Cloning and characterization of two cellulase genes from Lentinula edodes
نویسندگان
چکیده
منابع مشابه
Cloning and characterization of two cellulase genes from Lentinula edodes.
Lentinula edodes has traditionally been grown on fallen logs. It produces a wide array of enzymes to digest the lignocellulolytic substrate for nutrients. Thus, this organism represents a rich source of potentially potent lignocellulolytic enzymes that can be harnessed for conversion of biomass to simple sugars. These sugars can then be used as feedstock for ethanol production or other chemical...
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Hemicellulose represents a rich source of biomass that can be converted into useful chemical feedstocks. One of the main components of hemicellulose is xylan, a polymer of xylose residues. Xylanase enzymes that hydrolyze xylan are therefore of great commercial interest. We have cloned a gene (xyn11A) that encodes a 283-amino acid xylanase enzyme from the fungus Lentinula edodes. The enzyme has ...
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Hydrophobins play important roles in morphogenesis and pathogenesis in fungi and fruit development in mushrooms. Two genes encoding hydrophobins (Le.hyd1 and Le.hyd2) were isolated during sequencing of random clones from a primordial cDNA library of Lentinula edodes. The nucleotide sequences of these two genes were determined. These two genes are 760 and 738 bp in length and the deduced amino a...
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The effect of different substrates and various developmental stages (mycelium growth, primordium appearance, and fruiting-body formation) on laccase production in the edible mushroom Lentinula edodes was studied. The cap of the mature mushroom showed the highest laccase activity, and laccase activity was not stimulated by some well-known laccase inducers or sawdust. For our molecular studies, t...
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CelR, a protein that regulates transcription of cellulase genes in Thermomonospora fusca (Actinomycetaceae) was purified to homogeneity. A 6-kilobase NotI-SacI fragment of T. fusca DNA containing the celR gene was cloned into Esherichia coli and sequenced. The celR gene encodes a 340-residue polypeptide that is highly homologous to members of the GalR-LacI family of bacterial transcriptional re...
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ژورنال
عنوان ژورنال: FEMS Microbiology Letters
سال: 2001
ISSN: 0378-1097,1574-6968
DOI: 10.1111/j.1574-6968.2001.tb10972.x