent of beta-lactoglobulin hydrolysis under pressure was noticeably higher tha
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7e78b486f9fd654c716208bbe491e6b5
https://pubmed.ncbi.nlm.nih.gov/12617393
https://pubmed.ncbi.nlm.nih.gov/12617393
Autor:
Stefania, Iametti, Patrizia, Rasmussen, Hanne, Frøkiaer, Pasquale, Ferranti, Francesco, Addeo, Francesco, Bonomi
Publikováno v:
269 (2002): 1362–1372.
info:cnr-pdr/source/autori:Iametti S., Rasmussen P., Frokiaer H., Ferranti P., Addeo F., Bonomi F./titolo:Proteolysis of bovine beta-lactoglobulin during thermal treatment in subdenaturing conditions highlights some structural features of the temperature-modified protein and yields fragments with low immunoreactivity/doi:/rivista:/anno:2002/pagina_da:1362/pagina_a:1372/intervallo_pagine:1362–1372/volume:269
info:cnr-pdr/source/autori:Iametti S., Rasmussen P., Frokiaer H., Ferranti P., Addeo F., Bonomi F./titolo:Proteolysis of bovine beta-lactoglobulin during thermal treatment in subdenaturing conditions highlights some structural features of the temperature-modified protein and yields fragments with low immunoreactivity/doi:/rivista:/anno:2002/pagina_da:1362/pagina_a:1372/intervallo_pagine:1362–1372/volume:269
Bovine beta-lactoglobulin was hydrolyzed with trypsin or chymotrypsin in the course of heat treatment at 55, 60 and 65 degrees C at neutral pH. At these temperatures beta-lactoglobulin undergoes significant but reversible structural changes. In the c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::0da3ca11a7971c3dd65224a5ea821fa4
https://publications.cnr.it/doc/45525
https://publications.cnr.it/doc/45525