Littérature scientifique sur le sujet « GH ENZYMES »
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Articles de revues sur le sujet "GH ENZYMES"
Malgas, Samkelo, Mpho S. Mafa, Brian N. Mathibe et Brett I. Pletschke. « Unraveling Synergism between Various GH Family Xylanases and Debranching Enzymes during Hetero-Xylan Degradation ». Molecules 26, no 22 (9 novembre 2021) : 6770. http://dx.doi.org/10.3390/molecules26226770.
Texte intégralVucinic, Jelena, Gleb Novikov, Cédric Montanier, Claire Dumon, Thomas Schiex et Sophie Barbe. « A Comparative Study to Decipher the Structural and Dynamics Determinants Underlying the Activity and Thermal Stability of GH-11 Xylanases ». International Journal of Molecular Sciences 22, no 11 (31 mai 2021) : 5961. http://dx.doi.org/10.3390/ijms22115961.
Texte intégralAngelov, Angel, Christoph Loderer, Susanne Pompei et Wolfgang Liebl. « Novel Family of Carbohydrate-Binding Modules Revealed by the Genome Sequence of Spirochaeta thermophila DSM 6192 ». Applied and Environmental Microbiology 77, no 15 (17 juin 2011) : 5483–89. http://dx.doi.org/10.1128/aem.00523-11.
Texte intégralIakiviak, Michael, Roderick I. Mackie et Isaac K. O. Cann. « Functional Analyses of Multiple Lichenin-Degrading Enzymes from the Rumen Bacterium Ruminococcus albus 8 ». Applied and Environmental Microbiology 77, no 21 (2 septembre 2011) : 7541–50. http://dx.doi.org/10.1128/aem.06088-11.
Texte intégralAbe, Koichi, Masahiro Nakajima, Tetsuro Yamashita, Hiroki Matsunaga, Shinji Kamisuki, Takanori Nihira, Yuta Takahashi et al. « Biochemical and structural analyses of a bacterial endo-β-1,2-glucanase reveal a new glycoside hydrolase family ». Journal of Biological Chemistry 292, no 18 (7 mars 2017) : 7487–506. http://dx.doi.org/10.1074/jbc.m116.762724.
Texte intégralChristensen, Stefan Jarl, Silke Flindt Badino, Ana Mafalda Cavaleiro, Kim Borch et Peter Westh. « Functional analysis of chimeric TrCel6A enzymes with different carbohydrate binding modules ». Protein Engineering, Design and Selection 32, no 9 (septembre 2019) : 401–9. http://dx.doi.org/10.1093/protein/gzaa003.
Texte intégralRamirez, María Cecilia, Guillermina María Luque, Ana María Ornstein et Damasia Becu-Villalobos. « Differential neonatal testosterone imprinting of GH-dependent liver proteins and genes in female mice ». Journal of Endocrinology 207, no 3 (13 octobre 2010) : 301–8. http://dx.doi.org/10.1677/joe-10-0276.
Texte intégralGrøfte, Thorbjørn, Dorthe Svenstrup Jensen, Henning Grønbæk, Troels Wolthers, Søren Astrup Jensen, Niels Tygstrup et Hendrik Vilstrup. « Effects of growth hormone on steroid-induced increase in ability of urea synthesis and urea enzyme mRNA levels ». American Journal of Physiology-Endocrinology and Metabolism 275, no 1 (1 juillet 1998) : E79—E86. http://dx.doi.org/10.1152/ajpendo.1998.275.1.e79.
Texte intégralJaneček, Štefan, et Birte Svensson. « How many α-amylase GH families are there in the CAZy database ? » Amylase 6, no 1 (1 janvier 2022) : 1–10. http://dx.doi.org/10.1515/amylase-2022-0001.
Texte intégralOlsson, Bob, Mohammad Bohlooly-Y, Ola Brusehed, Olle G. P. Isaksson, Bo Ahrén, Sven-Olof Olofsson, Jan Oscarsson et Jan Törnell. « Bovine growth hormone-transgenic mice have major alterations in hepatic expression of metabolic genes ». American Journal of Physiology-Endocrinology and Metabolism 285, no 3 (septembre 2003) : E504—E511. http://dx.doi.org/10.1152/ajpendo.00444.2002.
