<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Criquet, S.</style></author><author><style face="normal" font="default" size="100%">Tagger, S.</style></author><author><style face="normal" font="default" size="100%">Vogt, G.</style></author><author><style face="normal" font="default" size="100%">Le petit, J.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Endoglucanase and β-glycosidase activities in an evergreen oak litter: annual variation and regulating factors</style></title><secondary-title><style face="normal" font="default" size="100%">Soil Biology and Biochemistry</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Cellulase</style></keyword><keyword><style  face="normal" font="default" size="100%">hemicellulase</style></keyword><keyword><style  face="normal" font="default" size="100%">Isoenzymes</style></keyword><keyword><style  face="normal" font="default" size="100%">litter</style></keyword><keyword><style  face="normal" font="default" size="100%">Polysaccharides</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2002</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2002///</style></date></pub-dates></dates><urls><web-urls><url><style face="normal" font="default" size="100%">http://linkinghub.elsevier.com/retrieve/pii/S0038071702000457</style></url></web-urls></urls><volume><style face="normal" font="default" size="100%">34</style></volume><pages><style face="normal" font="default" size="100%">1111 - 1120</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">This paper represents the third part of a larger study about the processes involved in litter biodegradation in an oak copse in France. It concerns the variations in activities of endoglucanases and of β-glycosidases over 13 months in forest litter. Evergreen oak (Quercus ilex L.) litter was taken as a model because Q. ilex is the most abundant tree species in forests of the French Mediterranean area. The activities of several endoglucanases and β-glycosidases, and the concentrations of the proteins and reducing sugars were measured in the evergreen oak litter between October 1997 and October 1998. Several biotic and abiotic factors, potentially involved in the regulation of the activities of these hydrolyzing enzymes, were also measured: culturable heterotrophic bacteria, cellulolytic bacteria and cellulolytic fungi, moisture, temperature and pH of the litter. Under this Mediterranean climate, the moisture of the litter was strongly correlated with many factors and is likely to be important in regulating the temporal dynamics of various biological parameters. A multiple regression analysis showed that the annual dynamic of the culturable heterotrophic bacteria was primarily influenced by moisture but also by variations in concentration of reducing sugars in the litter. Moreover, these bacteria were correlated with the activities of several β-glycosidases, and specifically with the N-acetyl-glucosaminidases (r=0.93). No relationships were established between the number of cellulolytic microorganisms (bacteria and fungi) and the activities of endoglucanases (i.e. cellulases and hemicellulases). The seasonal trends of certain biotic processes, and the influence of pH and of temperature on these processes are also discussed. Electrophoretic analyses were used to estimate the number of cellulase and xylanase isoenzymes in the litter, and to study their fluctuations over one year. The prevailing cellulase isoenzyme had a Rf of 0.64, and there was no relationship between the abundance of cellulolytic microorganisms and the electrophoretic profiles of the cellulases. In the case of the xylanases, the electrophoretic profiles were homogenous throughout the year, and the prevailing xylanase had a Rf of 0.75.</style></abstract><issue><style face="normal" font="default" size="100%">8</style></issue></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Criquet, S</style></author><author><style face="normal" font="default" size="100%">Tagger, S</style></author><author><style face="normal" font="default" size="100%">Vogt, G</style></author><author><style face="normal" font="default" size="100%">Le petit, J</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Endoglucanase and β-glycosidase activities in an evergreen oak litter: annual variation and regulating factors</style></title><secondary-title><style face="normal" font="default" size="100%">Soil Biology and Biochemistry</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Cellulase</style></keyword><keyword><style  face="normal" font="default" size="100%">hemicellulase</style></keyword><keyword><style  face="normal" font="default" size="100%">Isoenzymes</style></keyword><keyword><style  face="normal" font="default" size="100%">litter</style></keyword><keyword><style  face="normal" font="default" size="100%">Polysaccharides</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2002</style></year></dates><volume><style face="normal" font="default" size="100%">34</style></volume><pages><style face="normal" font="default" size="100%">1111-1120</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">This paper represents the third part of a larger study about the processes involved in litter biodegradation in an oak copse in France. It concerns the variations in activities of endoglucanases and of β-glycosidases over 13 months in forest litter. Evergreen oak (Quercus ilex L.) litter was taken as a model because Q. ilex is the most abundant tree species in forests of the French Mediterranean area. The activities of several endoglucanases and β-glycosidases, and the concentrations of the proteins and reducing sugars were measured in the evergreen oak litter between October 1997 and October 1998. Several biotic and abiotic factors, potentially involved in the regulation of the activities of these hydrolyzing enzymes, were also measured: culturable heterotrophic bacteria, cellulolytic bacteria and cellulolytic fungi, moisture, temperature and pH of the litter. Under this Mediterranean climate, the moisture of the litter was strongly correlated with many factors and is likely to be important in regulating the temporal dynamics of various biological parameters. A multiple regression analysis showed that the annual dynamic of the culturable heterotrophic bacteria was primarily influenced by moisture but also by variations in concentration of reducing