Purification of a novel low-molecular-mass laccase with HIV-1 reverse transcriptase inhibitory activity from the mushroom Tricholoma giganteum

Wang, H.X; Ng, Tzi Bun

doi:10.1016/j.bbrc.2004.01.064

Cited by 89 publications

(46 citation statements)

References 33 publications

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“…It is obviously too small for three domains, and considering that posttranslational modifications, such as glycosylation can increase the molecular weight, it could fall into the two-domain MCBP weight range. A low molecular-mass (43 kDa) laccase from a mushroom (Tricholoma giganteum) has also been isolated [129]. Another small dimeric laccase was isolated from a mushroom (Pleurotus eryngii) [130].…”

Section: Small Laccases In Fungismentioning

confidence: 98%

Function and molecular evolution of multicopper blue proteins

Nakamura

Gō

2005

Cell. Mol. Life Sci.

242

140

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Multicopper blue proteins (MCBPs) are multidomain proteins that utilize the distinctive redox ability of copper ions. There are a variety of MCBPs that have been roughly classified into three different groups, based on their domain organization and functions: (i) nitrite reductase-type with two domains, (ii) laccase-type with three domains, and (iii) ceruloplasmin-type with six domains. Together, the second and third group are often commonly called multicopper oxidases (MCOs). The rapid accumulation of genome sequence information in recent years has revealed several new types of proteins containing MCBP domains, mainly from bacteria. In this review, the recent research on the functions and structures of MCBPs is summarized, mainly focusing on the new types. The latter half of this review focusses on the two domain MCBPs, which we propose as the evolutionary intermediate of the MCBP family.

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Section: Small Laccases In Fungismentioning

confidence: 98%

Function and molecular evolution of multicopper blue proteins

Nakamura

Gō

2005

Cell. Mol. Life Sci.

242

140

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“…Twodomain laccases have been isolated from Botrytis cinerea [104] and from fresh fruiting bodies of Tricholoma giganteum [105]. The latter enzyme shows an N-terminal sequence with no homology to those of other mushroom laccases and is able to inhibit HIV-1 reverse transcriptase.…”

Section: Atypical Laccasesmentioning

confidence: 99%

Laccases: a never-ending story

Giardina¹,

Faraco²,

Pezzella³

et al. 2009

Cell. Mol. Life Sci.

866

638

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Laccases (benzenediol:oxygen oxidoreductases, EC 1.10.3.2) are blue multicopper oxidases that catalyze the oxidation of an array of aromatic substrates concomitantly with the reduction of molecular oxygen to water. In fungi, laccases carry out a variety of physiological roles during their life cycle. These enzymes are being increasingly evaluated for a variety of biotechnological applications due to their broad substrate range. In this review, the most recent studies on laccase structural features and catalytic mechanisms along with analyses of their expression are reported and examined with the aim of contributing to the discussion on their structure-function relationships. Attention has also been paid to the properties of enzymes endowed with unique characteristics and to fungal laccase multigene families and their organization.

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“…Raising the pH value above 4.0, or below 3.0, rapidly decreased laccase activity, indicating that G. lucidum laccase is relatively stable at pH 3.0 to 4.0 and has a narrow range of pH stability. (Halaburgi et al, 2011), Pleurotus eryngii (Wang and Ng, 2006a), Physisporinus rivulosus (Hildén et al, 2007), Tricholoma giganteum (Wang and Ng, 2004) and Pleurotus ostreatus (Liu et al, 2009). G. lucidum is an important member of the WRF and laccase from this species of fungi are currently used to decolorize some reactive dyes (Murugesan et al, 2009a); however, the production of thermostable laccase by G. lucidum has not received intensive investigation.…”

Section: Discussionmentioning

confidence: 99%

Production and characterization of thermostable laccase from the mushroom, Ganoderma lucidum, using submerged fermentation

Ding¹,

Lin²,

Chen³

et al. 2012

Afr. J. Microbiol. Res.

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Laccase production by the white rot fungus, Ganoderma lucidum, was investigated using submerged fermentation, and the laccase was purified and characterized. The effects of variations in the media nutrient composition or culture conditions and characteristics of purified laccase were provided for large scale production or industrial uses of the laccase. Low concentrations of glucose and yeast extract stimulated G. lucidum laccase production. The addition of lignocellulosic substrates to the media stimulated laccase production: pomelo peel induced the highest laccase activity of 11842.13 U/L and banana peel reduced laccase production, compared to control media containing wheat bran. Native PAGE and SDS PAGE demonstrated the presence of a single isoform with a molecular weight of 68 kDa. The optimum pH and temperature were 3.0 and 60°C, respectively. G. lucidum laccase is thermostable, with a residual activity of 46% after 80 min at 60°C. . The thermostable properties of the laccase produced by fermentation of G. lucidum in submerged culture had potential for industrial and biotechnology applications.

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Purification of a novel low-molecular-mass laccase with HIV-1 reverse transcriptase inhibitory activity from the mushroom Tricholoma giganteum

Cited by 89 publications

References 33 publications

Function and molecular evolution of multicopper blue proteins

Function and molecular evolution of multicopper blue proteins

Laccases: a never-ending story

Production and characterization of thermostable laccase from the mushroom, Ganoderma lucidum, using submerged fermentation

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