Texte intégralThèses sur le sujet "GH ENZYMES"
Paës, Gabriel O'Donohue Michael. « Etude structure / fonction d'hémicellulases thermostables la xylanase GH-11 et l'arabinofuranosidase GH-51 de Thermobacillus xylanilyticus / ». Reims : S.C.D. de l'Université, 2005. http://scdurca.univ-reims.fr/exl-doc/GED00000167.pdf.
Texte intégralPaës, Gabriel. « Etude structure / fonction d'hémicellulases thermostables : la xylanase GH-11 et l'arabinofuranosidase GH-51 de Thermobacillus xylanilyticus ». Reims, 2005. http://theses.univ-reims.fr/exl-doc/GED00000167.pdf.
Texte intégralHemicellulose-degrading enzymes such as xylanases and arabinofuranosidases are potentially useful as biocatalysts for industrial applications. Theses enzymes are already used in numerous sectors such as paper industry for paper pulp whitening, in animal feed preparation to increase nutritional value, in the wine industry to improve bouquet properties etc. In addition, hemicellulases will be key enzymes for the future development of biorefineries which will convert agricultural wastes into transport fuels and other renewable chemicals. To increase understanding of the structural features that are important for the functionality in hemicellulases, we have studied structure/function relationships in enzymes belonging to two hemicellulases families. Directed mutagenesis methods have been used to probe different functional aspects in a thermostable GH-11 endoxylanase (Tx-Xyl), and a crystallographic analysis has been used to study a thermostable GH-51 arabinofuranosidase (Tx-Abf), both enzymes being from Thermobacillus xylanilyticus. Tx-Xyl has been studied with regard to its thermostability and with regard to one of its major structural features, the “thumb”. In order to increase thermostability and hence the usefulness for the degradation of lignocellulosic biomass, an already-tested strategy involving the introduction of disulphide bonds was used. A mutant that exhibits both an increased (10-fold) half-life at 70°C and higher specific activity (30% increase) has been obtained. Gratifyingly, this mutant also displays an increased aptitude for the hydrolysis of arabinoxylans embedded in wheat bran. However, intriguingly, this increase is independent of the increased thermostability. On the basis of a molecular modelling study, modifications of the amino acid composition of Tx-Xyl thumb at key positions lead to increased or decreased catalytic activity. The abolition of the thumb by deletion mutagenesis altered substrate selectivity, and destroyed catalytic activity. In particular, the thumbless enzyme acquired the ability to fix cellotetraose, although this ligand could not be hydrolysed. Finally, a crystallographic study of Tx-Abf has provided a structural model for this enzyme at a resolution of 2. 1 Å. This new structure, the second for GH-51, revealed that the catalytic domain exhibits (b/a)8 architecture and the presence of a jelly-roll domain of unknown function. Compared to the only available structure for GH-51, Tx-Abf contains two putative disulphide bridges, one of which is close to the catalytic apparatus. In addition, the architecture of the catalytic cleft is topologically different to that of the other GH-51 structure. Site-directed mutagenesis of Trp248 has indicated an essential role for this residue in the hydrolysis of arabino-xylo oligosaccharides having a size of DP3 or more
Malgas, Samkelo. « The effect of GH family affiliations of mannanolytic enzymes on their synergistic associations during the hydrolysis of mannan-containing substrates ». Thesis, Rhodes University, 2015. http://hdl.handle.net/10962/d1017909.
Texte intégralTICKOO, ARUSHE. « CLONING AND EXPRESSION OF GENES BELONGING TO GH FAMILY OF ENZYMES IN BACILLUS SUBTILIS AND ASPERGILLUS ORYZAE ». Thesis, 2018. http://dspace.dtu.ac.in:8080/jspui/handle/repository/16196.
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