Co-occurrence of the Multicopper Oxidases Tyrosinase and Laccase in Lichens in Sub-order Peltigerineae

Laufer, Zsanett; Beckett, Richard P.; Minibayeva, Farida

doi:10.1093/aob/mcl184

Cited by 40 publications

(43 citation statements)

References 20 publications

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“…The effect of detergents on immobilized laccase was not reported earlier. In contrast to earlier studies reported on free enzymes (Laufer et al 2006;Sharma et al 2013), SDS decreased the enzymatic activity of immobilized laccase at concentrations higher than 2 mM. This study for the first time demonstrates the effect of detergents on immobilized laccase.…”

Section: Effect Of Detergentscontrasting

confidence: 88%

Assessing the tolerance of immobilized laccase from a salt-tolerant strain of Trichoderma viride Pers NFCCI-2745 to heavy metal ions, detergents and copper chelating agents

Divya

Prasanth

Sadasivan

2014

Int. J. Environ. Sci. Technol.

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The biotreatment of industrial effluents that contain heavy metals, detergents and metal chelating agents represents a great concern to industries as these compounds are either toxic to microbes or they act as noncompetitive inhibitors/denaturing agents for several enzymes. So, it is essential to know the effect of various agents usually present in the treatment plant on activity of the enzyme, for extending its applications in in situ treatment processes. This study describes the immobilization conditions of laccase and analysis of the sensitivity of immobilized laccase from Trichoderma viride Pers NFCCI-2745 to heavy metals, detergent and copper chelating agents. The concentrations and combinations of cations influenced the activity of immobilized enzyme and its yield. The immobilized Cu-Ba alginate enzyme showed comparatively higher activity compared to the Cu-alginate enzyme. Most of the metal ions tested enhanced laccase activity at lower concentration. Immobilized laccase retained more than 70 % of its activity even in the presence of 20 mM copper chelating agents like EDTA and sodium thioglycolic acid. Sodium azide, on the other hand, inhibited 80 % of the activity of all the beads even at a very low concentration of 0.5 mM. Cu-Ba and Cu-Ni alginate enzyme exhibited comparatively higher tolerance than Cualginate beads to EDTA and sodium thioglycolate. Tween 20 and cetyl trimethyl ammonium bromide significantly increased the activity of all the beads. These properties of the immobilized laccase may be aptly considered and suitably utilized in treating phenolic effluents that may contain heavy metals, detergents and certain copper chelating agents which may otherwise pose a threat to enzymatic activity.

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Section: Effect Of Detergentscontrasting

confidence: 88%

Assessing the tolerance of immobilized laccase from a salt-tolerant strain of Trichoderma viride Pers NFCCI-2745 to heavy metal ions, detergents and copper chelating agents

Divya

Prasanth

Sadasivan

2014

Int. J. Environ. Sci. Technol.

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“…from Collema, which lost more than 90% of their activity following extraction and the first chromatographic purification step (Q Sepharose; data not shown). Enzyme breakdown during extraction may be responsible for the low peroxidase activities reported in our earlier work on Peltigeralean lichens (Laufer et al, 2006a), and actual activities in intact thalli may be much higher. The strong ability of intact thalli from a range of lichen families to metabolize H 2 O 2 (Beckett and Minibayeva, 2007) suggests that peroxidase activity may be higher than indicated by activities present in crude extracts.…”

Section: Discussionmentioning

confidence: 66%

“…The presence of specific oxidoreductases was tested electrophoretically in crude extracts of the thalli of L. saturninum as described by Laufer et al (2006a). A modified method of Laemmli (1970) was followed using SDS-and native PAGE (10 and 12%, Invitrogen, Karlsruhe, Germany).…”

Section: Electrophoretic Studiesmentioning

confidence: 99%

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A heme peroxidase of the ascomyceteous lichen Leptogium saturninum oxidizes high-redox potential substrates

Liers

Ullrich

Hofrichter

et al. 2011

Fungal Genetics and Biology

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“…The activities of the enzyme for 2,6-dimethoxyphenol (39), guaiacol (7), syringaldazine (19), ABTS (12), 3,4-dimethoxybenzyl alcohol (8), resorcinol (35), catechol (33), pyrogallol (16), vanillic acid (38), hydroquinone (25), 4-methoxyphenol (25), 4-aminophenol (25), L-DOPA (18), and L-tyrosine (30) were spectrophotometrically estimated.…”

Section: Chemicalsmentioning

confidence: 99%

Purification, Characterization, and Gene Cloning ofCeriporiopsissp. Strain MD-1 Peroxidases That Decolorize Human Hair Melanin

Nagasaki

Kumazawa

Murakami

et al. 2008

Appl Environ Microbiol

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Ceriporiopsis sp. strain MD-1, isolated from forest soil, produced several extracellular enzymes that decolorized human hair melanin. Among them, three enzymes (E1, E2-1, and E2-2) were purified to homogeneity and characterized. The enzymes required hydrogen peroxide in their enzyme reactions and, typical of other fungal peroxidases, oxidized various phenol compounds such as guaiacol, but not 3,4-dimethoxybenzyl alcohol. The spectra of the three enzymes showed an absorption maximum at 406 nm, indicating that they were heme proteins. However, the A 406 /A 280 values of the enzymes were below 0.4, which was lower than those of other peroxidases. E2-1 and E2-2 were similar to each other in their molecular and catalytic properties, and they possibly represent products of posttranslational modifications and/or allelic variants of the same gene, mdcA. The corresponding cDNA was cloned and sequenced; the deduced amino acid sequence showed high identities to the manganese peroxidases from other microorganisms. The specific activities and K m values of E2-1 and E2-2 for synthetic and human hair melanins were much higher than those of Phanerochaete chrysosporium manganese peroxidase and lignin peroxidase.

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Co-occurrence of the Multicopper Oxidases Tyrosinase and Laccase in Lichens in Sub-order Peltigerineae

Abstract: Cell walls of lichens in sub-order Peltigerineae have much higher activities and a greater diversity of cell wall redox enzymes compared with other lichens. Possible roles of tyrosinases include melanization, removal of toxic phenols or quinones, and production of herbivore deterrents.

Cited by 40 publications

References 20 publications

Assessing the tolerance of immobilized laccase from a salt-tolerant strain of Trichoderma viride Pers NFCCI-2745 to heavy metal ions, detergents and copper chelating agents

Assessing the tolerance of immobilized laccase from a salt-tolerant strain of Trichoderma viride Pers NFCCI-2745 to heavy metal ions, detergents and copper chelating agents

A heme peroxidase of the ascomyceteous lichen Leptogium saturninum oxidizes high-redox potential substrates

Purification, Characterization, and Gene Cloning ofCeriporiopsissp. Strain MD-1 Peroxidases That Decolorize Human Hair Melanin

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