Publication: Isolation, characterization and function of laccase from Trichoderma
Issued Date
1992-11-01
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ISSN
14320614
01757598
01757598
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2-s2.0-0026448663
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Mahidol University
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SCOPUS
Bibliographic Citation
Applied Microbiology and Biotechnology. Vol.38, No.2 (1992), 198-202
Suggested Citation
Apinya Assavanig, Boonthum Amornikitticharoen, Nattapol Ekpaisal, Vithaya Meevootisom, Timothy William Flegel Isolation, characterization and function of laccase from Trichoderma. Applied Microbiology and Biotechnology. Vol.38, No.2 (1992), 198-202. doi:10.1007/BF00174468 Retrieved from: https://repository.li.mahidol.ac.th/handle/20.500.14594/22253
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Title
Isolation, characterization and function of laccase from Trichoderma
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Abstract
Of fourteen natural isolates of Trichoderma, no correlation was found between substrate weight loss and phenol oxidase (PO) activity in rice straw cultures. The highest PO producer from these laccase-positive strains was subjected to UV mutagenesis in order to select high and low PO activity mutants. There was no significant difference in substrate weight loss for mutant strains with six times higher and six times lower PO activity than the parent strain. Nor did the enzyme activity result in decreased growth inhibition by inhibitory phenolic compounds. PO enzyme from the parent Trichoderma and one of its high-PO-activity mutants was subsequently purified by ethanol precipitation from liquid cultures optimized by supplementation with copper sulphate and cycloheximide. Protein staining and activity staining of disc electrophoresis gels showed that only one PO enzyme of approximately 71 000 Da was produced. The enzyme could be defined as a laccase (benzenediol: oxygen oxidoreductase E.C. 1.10.3.2) because it catalysed the oxidation of syringaldazine and p-phenylenediamine in the absence of hydrogen peroxide, and because it was inhibited by cetyltrimethylammonium because but not by cinnamic acid. No specific in-vivo function could be assigned to this enzyme. © 1992 Springer-Verlag.