Screening for Phenoloxidases from Edible Mushrooms

Morisaki, Kohei; Fushimi, Tsutomu; Kaneko, Satoshi; Kusakabe, Isao; Kobayashi, Hideyuki

doi:10.1271/bbb.65.2334

Cited by 16 publications

(9 citation statements)

References 13 publications

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“…Preparations of this fungus on potato dextrose agar plates have shown strong Lcc activity with no lignin peroxidase and weak MnP activities (Morisaki et al 2001). Recently, Lccs have been attracted wide attention because of their ability to degrade phenolic compounds (Ullah et al 2000;Fukuda et al 2001;Schultz et al 2001).…”

Section: Masaru Nagai · Yuichi Sakamoto · Keiko Nakade Toshitsugu Satomentioning

confidence: 99%

Purification of a novel extracellular laccase from solid-state culture of the edible mushroom Lentinula edodes

et al. 2009

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The laccases (EC 1.10.3.2) secreted into solidstate culture by Lentinula edodes were analyzed. The fungus secreted at least two laccases in the solid-state culture. One laccase was purifi ed to a homogeneous preparation using anion-exchange, hydrophobic, and size-exclusion chromatography. SDS-PAGE analysis showed that the purifi ed laccase, Lcc6, was a monomeric protein of 58.5 kDa. The optimum pH for enzyme activity was about 3.5, and the laccase was most active at 40°C. The N-terminal amino acid sequence of Lcc6 did not correspond to the sequence of Lcc1, which was previously purifi ed from L. edodes. Lcc6 had decolorization activity to some chemical dyes.

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Section: Masaru Nagai · Yuichi Sakamoto · Keiko Nakade Toshitsugu Satomentioning

confidence: 99%

Purification of a novel extracellular laccase from solid-state culture of the edible mushroom Lentinula edodes

et al. 2009

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“…The culture fi ltrates of this fungus exhibit strong laccase activity, and we have reported the purifi cation of two laccases from L. edodes cultures (Nagai et al 2004). In contrast, a recent report indicated that L. edodes has no LiP and only weak MnP activity (Morisaki et al 2001). Forrester et al (1990) reported that L. edodes produced only one MnP in solid-state cultures using oak wood as the substrate.…”

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confidence: 93%

Isolation and characterization of the gene encoding a manganese peroxidase from Lentinula edodes

et al. 2007

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A genomic DNA sequence and cDNA encoding a putative manganese peroxidase were isolated from the white-rot basidiomycete Lentinula edodes. The gene, called lemnp1, consists of a 1985-bp open reading frame interrupted by 16 introns and was fl anked by an upstream region having putative CAAT, TATA, and heat shock elements and by a downstream region having polyadenylation signals. The lemnp1 gene encodes a protein of 364 amino acids that shows high sequence homology to manganese peroxidases of other basidiomycetes. The deduced N-terminal amino acid sequence is different from the L. edodes manganese peroxidase reported previously.

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“…Shiitake grown on sawdust medium blocks the secretion of lignindegrading enzymes into the waste medium. It is reported that L. edodes produces strong Lcc activity in liquid cultivation (Morisaki et al 2001;Nagai et al 2002). Two independent Lccs have been purifi ed (Nagai et al 2002(Nagai et al , 2003, and Lcc-encoding genes have been cloned (Zhao and Kwan 1999) from L. edodes.…”

Section: Introductionmentioning

confidence: 99%

Cloning of Lentinula edodes lemnp2, a manganese peroxidase that is secreted abundantly in sawdust medium

et al. 2009

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Manganese peroxidase (MnP), which is one of the lignin-degrading enzymes from white-rot fungi, possesses oxidative activity against phenolic compounds, making it a useful enzyme for bioremediation. A novel MnP-encoding gene (lemnp2) was isolated from Lentinula edodes. The deduced amino acid sequence showed approximately 48.8% homology to LeMnP1. The cDNA clone was approximately 1.4 kbp whereas the genomic sequence was 1.9 kbp, and comparison of the two indicated that lemnp2 contains 13 introns. The upstream region of lemnp2 contains putative CAAT, TATA, and metal response elements. Additionally, LeMnP2 contains conserved motifs that are observed in fungal MnPs, including 10 cysteines, a Mn-binding site, and Ca 2+ -binding sites. The lemnp2 transcript was identifi ed in mycelium cultivated on sawdust medium, and the protein was secreted into the medium. MnP activity was purifi ed from the sawdust medium as one peak during purifi cation. Western blot analysis confi rmed that LeMnP2, but not LeMnP1, was secreted into the sawdust medium. These results collectively demonstrate that LeMnP2 is the major MnP secreted into sawdust medium.

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Screening for Phenoloxidases from Edible Mushrooms

Cited by 16 publications

References 13 publications

Purification of a novel extracellular laccase from solid-state culture of the edible mushroom Lentinula edodes

Purification of a novel extracellular laccase from solid-state culture of the edible mushroom Lentinula edodes

Isolation and characterization of the gene encoding a manganese peroxidase from Lentinula edodes

Cloning of Lentinula edodes lemnp2, a manganese peroxidase that is secreted abundantly in sawdust medium

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