Decolorization of Remazol Brilliant Blue R by a Purified Laccase of Polyporus brumalis

Kim, Hyewon; Lee, Sungsuk; Ryu, Sun-Hwa; Choi, Hyoung T.

doi:10.1007/s12010-011-9412-y

Cited by 26 publications

(10 citation statements)

References 17 publications

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“…In this study, the StLAC4 gene was successfully expressed in E. coli for the first time and the maximum activity of the purified laccase reached 127.78 U · mg −1 at a lower production cost. The results showed the optimum pH for Stlac4 is 4.0, which is similar to most of the studied fungal laccases , but the optimum temperature is 60 °C, which is significantly higher than most . If this advantage can be enhanced , it may improve the potential of Stlac4 in industrial applications.…”

Section: Discussionmentioning

confidence: 57%

Expression, purification, and characterization of a novel laccase from Setosphaeria turcica in Eschericha coli

Liu

Jia

et al. 2017

J Basic Microbiol

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Laccases are multicopper oxidases (E.C. 1.10.3.2) that catalyze the oxidation of many phenolic compounds. In this study, a novel laccase, Stlac4, from Setosphaeria turcica was cloned and expressed in Escherichia coli by insertion into the pET-30a expression plasmid. The recombinant laccase was purified and visualized on SDS-PAGE as a single band with an apparent molecular weight of 71.5 KDa, and confirmed by Western blot. The maximum activity of the purified laccase was 127.78 U · mg −1 , the optimum temperature and pH value were 60°C and 4. Laccases are wide-spread in nature and over 220 species of laccases have been isolated from many sources,including plants, fungi, bacteria, and insects [3][4][5][6][7]. Fungal laccases are the most extensively studied multicopper oxidases, and while primarily considered to be involved in lignin degradation [8], recent studies have shown that fungal laccases participate in fruiting body formation [9], pigment biosynthesis [10], pathogenesis, and stress defense [11]. Laccases are also very important and valuable enzymes for various biotechnological and industrial applications, such as biodegradation of lignin without polluting the environment, degradation of recalcitrant compounds, environmental protection and bioremediation, biological bleaching in the paper industry, and textile dye decolorization [12,13]. Several laccase genes have been cloned from different fungal sources and heterologously expressed with the specific purpose of using laccases more efficiently in biotechnology. Like other enzymes, laccases often face harsh conditions in industrial processes, such as high temperature, high salt concentration, and extremely acidic or alkaline pH [14,15]. Identification of laccase enzymes robust to harsh conditions could improve economic viability of this process. The majority of fungal laccases operate in the range of 30-55°C, and their optimal pH range is limited to mildly acidic conditions [16]. Many strategies Shuangxin Ma and Ning Liu contributed equally to this work.68 |

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Section: Discussionmentioning

confidence: 57%

Expression, purification, and characterization of a novel laccase from Setosphaeria turcica in Eschericha coli

Liu

Jia

et al. 2017

J Basic Microbiol

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“…In that work, most of the dye decolorization was mainly due to laccase activity and this feature was confirmed with marine-derived strains [11]. Concerning purified enzymes, a laccase from Polyporus brumalis showed effective decolorization of a dye, Remazol Brilliant Blue R (RBBR), without any laccase mediator [56]. In the case of Ps Lacs, both of them have decolorization activity against synthetic dyes such as Azure Blue, Reactive Black 5, Acid Yellow 17, Nitrosulfonazo III, Poly-R478, and Bromo Cresol Purple in the presence of mediators.…”

Section: Discussionmentioning

confidence: 81%

Characterization and Dye Decolorization Potential of Two Laccases from the Marine-Derived Fungus Pestalotiopsis sp.

Wikee

Hatton

Turbé-Doan

et al. 2019

IJMS

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: Two laccase-encoding genes from the marine-derived fungus Pestalotiopsis sp. have been cloned in Aspergillus niger for heterologous production, and the recombinant enzymes have been characterized to study their physicochemical properties, their ability to decolorize textile dyes for potential biotechnological applications, and their activity in the presence of sea salt. The optimal pH and temperature of PsLac1 and PsLac2 differed in relation to the substrates tested, and both enzymes were shown to be extremely stable at temperatures up to 50 °C, retaining 100% activity after 3 h at 50 °C. Both enzymes were stable between pH 4–6. Different substrate specificities were exhibited, and the lowest Km and highest catalytic efficiency values were obtained against syringaldazine and 2,6-dimethoxyphenol (DMP) for PsLac1 and PsLac2, respectively. The industrially important dyes—Acid Yellow, Bromo Cresol Purple, Nitrosulfonazo III, and Reactive Black 5—were more efficiently decolorized by PsLac1 in the presence of the redox mediator 1-hydroxybenzotriazole (HBT). Activities were compared in saline conditions, and PsLac2 seemed more adapted to the presence of sea salt than PsLac1. The overall surface charges of the predicted PsLac three-dimensional models showed large negatively charged surfaces for PsLac2, as found in proteins for marine organisms, and more balanced solvent exposed charges for PsLac1, as seen in proteins from terrestrial organisms.

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“…White-rot fungi such as Pleurotus ostreatus and Trametes 20 versicolor are being used as model organisms for laccase activity. The laccases have also been reported in 21 other fungi such as Phanerochaete chrysosporium, Ganoderma lucidum, Coriolus versicolor (Manavalan 22 et al, 2015) and Polyporus brumalis (Kim et al, 2012). However, laccase from the newly isolated white-23 rot fungus, Cotylidia pannosa (Gene Accession No.…”

mentioning

confidence: 89%

A novel laccase from newly isolated Cotylidia pannosa and its application in decolorization of synthetic dyes

Sharma

Goel

Sud

et al. 2015

Biocatalysis and Agricultural Biotechnology

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Decolorization of Remazol Brilliant Blue R by a Purified Laccase of Polyporus brumalis

Cited by 26 publications

References 17 publications

Expression, purification, and characterization of a novel laccase from Setosphaeria turcica in Eschericha coli

Expression, purification, and characterization of a novel laccase from Setosphaeria turcica in Eschericha coli

Characterization and Dye Decolorization Potential of Two Laccases from the Marine-Derived Fungus Pestalotiopsis sp.

A novel laccase from newly isolated Cotylidia pannosa and its application in decolorization of synthetic dyes

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