Cloning and Expression of a cDNA Encoding the Laccase from<i>Schizophyllum commune</i>

Hatamoto, Osamu; Sekine, Hiroshi; Nakano, E.; Abe, Keietsu

doi:10.1271/bbb.63.58

Cited by 53 publications

(29 citation statements)

References 18 publications

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“…In order to improve laccase production, fungal laccases have been expressed heterologously in Saccharomyces cerevisiae [48,49,[60][61][62][63], Trichoderma reesei [48,54,64], Aspergillus oryzae [65][66][67][68][69][70][71], Pichia pastoris [51,[72][73][74][75][76], Yarrowia lipolitica [77], Aspergillus sojae [78], Aspergillus niger [52,79], Aspergillus nidulans [69,79,80], Aspergillus ficuum [81], tobacco [82][83][84][85] and maize [86][87][88]. Bacterial laccases from B.…”

Section: Heterologous Production Of Laccasesmentioning

confidence: 99%

Laccases and Their Applications: A Patent Review

Kunamneni

Plou²,

Ballesteros³

et al. 2008

BIOT

278

172

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Abstract:Laccases are an interesting group of multi copper enzymes, which have received much attention of researchers in last decades due to their ability to oxidize both phenolic and non-phenolic lignin related compounds as well as highly recalcitrant environmental pollutants. This makes these biocatalysts very useful for their application in several biotechnological processes. Such applications include the detoxification of industrial effluents, mostly from the paper and pulp, textile and petrochemical industries, polymer synthesis, bioremediation of contaminated soils, wine and beverage stabilization. Laccases are also used as catalysts for the manufacture of anti-cancer drugs and even as ingredients in cosmetics. Recently, the utility of laccases has also been applied to nanobiotechnology. This paper reviews recent and important patents related to the properties, heterologous production, molecular cloning, and applications of laccases within different industrial fields as well as their potential extension to the nanobiotechnology area.

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Section: Heterologous Production Of Laccasesmentioning

confidence: 99%

Laccases and Their Applications: A Patent Review

Kunamneni

Plou²,

Ballesteros³

et al. 2008

BIOT

278

172

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“…21 These oxidases are involved in biotransformation and bioremediation processes, they can be also used in molecular genetics, 22 genetic expression, 23 genetic transcription 24 and cloning. 25 Consequently, laccases from white-rot fungi such as Pleurotus ostreatus are good candidates for further investigation, as they have potential in biosensor applications. Thus, some purified laccases [26][27][28][29][30] in combination with other enzymes have been used to prepare bienzymatic electrodes for the determination of phenolic compounds 26,27 and catecholamines.…”

Section: Introductionmentioning

confidence: 99%

Determination of catecholamines in pharmaceutical formulations using a biosensor modified with a crude extract of fungi laccase (Pleurotus ostreatus)

