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            <title xml:lang="en">Differential patterns of activity displayed by two exo-beta-1,3-glucanases associated with the Aspergillus fumigatus cell wall.</title>
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                <forename type="first">Thierry</forename>
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                <forename type="first">Robbert P.</forename>
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            <idno type="halRefHtml">&lt;i&gt;Journal of Bacteriology&lt;/i&gt;, 1997, 179 (10), pp.3154-63. &lt;a target="_blank" href="https://dx.doi.org/10.1128/jb.179.10.3154-3163.1997"&gt;&amp;#x27E8;10.1128/jb.179.10.3154-3163.1997&amp;#x27E9;&lt;/a&gt;</idno>
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                <title xml:lang="en">Differential patterns of activity displayed by two exo-beta-1,3-glucanases associated with the Aspergillus fumigatus cell wall.</title>
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                    <forename type="first">Thierry</forename>
                    <surname>Fontaine</surname>
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                    <surname>Hartland</surname>
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                    <forename type="first">Michel</forename>
                    <surname>Diaquin</surname>
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                  <affiliation ref="#struct-19607"/>
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                    <surname>Simenel</surname>
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                    <forename type="first">Jean-Paul</forename>
                    <surname>Latgé</surname>
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                <title level="j">Journal of Bacteriology</title>
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                  <publisher>American Society for Microbiology</publisher>
                  <biblScope unit="volume">179</biblScope>
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              <classCode scheme="mesh">Aspergillus fumigatus</classCode>
              <classCode scheme="mesh">Cations, Divalent</classCode>
              <classCode scheme="mesh">Glucose</classCode>
              <classCode scheme="mesh">Hydrogen-Ion Concentration</classCode>
              <classCode scheme="mesh">Hydrolysis</classCode>
              <classCode scheme="mesh">Kinetics</classCode>
              <classCode scheme="mesh">Metals</classCode>
              <classCode scheme="mesh">Molecular Weight</classCode>
              <classCode scheme="mesh">Polysaccharides</classCode>
              <classCode scheme="mesh">Substrate Specificity</classCode>
              <classCode scheme="mesh">Temperature</classCode>
              <classCode scheme="mesh">beta-Glucosidase</classCode>
              <classCode scheme="mesh">Cell Wall</classCode>
              <classCode scheme="mesh">Enzyme Activation</classCode>
              <classCode scheme="mesh">Glucan 1,3-beta-Glucosidase</classCode>
              <classCode scheme="halDomain" n="sdv.mp">Life Sciences [q-bio]/Microbiology and Parasitology</classCode>
              <classCode scheme="halTypology" n="ART">Journal articles</classCode>
              <classCode scheme="halOldTypology" n="ART">Journal articles</classCode>
              <classCode scheme="halTreeTypology" n="ART">Journal articles</classCode>
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              <p>Two exo-beta-1,3-glucanases (herein designated exoG-I and exoG-II) were isolated from the cell wall autolysate of the filamentous fungus Aspergillus fumigatus and purified by ion-exchange, hydrophobic-interaction, and gel filtration chromatographies. Molecular masses estimated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and gel filtration chromatography were 82 kDa for the monomeric exoG-I and 230 kDa for the dimeric exoG-II. exoG-I and exoG-II were glycosylated, and N glycans accounted, respectively, for 2 and 44 kDa. Their pH optimum is 5.0. Their optimum temperatures are 55 degrees C for exoG-I and 65 degrees C for exoG-II. By a sensitive colorimetric method and high-performance anion-exchange chromatography for product analysis, two patterns of exo-beta-1,3-glucanase activities were found. The 230-kDa exoG-II enzyme acts on p-nitrophenyl-beta-D-glucoside, beta-1,6-glucan, and beta-1,3-glucan. This activity, which retains the anomeric configuration of glucose released, presented a multichain pattern of attack of the glucan chains and a decrease in the maximum initial velocity (Vm) with the increasing size of the substrate. In contrast, the 82-kDa exoG-I, which inverts the anomeric configuration of the glucose released, hydrolyzed exclusively the beta-1,3-glucan chain with a minimal substrate size of 4 glucose residues. This enzyme presented a repetitive-attack pattern, characterized by an increase in Vm with an increase in substrate size and by a degradation of the glucan chain until it reached laminaritetraose, the limit substrate size. The 82-kDa exoG-I and 230-kDa exoG-II enzymes correspond to a beta-1,3-glucan-glucohydrolase (EC 3.2.1.58) and to a beta-D-glucoside-glucohydrolase (EC 3.2.1.21), respectively. The occurrence and functions of these two classes of exo-beta-1,3-glucanases in other fungal species are discussed.</p>
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          <date type="start">2000-06-09</date>
          <date type="end">2018-10-31</date>
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