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      <ref-type name="Journal Article">17</ref-type>
      <contributors>
        <authors>
          <author>P. Sofia</author>
          <author>M. Asgher</author>
          <author>M. Shahid</author>
          <author>M. A. Randhawa</author>
        </authors>
      </contributors>
      <titles>
        <title>CHITOSAN BEADS IMMOBILIZED SCHIZOPHYLLUM COMMUNE IBL-06 LIGNIN PEROXIDASE WITH NOVEL THERMO STABILITY, CATALYTIC AND DYE REMOVAL PROPERTIES</title>
        <secondary-title>Journal of Animal and Plant Sciences</secondary-title>
        <alt-title>JAPS</alt-title>
      </titles>
      <dates><year>2016</year><pub-dates><date>2016/10/01</date></pub-dates></dates>
      <volume>26</volume>
      <number>5</number>
      <pages>1451-1463</pages>
      <isbn>1018-7081</isbn>
      <electronic-resource-num>NA</electronic-resource-num>
      <abstract>&lt;p&gt;The lignin mineralizing enzymes system of white rot fungi has tremendous catalytic prospect for oxidative bioremediation of a number of toxic pollutants and many other industrial uses. Immobilization enables the reuse of enzymes and making them industrially relevant and economical biocatalysts.&amp;nbsp;&lt;em&gt;Schizophyllum commune&amp;nbsp;&lt;/em&gt;IBL-06 was cultivated for the secretion of lignin peroxidase (LiP) in pre-optimized solid state fermentation medium of corn stover. A high yield of lignin peroxidase (1347.3 U/mL) was recorded in crude culture supernatant. LiP was purified (5.65 folds) by a pre-standardized four step protocol comprising ammonium sulphate fractionation, dialysis, DEAE cellulose ion exchange and Sephadex G-100 column chromatography. The 38 kDa single polypeptide&amp;nbsp;&lt;em&gt;S. commune&amp;nbsp;&lt;/em&gt;IBL-06 LiP migrating as a single clear band on both native and SDS-PAGE gels. The purified enzyme was then immobilized on chitosan beads activated with gluteraldehyde (cross-linker).Scanning electron microscopy (SEM) was conducted for the confirmation of LiP attachment on chitosan beads. The highest textile dye decolorization (95.45%) potential was observed with chitosan-immobilized enzyme at 30&amp;deg;C without hemolytic toxicity. The chitosan beads-LiP retained approximately more than 70% activity after three repeated runs that gradually decreased to 35 % after 7th cycle of reusability. The immobilized LiP was found to show superior dye removal properties as compared to free LiP. Higher thermo stability, lower K&lt;em&gt;m&lt;/em&gt;and high V&lt;em&gt;max&amp;nbsp;&lt;/em&gt;features of chitosan beads immobilizedLiP suggested its suitibility for variousbiotechnological and industrial applictaions.&lt;/p&gt;</abstract>
      <keywords><keyword>Schizophyllum commune IBL-06, lignin peroxidase, chitosan beads immobilization, characterization, dye decolorization</keyword></keywords>
      <publisher>Pakistan Agricultural Scientists Forum</publisher>
      <urls><related-urls><url>https://thejaps.org.pk/AbstractView.aspx?mid=2016-JAPS-191</url></related-urls></urls>
    </record>
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