<?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></contributors><titles><title><style face="normal" font="default" size="100%">Biochemical and molecular characterization of a laccase from Marasmius quercophilus</style></title><secondary-title><style face="normal" font="default" size="100%">APPLIED AND ENVIRONMENTAL MICROBIOLOGY</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2000</style></year></dates><publisher><style face="normal" font="default" size="100%">AMER SOC MICROBIOLOGY</style></publisher><pub-location><style face="normal" font="default" size="100%">1325 MASSACHUSETTS AVENUE, NW, WASHINGTON, DC 20005-4171 USA</style></pub-location><volume><style face="normal" font="default" size="100%">66</style></volume><pages><style face="normal" font="default" size="100%">925-929</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">The basidiomycete Marasmius quercophilus is commonly found during autumn on the decaying litter of the evergreen oak (Quercus ilex L.), a plant characteristic of Mediterranean forest. This white-rot fungus colonizes the leaf surface with rhizomorphs, causing a total bleaching of the leaf. In synthetic liquid media, this white-rot fungus has strong laccase activity. From a three-step chromatographic procedure, we purified a major isoform to homogeneity, The gene encodes a monomeric glycoprotein of approximately 63 kDa, with a 3.6 isoelectric point, that contains 12% carbohydrate, Spectroscopic analysis of the purified enzyme (UV/visible and electron paramagnetic resonance, atomic absorption) confirmed that it belongs to the ``blue copper oxidase{''} family. With syringaldazine as the substrate, the enzyme's pH optimum was 4.5, the optimal temperature was 75 degrees C, and the K-m was 7.1 mu M. The structural gene, lac1, was cloned and sequenced. This gene encodes a 517-amino-acid protein 99% identical to a laccase produced by PM1, an unidentified basidiomycete previously isolated from wastewater from a paper factory in Spain. This similarity may be explained by the ecological distribution of the evergreen oak in Mediterranean forest.</style></abstract><notes><style face="normal" font="default" size="100%">Keys: APS</style></notes><research-notes><style face="normal" font="default" size="100%">Keys: APS</style></research-notes></record></records></xml>