Characterization of a Coprinus cinereus laccase

Schneider, Palle; Caspersen, Mikael B.; Mondorf, K; Halkier, Torben; Skov, L.K.; Østergaard, Per; Brown, Kimberly M.; Brown, Stephen H.M.; Xu, Feng

doi:10.1016/s0141-0229(99)00085-x

Cited by 132 publications

(64 citation statements)

References 30 publications

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“…L. sordida laccase presented highest activity at pH 3.5, with a second activity peak at pH 6.0. These data are consistent with other studies showing optima pH values for other fungal species, like Pycnoporus cinnabarinus (pH 4.0) (7), Lentinula edodes (pH 4.0) (5) and Coprinus cinereus (4.0) (25). The two activity peaks detected suggest the presence of an isozyme or indicate that this laccase presents two distinct pH optima, like observed in Agaricus bisporus (32) and Monocillium saxena (28).…”

supporting

confidence: 92%

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Laccase production by Lepista sordida

Cavallazzi¹,

Oliveira²,

Kasuya³

2004

Braz. J. Microbiol.

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supporting

confidence: 92%

“…The Km app was 101.6 µM and Vmax app was 0.84 µM.s -1 . Similar values were found in other fungal laccases (11,20,24,25). It can be observed in Fig.…”

supporting

confidence: 89%

Laccase production by Lepista sordida

Cavallazzi¹,

Oliveira²,

Kasuya³

2004

Braz. J. Microbiol.

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“…The parameters K m and k cat for both laccases were very similar. When compared to other laccases, M. albomyces laccase has a rather high K m value (0?28 mM) for the nonphenolic ABTS, as K m values around 0?03-0?05 mM have been observed for most fungal laccases Chefetz et al, 1998;Garzillo et al, 1998;Schneider et al, 1999;Record et al, 2002). On the other hand, the K m values for the phenolic 2,6-DMP (0?005 mM) and syringaldazine (0?003 mM) were very low, indicating that phenolic compounds are better substrates for M. albomyces laccase than the commonly used ABTS.…”

Section: Discussionmentioning

confidence: 97%

Expression of Melanocarpus albomyces laccase in Trichoderma reesei and characterization of the purified enzyme

et al. 2004

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Previous studies on Melanocarpus albomyces laccase have shown that this enzyme is very interesting for both basic research purposes and industrial applications. In order to obtain a reliable and efficient source for this laccase, it was produced in the filamentous fungus Trichoderma reesei. Two approaches were used: production of a non-fused laccase and a hydrophobin-laccase fusion protein. Both proteins were expressed in T. reesei under the cbh1 promoter, and significantly higher activities were obtained with the non-fused laccase in shake-flask cultures (corresponding to about 230 mg l "1 ). Northern blot analyses showed rather similar mRNA levels from both expression constructs. Western analysis indicated intracellular accumulation and degradation of the hydrophobin-laccase fusion protein, showing that production of the fusion was limited at the post-transcriptional level. No induction of the unfolded protein response pathway by laccase production was detected in the transformants by Northern hybridization. The most promising transformant was grown in a fermenter in batch and fed-batch modes. The highest production level obtained in the fed-batch culture was 920 mg l "1 . The recombinant laccase was purified from the culture supernatant after cleaving the major contaminating protein, cellobiohydrolase I, by papain. The recombinant and wild-type laccases were compared with regard to substrate kinetics, molecular mass, pH optimum, thermostability, and processing of the N-and C-termini, and they showed very similar properties.

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“…Botrytis cinerea laccase (BcL) (22), Coprinus cinereus laccase-1 (CcL) (30), Myceliophthora thermophila laccase (MtL) (5), Myrothecium verrucaria bilirubin oxidase (MvBO) (39), Pycnoporus cinnabarinus laccase (PcL) (22), Rhizoctonia solani laccase 4 (RsL) (34), Scytalidium thermophilum laccase (StL) (39), and Trametes villosa (Polyporus pinsitus) laccase 1 (TvL) (40) were purified as previously reported. Violuric acid (VA) and 1-hydroxybenzotriazole (HBT) were purchased from Aldrich.…”

Section: Methodsmentioning

confidence: 99%

Redox Chemistry in Laccase-Catalyzed Oxidation of N-Hydroxy Compounds

Kulys

Duke

et al. 2000

Appl Environ Microbiol

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271

165

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1-Hydroxybenzotriazole, violuric acid, and N-hydroxyacetanilide are three N-OH compounds capable of mediating a range of laccase-catalyzed biotransformations, such as paper pulp delignification and degradation of polycyclic hydrocarbons. The mechanism of their enzymatic oxidation was studied with seven fungal laccases. The oxidation had a bell-shaped pH-activity profile with an optimal pH ranging from 4 to 7. The oxidation rate was found to be dependent on the redox potential difference between the N-OH substrate and laccase. A laccase with a higher redox potential or an N-OH compound with a lower redox potential tended to have a higher oxidation rate. Similar to the enzymatic oxidation of phenols, phenoxazines, phenothiazines, and other redox-active compounds, an "outer-sphere" type of single-electron transfer from the substrate to laccase and proton release are speculated to be involved in the rate-limiting step for N-OH oxidation.Laccases (EC 1.10.3.2) are multi-Cu oxidases that can catalyze the oxidation of a range of reducing substances with the concomitant reduction of O 2 (for recent reviews, see reference 24 and references therein). Because of their capability of catalyzing the oxidation of aromatic compounds, laccases are receiving increasing attention as potential industrial enzymes in various applications, such as pulp delignification, wood fiber modification, dye or stain bleaching, chemical or medicinal synthesis, and contaminated water or soil remediation (15, 37).Laccases contain one type 1 (T1) Cu center, one type 2 (T2) Cu center, and one type 3 (T3) Cu center. The T2 and T3 sites form a trinuclear Cu cluster onto which O 2 is reduced. The T1 Cu oxidizes the reducing substrate and transfers electrons to the T2 and T3 Cu. Laccase is able to oxidize certain phenols with E 0 values higher than its own (0.5 to 0.8 V versus the normal hydrogen electrode [NHE]) (36). However, many inorganic and organic compounds with comparable E 0 values (such as 1,2,3,5-tetramethoxybenzene [18]) are not laccase substrates due to unfavorable kinetics. Under certain conditions, however, these compounds can be indirectly oxidized by laccase through the mediation of small, redox-active laccase substrates. 2,2Ј-Azinobis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) was the first compound found capable of efficiently mediating the laccase oxidation of high-E 0 , nonsubstrate lignin model compounds (such as veratryl alcohol and nonphenolic lignin model dimers) (8). Based on product structure analysis, it has been proposed that laccase-oxidized ABTS can abstract an H atom from the lignin model compounds, leading to indirect laccase catalysis upon the oxidation of the compounds (25). To date, other types of mediators, particularly phenoxazines and N-OH compounds, also have been recognized for their mediation function in laccase catalysis (1, 6,17,29).Mediated laccase catalysis has been applied to a wide range of applications, such as pulp delignification (9, 10, 12, 22, 32), textile dye bleaching (31), polycyclic aromatic h...

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Characterization of a Coprinus cinereus laccase

Cited by 132 publications

References 30 publications

Laccase production by Lepista sordida

Laccase production by Lepista sordida

Expression of Melanocarpus albomyces laccase in Trichoderma reesei and characterization of the purified enzyme

Redox Chemistry in Laccase-Catalyzed Oxidation of N-Hydroxy Compounds

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