Purification, characterization, and cloning of an extracellular laccase with potent dye decolorizing ability from white rot fungus Cerrena unicolor GSM-01

Wang, Shanshan; Ning, Ying-Jie; Wang, Shou-Nan; Zhang, Jing; Zhang, Guoqing; Chen, Qingjun

doi:10.1016/j.ijbiomac.2016.10.079

Cited by 57 publications

(34 citation statements)

References 51 publications

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“…Similar activation of fungal laccases by Mn 2+ has been reported for laccases from the ascomycete Cladosporium cladosporioides and the basidiomycete S. carnis CPF-05 [24,26], while an important inhibitory effect was reported in presence of Mn 2+ at 1-10 mM in other studies [7,40]. In presence of 10 mM Zn 2+ and Mn 2+ , TaLac1 showed higher activity compared to that obtained by Cerrena unicolor GSM-01 laccase [2]. Moreover, there was inactivation of TaLac1 by more than 10 mM Cu 2+ , which is consistent with many reports showing the inhibitory effect associated with the increase of Cu 2+ in the reactions [26,41].…”

Section: Accepted Manuscriptsupporting

confidence: 81%

“…A C C E P T E D M A N U S C R I P T 4 as textile dye decolorization, pulp bleaching, detoxification and bioremediation of environmental pollutants and delignification or second generation ethanol production [2,4,5,6].…”

Section: Accepted Manuscriptmentioning

confidence: 99%

“…During last years a wide number of studies have focused on lignolytic fungi because they have a versatile enzyme system (including laccases, peroxidases and oxidases producing H2O2) which participate in the degradation of lignin but also of other recalcitrant aromatic compounds causing environmental problems [2]. Among these groups of extracellular enzymes, laccases (benzenediol: oxygen oxidoreductases, EC 1.10.3.2) have received great attention because they possess huge applicability in different biotechnological and industrial applications [3,4,5], such…”

Section: Introductionmentioning

confidence: 99%

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Purification and characterization of a fungal laccase from the ascomycete Thielavia sp. and its role in the decolorization of a recalcitrant dye

Mtibaà

Barriuso

Eugenio

et al. 2018

International Journal of Biological Macromolecules

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Section: Accepted Manuscriptsupporting

confidence: 81%

Section: Accepted Manuscriptmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Purification and characterization of a fungal laccase from the ascomycete Thielavia sp. and its role in the decolorization of a recalcitrant dye

Mtibaà

Barriuso

Eugenio

et al. 2018

International Journal of Biological Macromolecules

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“…Cerrena unicolor (Wang et al, 2017), Lentinula edodes (Nagai et al, 2003), Pycnoporus sanguineus (Ramírez-Cavazos et al, 2014), Trametes orientalis (Zheng et al, 2017), Trichoderma harzianum (El Monssef et al, 2016;Bagewadi et al, 2017), Pleurotus ostreatus (Othman et al, 2014;El-Batal et al, 2015), Pleurotus sajor-caju (Fokina et al, 2016), Pleurotus pulmonarius (Marques de Souza and Peralta, 2003;Behrens et al, 2017), Pleurotus sapidus (Schwienheer et al, 2015), Pleurotus eryngii (Loi et al, 2018), Pleurotus ferulae (Ding et al, 2014;Wang et al, 2015), and Pleurotus djamor (Salmones and Mata 2015) have been purified, characterized and studied in detail by many authors. However, laccase produced by P. tuber-regium has never been studied in detail, even though a previous study demonstrated the versatility of this fungus (Isikhuemhen and Nerud, 1999).…”

Section: Discussionmentioning

confidence: 99%

Purification and characterization of laccase from Pleurotus tuber-regium and its application in dye decolourization

Bamigboye¹,

Oloke²,

Olaogun³

et al. 2019

bta

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Pleurotus tuber-regium is a unique sclerotium-forming white rot fungus. It is edible and has medicinal value and a high potentials of application in various industries. However, to date, there is no information on the production of laccase by this fungus, the purification and determination of decolourization potential of laccase have also not been reported. In this study, purification of laccase from P. tuber-regium is demonstrated for the first time. Laccase was purified from the submerged culture of P. tuber-regium using ammonium sulfate precipitation, ion-exchange chromatography and gel filtration chromatography. The molecular weight of laccase was determined using sodium dodecyl sulfate polyacrylamide gel electrophoresis. The purified laccase was characterized to determine its optimum pH and temperature, substrate specificity, Michaelis-Menten constant, and inhibitors. The decolourization potential of the crude laccase was evaluated using Congo red, trypan blue, textile dyes and textile effluent. The purified laccase had a molecular weight of 52 kDa, optimum pH and temperature were 4 and 60EC, respectively. The best substrate for laccase was found to be 2,2N-azino-bis (3-ethylbenzothiazoline-6-sulfonate), with a Michaelis-Menten constant (K m ) of 7.82 μM. Laccase activity was mildly inhibited by ethylenediamine tetraacetic acid (EDTA) and L-cysteine, but strongly inhibited by sodium azide. The activity of the purified laccase was enhanced by more than two fold by Na + , Ca 2+ and Ba 2+ , and slightly enhanced by Hg 2+ and Mn 2+ . The crude laccase was able to efficiently decolourize trypan blue and Congo red dyes and red and blue textile dyes. Notably, on solid agar, trypan blue was completely degraded by intracellular laccase.

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“…Tetracycline could be degraded by immobilized laccase and the mechanism was proposed [6]. Synthetic dyes were also decolorized by laccaes from different organisms [7,8]. The scope of laccase substrates can be widened to higher-redox potential compounds than laccase itself with the help of diffusible electron carriers like2,2'-azino-bis(3-ethylbenzothiazoline-6-sulphonic) (ABTS) that constitute the laccase-mediator system (LMS) [9].…”

Section: Introductionmentioning

confidence: 99%

Heterologous expression and characterization of a laccase from Laccaria bicolor in Pichia pastoris and Arabidopsis thaliana

Wang¹,

Xu²,

Fu³

et al. 2018

Journal of Microbiology and Biotechnology

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Laccases can oxidize a variety of phenolic and non-phenolic substrates including synthetic dyes. In this research, a laccase gene Lcc9 from Laccaria bicolor was chemically synthesized and optimized to heterogeneous expression in Pichia pastoris and Arabidopsis thaliana. The properties of recombinant laccase expressed by P. pastoris were investigated. The laccase activity was optimal at 3.6 pH and 40 °C. It exhibited Km and Vmax values of 0.565 mmol l-1 and 1.51 μmol l-1 min-1 for ABTS respectively. As compared with untransformed control plants, the laccase activity in crude extracts of transgenic lines exhibited a 5.4 to 12.4-fold increased. Both laccases expressed in transgenic P. pastoris or A. thaliana could decolorize crystal violet. These results indicated that L. bicolor laccase gene may be transgenically exploited in fungi or plants for dye decolorization.

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Purification, characterization, and cloning of an extracellular laccase with potent dye decolorizing ability from white rot fungus Cerrena unicolor GSM-01

Cited by 57 publications

References 51 publications

Purification and characterization of a fungal laccase from the ascomycete Thielavia sp. and its role in the decolorization of a recalcitrant dye

Purification and characterization of a fungal laccase from the ascomycete Thielavia sp. and its role in the decolorization of a recalcitrant dye

Purification and characterization of laccase from Pleurotus tuber-regium and its application in dye decolourization

Heterologous expression and characterization of a laccase from Laccaria bicolor in Pichia pastoris and Arabidopsis thaliana

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