Leite¹,

Fatibello‐Filho²,

Barbosa-Dekker³

2003

J. Braz. Chem. Soc.

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Um biossensor de pasta de carbono modificado com extrato bruto enzimático do fungo Pleurotus ostreatus como fonte de lacase é proposto para a determinação de catecolaminas em formulações farmacêuticas. Essa enzima catalisa a oxidação de adrenalina ou dopamina nas quinonas correspondentes e a corrente obtida na redução eletroquímica de cada um dos produtos é relacionada a concentração dessas catecolaminas em solução da amostra. O efeito da concentração de lacase de 0,29 a 1,8 U/mg de pasta de carbono, do pH de 3,0 a 8,0, da velocidade de varredura de 10 a 40 mV s -1 e amplitudes de pulso de potencial de 10 a 60 mV sobre a resposta voltamétrica de pulso diferencial foi investigado. O desvio padrão relativo foi menor que 1,8% para solução de hidroquinona 2,8 x 10 -4 mol L -1 em pH 7 (n=10). Recuperações variando de 97,3 a 101% para adrenalina e de 95,8 a 102% para dopamina foram obtidas. As curvas analíticas foram lineares no intervalo de concentração de adrenalina de 6,0 x 10 -5 a 7,0 x 10 -4 mol L -1 e de 7,0 x 10 -5 a 4,0 x 10 -4 mol L -1 para dopamina, com limites de detecção de 7,9 x 10 -6 mol L -1 e 9,8 x 10 -6 mol L -1 , respectivamente. Esse biossensor foi empregado para a determinação de adrenalina e dopamina em formulações farmacêuticas. Os resultados obtidos com o biossensor para a determinação dessas catecolaminas em formulações farmacêuticas estão em concordância a um nível de confiança de 95% com o procedimento da Farmacopéia americana.A carbon paste biosensor modified with a crude enzymatic extract of the Pleurotus ostreatus fungi as a laccase source is proposed for catecholamine determination in pharmaceutical formulations. This enzyme catalyzes the oxidation of adrenaline or dopamine in the corresponding quinones and the current obtained in the electrochemical reduction of each of the products is related to the concentration of these catecholamines in the sample solution. The effect of the laccase concentration from 0.29 to 1.8 U/mg of carbon paste, pH from 3.0 to 8.0, scan rate from 10 to 40 mV s -1 and potential pulse amplitude from 10 to 60 mV on the differential pulse voltammetric response was investigated. The relative standard deviation was smaller than 1.8% for a 2.8 x 10 -4 mol L -1 hydroquinone solution at pH 7.0 (n=10). Recoveries varied from 97.3 to 101% for adrenaline and from 95.8 to 102% for dopamine. The analytical curves were rectilinear in the adrenaline concentration range from 6.0 x 10 -5 to 7.0 x 10 -4 mol L -1 and 7.0 x 10 -5 to 4.0 x 10 -4 mol L -1 for dopamine, with detection limits of 7.9 x 10 -6 mol L -1 and 9.8 x 10 -6 mol L -1 , respectively. This biosensor was used for adrenaline and dopamine determinations in pharmaceutical formulations. The results obtained using the proposed biosensor are in close agreement with those obtained using an American Pharmacopoeia procedure at a 95% confidence level. Keywords: laccase, Pleurotus ostreatus, catecholamines, biosensor IntroductionCatecholamines play an important role in the central nervous system as neurotransmitters. They als...

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“…A. oryzae has the ability to secrete large amounts of a wide range of different enzymes into its environment, and this characteristic has been used for commercial production of both recombinant enzyme and its own enzyme. Because of its high-level production of enzymes and high degree of safety, A. oryzae, as well as Aspergillus niger and Aspergillus sojae, has received increasing attention as a host for homologous (5,11) and heterologous (15) protein production. Many recombinant proteins have been produced in submerged culture for easy cultivation.…”

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confidence: 99%

Proteomic Analysis of Extracellular Proteins from Aspergillus oryzae Grown under Submerged and Solid-State Culture Conditions

Oda

Kakizono

Iefuji

et al. 2006

Appl Environ Microbiol

242

147

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Filamentous fungi are widely used for the production of homologous and heterologous proteins. Recently, there has been increasing interest in Aspergillus oryzae because of its ability to produce heterologous proteins in solid-state culture. To provide an overview of protein secretion by A. oryzae in solid-state culture, we carried out a comparative proteome analysis of extracellular proteins in solid-state and submerged (liquid) cultures. Extracellular proteins prepared from both cultures sequentially from 0 to 40 h were subjected to twodimensional electrophoresis, and protein spots at 40 h were identified by peptide mass fingerprinting using matrix-assisted laser desorption ionization-time-of-flight mass spectrometry. We also attempted to identify cell wall-bound proteins of the submerged culture. We analyzed 85 spots from the solid-state culture and 110 spots from the submerged culture. We identified a total of 29 proteins, which were classified into 4 groups. Group 1 consisted of extracellular proteins specifically produced in the solid-state growth condition, such as glucoamylase B and alanyl dipeptidyl peptidase. Group 2 consisted of extracellular proteins specifically produced in the submerged condition, such as glucoamylase A (GlaA) and xylanase G2 (XynG2). Group 3 consisted of proteins produced in both conditions, such as xylanase G1. Group 4 consisted of proteins that were secreted to the medium in the solid-state growth condition but trapped in the cell wall in the submerged condition, such as ␣-amylase (TAA) and ␤-glucosidase (Bgl). A Northern analysis of seven genes from the four groups suggested that the secretion of TAA and Bgl was regulated by trapping these proteins in the cell wall in submerged culture and that secretion of GlaA and XynG2 was regulated at the posttranscriptional level in the solid-state culture.

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Cloning and Expression of a cDNA Encoding the Laccase fromSchizophyllum commune

Cited by 53 publications

References 18 publications

Laccases and Their Applications: A Patent Review

Laccases and Their Applications: A Patent Review

Determination of catecholamines in pharmaceutical formulations using a biosensor modified with a crude extract of fungi laccase (Pleurotus ostreatus)

Proteomic Analysis of Extracellular Proteins from Aspergillus oryzae Grown under Submerged and Solid-State Culture Conditions

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