{Reference Type}: Journal Article

{Author}: Shuai Zhou;Yanfang Liu;Yan Yang;Wei Jia;Qingjiu Tang;Chuanhong Tang;Na Feng;JingSong Zhang

{Year}: 2013

{Title}:Separation and structural elucidation of a polysaccharide CC30w-1 from the fruiting body of Coprinus

{Tag}: 0

{Star}: 0

{Volume}:1

{Issue}: 2

{Pages}: 99-104

{DOL}: http://dx.doi.org/10.1016/j.bcdf.2013.03.003

{ISBN/ISSN}:2212-6198

{Keywords}: Polysaccharide;Coprinus comatus;Separation;Structural elucidation

{Abstract}:

In this study, a water soluble polysaccharide (CC30w-1), with a molecular mass of 1.03×104, was isolated from the fruiting body of Coprinus comatus. The polysaccharide moiety was composed of L-Fuc and D-Gal in the ratio of 1:3.84. The structure of CC30w-1was elucidated by methylated analysis, GC–MS, 1H and 13C NMR spectroscopy, together with 1H–1H COSY, TOCSY, HMQC and HMBC. Results showed that the polysaccharide consists of the following repeating units:

  α − L − Fuc p 1 ↓ 2 → 6 ) − α − D − Gal p − ( 1 → 6 ) − α − D − Gal p − ( 1 → 6 ) − α − D − Gal p − ( 1 → 6 ) − α − D − Gal p ( 1 →

{Author Address}:   http://www.sciencedirect.com

{Language}: English

{Reference Type}: Journal Article

{Author}: Shuichi Sekiya;Masato Yamada;Kou Shibata;Toru Okuhara;Masumi Yoshida;Satoshi Inatomi;Goro Taguchi;Makoto Shimosaka

{Year}: 2013

{Title}:Characterization of a gene coding for a putative adenosine deaminase-related growth factor by RNA interference in the Basidiomycete Flammulina velutipes

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{Star}: 0

{Volume}: 115

{Issue}: 4

{Pages}: 360-365

{DOL}: http://dx.doi.org/10.1016/j.jbiosc.2012.10.020

{ISBN/ISSN}:1389-1723

{Keywords}: Basidiomycete;Flammulina velutipes;Adenosine deaminase;Growth factor;RNA interference

{Abstract}: A full-length cDNA coding for a putative adenosine deaminase (Fv-ada) was isolated from the basidiomycete Flammulina velutipes. Fv-ada encodes a polypeptide consisting of 537 amino acid residues, which has a consensus sequence conserved among adenosine deaminase-related growth factors (ADGF) found in several metazoa, including chordates and insects. Fv-ada transcript was detected at all stages of growth in dikaryotic F.  velutipes cells, with a peak at the primordial stage. Heterologous expression of Fv-ada in the yeast Pichia pastoris produced recombinant Fv-ADA that catalyzed the conversion of adenosine to inosine. Dikaryotic mycelia from F.  velutipes were transformed with the binary plasmid pFungiway-Fv-ada, which was designed to suppress the expression of Fv-ada through RNA interference. The growth rates of the resulting transformants were retarded in response to the degree of suppression, indicating that Fv-ada plays an important role in the mycelial growth of F.  velutipes. These results suggested that ADGF could function as growth factors in fungi, as is seen in other eukaryotes.

{Author Address}:   http://www.sciencedirect.com

{Language}: English

{Reference Type}: Journal Article

{Author}: Tomoko Maehara;.Koji Takabatake;Satoshi Kaneko

{Year}: 2013

{Title}:Expression of Arabidopsis thaliana xylose isomerase gene and its effect on ethanol production in Flammulina velutipes

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{Star}: 0

{Volume}: 117

{Issue}: 11–12

{Pages}: 776 - 782

{DOL}: http://dx.doi.org/10.1016/j.funbio.2013.09.005

{ISBN/ISSN}:1878-6146

{Keywords}: Flammulina velutipes;Basidiomycete fungi;Ethanol fermentation;Heterologous gene expression;Xylose metabolism

{Abstract}: To improve the pentose fermentation rate in Flammulina velutipes, the putative xylose isomerase (XI) gene from Arabidopsis thaliana was cloned and introduced into F. velutipes and the gene expression was evaluated in transformants. mRNA expression of the putative XI gene and XI activity were observed in two transformants, indicating that the putative gene from A. thaliana was successfully expressed in F. velutipes as a xylose isomerase. In addition, ethanol production from xylose was increased in the recombinant strains. This is the first report demonstrating the possibility of using plant genes as candidates for improving the characteristics of F. velutipes.

{Author Address}:   http://www.sciencedirect.com

{Language}: English