Purification and characterization of a thermostable laccase from the ascomycetes Cladosporium cladosporioides and its applications

Halaburgi, Vijaykumar M.; Sharma, Sujata; Sinha, Mau; Singh, T.P.; Karegoudar, T. B.

doi:10.1016/j.procbio.2011.02.002

Cited by 96 publications

(59 citation statements)

References 33 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…After the addition of Phragmites australis stem powder into the culture medium as nutrient, laccase production (6.5 U/mL) was dramatically increased than that of cultivation without any supplement (1.8 U/mL). This laccase production level was comparable to a few previous studies using optimized culture media, e.g., 4.16 U/mL from Cladosporium cladosporioides (Halaburgi et al 2011).…”

Section: Resultssupporting

confidence: 87%

Simultaneous Laccase Production and Color Removal by Culturing Fungus Pycnoporus sp. SYBC-L3 in a Textile Wastewater Effluent Supplemented with a Lignocellulosic Waste Phragmites australis

Liu

Cai

Liao

et al. 2012

Bull Environ Contam Toxicol

View full text Add to dashboard Cite

We conducted experiments to culture Pycnoporus sp. SYBC-L3 in a medium comprising an industrial waste (dye-containing textile effluent) and a lignocellulosic waste (Phragmites australis) that achieved laccase production while having the color removed from the wastewater. Our experimental results showed that the fungus grew well in liquid submerged cultivation with the diluted textile effluent as the sole culture medium, but relatively low extracellular laccase activity (1.8 U/mL) was produced. Addition of the lignocellulosic biomass enhanced laccase production and color removal. The highest laccase activity was found to be 6.5 U/mL in the presence of Phragmites australis stem. Under this condition, 70 % color removal occurred in the culture medium. This study provided an alternative novel scheme to remove color in textile wastewater while having an economic value added by producing laccase.

show abstract

Section: Resultssupporting

confidence: 87%

Simultaneous Laccase Production and Color Removal by Culturing Fungus Pycnoporus sp. SYBC-L3 in a Textile Wastewater Effluent Supplemented with a Lignocellulosic Waste Phragmites australis

Liu

Cai

Liao

et al. 2012

Bull Environ Contam Toxicol

View full text Add to dashboard Cite

show abstract

“…Many reports have shown that the optimal pH for laccase varies when different substrates are used (Table 2); however, using ABTS as a substrate many laccase enzymes exhibit an optimal catalytic pH value in the acidic range (Halaburgi et al, 2011;Wang and Ng, 2006b), which is consistent with this study as the optimal pH was 3.0. 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.…”

Section: Discussionsupporting

confidence: 89%

“…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.

View full text Add to dashboard Cite

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.

show abstract

“…The similar phenomenon was also found in the laccases from Cladosporium cladosporioides and Pycnoporus sp. [17,26], whereas the thermostable laccase from Polyporus sp. was promoted by 4.0 mM of Mg 2+ , Mn 2+ , Zn 2+ , and Ca 2+ [38].…”

Section: Discussionmentioning

confidence: 99%

Production of a thermostable metal-tolerant laccase from Trametes versicolor and its application in dye decolorization

Zhang

Cao

et al. 2011

Biotechnol Bioproc E

View full text Add to dashboard Cite

Production of laccase using a submerged culture of Trametes versicolor sdu-4 was optimized using a central composite design of the Response Surface Methodology. Optimized conditions gave a laccase yield of 4,213 U/L which was approximately three times of that in basal medium. The laccase was purified to homogeneity using a three-step process. The overall yield of the purification was 58%, with a purification fold of 11.4 and a specific activity of 1320.7 U/mg protein. The molecular mass of the laccase was 60 kDa. The optimum pH values of the enzyme were 2.2, 3.7, and 7 for the oxidations of ABTS, DMP, and syringaldazine, respectively. The enzyme had adaptability to a broad pH range and high temperature and wsa stable at pH 3.0 ~ 10.0. The half-life of this laccase at 70°C was 2.2 h. Methyl red, 2-bromophenol, and 4-bromophenol were oxidized by the purified laccase in the absence of mediators. Purified laccase was effective in the decolorization of several dyes and was not inhibited by Cu 2+ , Mn 2+ , Zn 2+ , Na + , K + , Mg 2+ , Ba 2+ , and Ca 2+ at 5 mM. These excellent characteristics made it a highly attractive candidate for industrial use.

show abstract

Purification and characterization of a thermostable laccase from the ascomycetes Cladosporium cladosporioides and its applications

Cited by 96 publications

References 33 publications

Simultaneous Laccase Production and Color Removal by Culturing Fungus Pycnoporus sp. SYBC-L3 in a Textile Wastewater Effluent Supplemented with a Lignocellulosic Waste Phragmites australis

Simultaneous Laccase Production and Color Removal by Culturing Fungus Pycnoporus sp. SYBC-L3 in a Textile Wastewater Effluent Supplemented with a Lignocellulosic Waste Phragmites australis

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

Production of a thermostable metal-tolerant laccase from Trametes versicolor and its application in dye decolorization

Contact Info

Product

Resources

About