Diversity of laccases from lichens in suborder Peltigerineae

Laufer, Zsanett; Beckett, Richard P.; Minibayeva, Farida; Lüthje, Sabine; Böttger, Michael

doi:10.1639/0007-2745-112.2.418

Cited by 26 publications

(19 citation statements)

References 22 publications

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“…40 and 80 kDa), similar to the behavior of lichen laccases (Lisov et al, 2007;Laufer et al, 2009). Also in crude extracts of thalli from two further Peltigerales lichens monomeric and dimeric laccases (88 & 158 kDa for C. flaccidum) as well as peroxidase (39 & 82 kDa as well as 36 & 47 kDa for C. flaccidum and P. canina, respectively) were electrophoretically identified (data not shown).…”

Section: Discussionsupporting

confidence: 58%

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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Section: Discussionsupporting

confidence: 58%

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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“…1.10.3.2.) are extracellular, multicopper oxidases widely distributed in fungi, higher plants, bacteria, lichens and insects [1-3]. They contain a T1 copper atom at which the reducing substrate is oxidized and a trinuclear copper cluster at which oxygen is reduced to water [4].…”

Section: Introductionmentioning

confidence: 99%

Functional expression of a blood tolerant laccase in Pichia pastoris

et al. 2013

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BackgroundBasidiomycete high-redox potential laccases (HRPLs) working in human physiological fluids (pH 7.4, 150 mM NaCl) arise great interest in the engineering of 3D-nanobiodevices for biomedical uses. In two previous reports, we described the directed evolution of a HRPL from basidiomycete PM1 strain CECT 2971: i) to be expressed in an active, soluble and stable form in Saccharomyces cerevisiae, and ii) to be active in human blood. In spite of the fact that S. cerevisiae is suited for the directed evolution of HRPLs, the secretion levels obtained in this host are not high enough for further research and exploitation. Thus, the search for an alternative host to over-express the evolved laccases is mandatory.ResultsA blood-active laccase (ChU-B mutant) fused to the native/evolved α-factor prepro-leader was cloned under the control of two different promoters (PAOX1 and PGAP) and expressed in Pichia pastoris. The most active construct, which contained the PAOX1 and the evolved prepro-leader, was fermented in a 42-L fed-batch bioreactor yielding production levels of 43 mg/L. The recombinant laccase was purified to homogeneity and thoroughly characterized. As happened in S. cerevisiae, the laccase produced by P. pastoris presented an extra N-terminal extension (ETEAEF) generated by an alternative processing of the α-factor pro-leader at the Golgi compartment. The laccase mutant secreted by P. pastoris showed the same improved properties acquired after several cycles of directed evolution in S. cerevisiae for blood-tolerance: a characteristic pH-activity profile shifted to the neutral-basic range and a greatly increased resistance against inhibition by halides. Slight biochemical differences between both expression systems were found in glycosylation, thermostability and turnover numbers.ConclusionsThe tandem-yeast system based on S. cerevisiae to perform directed evolution and P. pastoris to over-express the evolved laccases constitutes a promising approach for the in vitro evolution and production of these enzymes towards different biocatalytic and bioelectrochemical applications.

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“…In addition to copper minerals and copper lichen acid complexes, copper could also be complexed organically in a laccase or tyrosinase as in the Peltigerineae (Laufer et al 2009). In addition to copper minerals and copper lichen acid complexes, copper could also be complexed organically in a laccase or tyrosinase as in the Peltigerineae (Laufer et al 2009).…”

Section: Discussionmentioning

confidence: 99%

Copper localization, elemental content, and thallus colour in the copper hyperaccumulator lichenLecanora sierraefrom California

2011

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An unusual dark blue-green lichen, Lecanora sierrae, was discovered over 30 years ago by Czehura near copper mines in the Lights Creek District, Plumas County, Northern California. Using atomic absorption spectroscopy, Czehura found that dark green lichen samples from Warren Canyon contained 4% Cu in ash and suggested that its colour was due to copper accumulation in the cortex. The present study addressed the hypothesis that the green colour in similar material we sampled from Warren Canyon in 2008, is caused by copper localization in the thallus. Optical microscopy and electron microprobe analysis of specimens of L. sierrae confirmed that copper localization took place in the cortex. Elemental analyses of L. sierrae and three other species from the same localities showed high enrichments of copper and selenium, suggesting that copper selenates or selenites might occur in these lichens and be responsible for the unusual colour.

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Diversity of laccases from lichens in suborder Peltigerineae

Cited by 26 publications

References 22 publications

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

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

Functional expression of a blood tolerant laccase in Pichia pastoris

Copper localization, elemental content, and thallus colour in the copper hyperaccumulator lichenLecanora sierraefrom California

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