Zobrazeno 1 - 10
of 19
pro vyhledávání: '"Isabelle Boucher"'
Publikováno v:
Social Robotics ISBN: 9783031246661
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7b1aeec9bc03a58fa4ccc043fc6b4638
https://doi.org/10.1007/978-3-031-24667-8_23
https://doi.org/10.1007/978-3-031-24667-8_23
Autor:
Pauline Cayer, Nathalie Côté, Isabelle Boucher, Christian Bleau, Lucie Lamontagne, Alexia Monges
Publikováno v:
Phytothérapie. 5:27-31
Le chitosane est une molecule retrouvee naturellement dans les carapaces de crustaces marins. Les derives obtenus par hydrolyse de cette molecule possedent plusieurs proprietes biologiques interessantes au niveau nutraceutique. Des experiences dans u
Publikováno v:
The Journal of Supercritical Fluids. 38:94-102
In the pharmaceutical area, fine particles with a narrow particle size distribution are required to obtain a high surface area. In addition, particle size is one of the critical factors for the determination of appropriate routes of drug administrati
Publikováno v:
Journal of Food Protection. 65:828-833
The antimicrobial properties of various chitosan-lactate polymers (ranging from 0.5 to 1.2 MDa in molecular weight) against two yeasts isolated from fermented vegetables and against three lactic acid bacteria from a mixed starter for sauerkraut on me
Publikováno v:
Scopus-Elsevier
Chitosanase was produced by the strain of Streptomyces lividans TK24 bearing the csn gene from Streptomyces sp. N174, and purified by S-Sepharose and Bio-Gel A column chromatography. Partially (25-35%) N-acetylated chitosan was digested by the purifi
Publikováno v:
Petite enfance, services de garde éducatifs et développement des enfants
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::80a11efd8b39d2b02dab7ffe8a527568
https://doi.org/10.2307/j.ctv18pgsk2.8
https://doi.org/10.2307/j.ctv18pgsk2.8
Publikováno v:
Biotechnology Letters. 13:845-850
The chitosanase gene from a new soil isolate, the actinomyceteKitasatosporia N174, was cloned inStreptomyces lividans TK24. The enzyme expressed from the cloned gene had a molecular weight of approximately 29,500; an isoelectric point of 7.5 and was
Lactococcus raffinolactis , unlike most lactococci, is able to ferment α-galactosides, such as melibiose and raffinose. More than 12 kb of chromosomal DNA from L. raffinolactis ATCC 43920 was sequenced, including the α-galactosidase gene and genes
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b3b8ae2aa720f06a8635762a425b74dd
https://europepmc.org/articles/PMC165199/
https://europepmc.org/articles/PMC165199/
Publikováno v:
Journal of dairy science. 84(7)
The three Lactococcus lactis plasmids pSRQ700, pSRQ800, and pSRQ900 encode the previously described anti-phage resistance mechanisms LlaDCHI, AbiK, and AbiQ, respectively. Since these plasmids are likely to be introduced into industrial Lactococcus l
Autor:
Tamo Fukamizo, André H. Juffer, Ryszard Brzezinski, Witold Neugebauer, Isabelle Boucher, Hans J. Vogel, Hugo Tremblay, Yuji Honda
Publikováno v:
The Journal of biological chemistry. 275(33)
Based on the crystal structure of chitosanase from Streptomyces sp. N174, we have calculated theoretical pK(a) values of the ionizable groups of this protein using a combination of the boundary element method and continuum electrostatics. The pK(a) v