Purification and immobilization of laccase from Trichoderma harzianum strain HZN10 and its application in dye decolorization.
Ontology highlight
ABSTRACT: In this study we report the purification of laccase produced by Trichoderma harzianum strain HZN10 (using wheat bran under solid state fermentation) and its application in decolorization of synthetic dyes. Extracellular laccase was purified to homogeneity by DEAE-Sepharose and Sephadex G-100 chromatography with specific activity of 162.5 U/mg and 25-fold purification. Purified laccase was immobilized in various entrapments like calcium alginate, copper alginate, calcium alginate-chitosan beads and sol-gel matrix. Optimization results revealed that the laccase immobilized in sol-gel was optimally active in wide pH range (4.0-7.0) and thermo-stable (50-70 °C) than free enzyme which was optimum at 50 °C and pH 6.0. Kinetic analysis showed K m of 0.5 mM and 2.0 mM and
SUBMITTER: Bagewadi ZK
PROVIDER: S-EPMC6296572 | biostudies-literature | 2017 Jun
REPOSITORIES: biostudies-literature
ACCESS DATA