sugars in the litter. Moreover, these bacteria were correlated with the activities of several β-glycosidases, and specifically with the N-acetyl-glucosaminidases (r=0.93). No relationships were established between the number of cellulolytic microorganisms (bacteria and fungi) and the activities of endoglucanases (i.e. cellulases and hemicellulases). The seasonal trends of certain biotic processes, and the influence of pH and of temperature on these processes are also discussed. Electrophoretic analyses were used to estimate the number of cellulase and xylanase isoenzymes in the litter, and to study their fluctuations over one year. The prevailing cellulase isoenzyme had a Rf of 0.64, and there was no relationship between the abundance of cellulolytic microorganisms and the electrophoretic profiles of the cellulases. In the case of the xylanases, the electrophoretic profiles were homogenous throughout the year, and the prevailing xylanase had a Rf of 0.75.</style></abstract></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Pascoal Neto, C.</style></author><author><style face="normal" font="default" size="100%">Rocha, J.</style></author><author><style face="normal" font="default" size="100%">Gil, A.</style></author><author><style face="normal" font="default" size="100%">Cordeiro, N.</style></author><author><style face="normal" font="default" size="100%">Esculcas, a P.</style></author><author><style face="normal" font="default" size="100%">Rocha, S.</style></author><author><style face="normal" font="default" size="100%">Delgadillo, I.</style></author><author><style face="normal" font="default" size="100%">de Jesus, J. D.</style></author><author><style face="normal" font="default" size="100%">Correia, a J.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">13C solid-state nuclear magnetic resonance and Fourier transform infrared studies of the thermal decomposition of cork.</style></title><secondary-title><style face="normal" font="default" size="100%">Solid state nuclear magnetic resonance</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Fourier Transform Infrared (citation)</style></keyword><keyword><style  face="normal" font="default" size="100%">Hot Temperature</style></keyword><keyword><style  face="normal" font="default" size="100%">Lignin</style></keyword><keyword><style  face="normal" font="default" size="100%">Lignin: chemistry</style></keyword><keyword><style  face="normal" font="default" size="100%">Lipids</style></keyword><keyword><style  face="normal" font="default" size="100%">Magnetic Resonance Spectroscopy</style></keyword><keyword><style  face="normal" font="default" size="100%">Membrane Lipids</style></keyword><keyword><style  face="normal" font="default" size="100%">Membrane Lipids: chemistry</style></keyword><keyword><style  face="normal" font="default" size="100%">Polysaccharides</style></keyword><keyword><style  face="normal" font="default" size="100%">Polysaccharides: chemistry</style></keyword><keyword><style  face="normal" font="default" size="100%">Spectroscopy</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">1995</style></year><pub-dates><date><style  face="normal" font="default" size="100%">1995///</style></date></pub-dates></dates><urls><web-urls><url><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/7773647</style></url></web-urls></urls><volume><style face="normal" font="default" size="100%">4</style></volume><pages><style face="normal" font="default" size="100%">143 - 151</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">The thermal decomposition of cork has been studied by Fourier transform infrared (FTIR) spectroscopy and 13C solid-state nuclear magnetic resonance (NMR) spectroscopy with cross-polarization and magic-angle spinning (CP-MAS), high-power 1H decoupling (HPDEC) and cross-polarization depolarization-polarization (CPDP). Waxes and other soluble components of cork begin to decompose at ca. 150 degrees C. This is accompanied by partial decomposition of suberin, probably initiated at the points of attachment to the cell wall. The carbohydrates begin to decompose at ca. 200 degrees C. The decomposition of lignin begins at 250-300 degrees C, while suberin undergoes further degradation. Significant amounts of coke are formed in the process. At 400 degrees C cork has been transformed into coke with traces of partially decomposed suberin. The thermal decomposition of cork is dependent on the calcination time, particularly in the 200-350 degrees C range.</style></abstract><issue><style face="normal" font="default" size="100%">3</style></issue><notes><style face="normal" font="default" size="100%">The following values have no corresponding Zotero field:&lt;br/&gt;accession-num: 7773647</style></notes></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Asensio, A</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Structural studies of a hemicellulose B fraction (B-2) from the cork of Quercus suber</style></title><secondary-title><style face="normal" font="default" size="100%">Canadian journal of chemistry</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Configuration</style></keyword><keyword><style  face="normal" font="default" size="100%">GLC-MS (voyant)</style></keyword><keyword><style  face="normal" font="default" size="100%">Polysaccharides</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">1988</style></year></dates><volume><style face="normal" font="default" size="100%">66</style></volume><pages><style face="normal" font="default" size="100%">449</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">Polysaccharide B-2 contains xylose, arabinose, glucose, galactose, 4-0-methylglucuronic acid, and rhamnose in the molar ratio of 17: 12: 12:6:4: 1. The polysaccharide has a backbone of P(1-4)- and P( 1-3)-linked glucopyranosyl, P(lk4)-linked xylopyranosyl, and (1-4)- and (1-6)-linked galactopyranosyl residues. Arabinofuranosyl, rhamnopyranosyl, and some xylopyranosyl and galactopyranosyl groups are present as nonreducing end units. Glucopyranosyluronic acid side chains are attached at 0 - 2 of some xylose residues. The anomeric configurations of the different glycosyl groups were determined by a study of the chromium trioxide oxidation of the acetylatcd polysaccharide and by nuclear magnetic reasonance spectra of the methylated polysaccharide.</style></abstract></record></records></xml>