{Reference Type}: Journal Article
{Author}: Imanishi, Y.; Jindamorakot, S.; Mikata, K.; Nakagiri, A.; Limtong, S.; Potacharoen, W.; Tanticharoen, M.; Nakase, T.
{Year}: 2008
{Title}: Two new ascomycetous anamorphic yeast species related to Candida friedrichii--Candida jaroonii sp. nov., and Candida songkhlaensis sp. nov.--isolated in Thailand
{URL}: http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=18425597&query_hl=1
{Tag}: 0
{Star}: 0
{Journal}: Antonie Van Leeuwenhoek
{Volume}: 94
{Issue}: 2
{Pages}: 267-76
{DOI}: 10.1007/s10482-008-9242-2
{Date Displayed}: 2008 Aug
{Date}: 2008-08-01
{Type of Work}: Journal Article
{Accession Number}: 18425597
{Keywords}: *Agaricales; Animals; Bryophyta/*microbiology; Candida/*classification/genetics/*isolation & purification/metabolism; DNA, Fungal/genetics; DNA, Ribosomal Spacer/genetics; Ecology; Flowers/*microbiology; Insects/*microbiology; Molecular Sequence Data; Mycological Typing Techniques; Phylogeny; RNA, Ribosomal/genetics; Thailand
{Abstract}: In a study of yeast diversity in Thailand, eight strains of hitherto undescribed   anamorphic yeasts were isolated: four from insect frass, two from Marasmius sp. fruiting bodies, one from a flower, and one from jackfruit exudates. Phylogenetic analysis of the D1/D2 domain of 26S ribosomal DNA nucleotide sequences indicated   that the eight strains represented two new species related to Candida friedrichii. Genetic separation of the two new species was further supported by DNA-DNA hybridization analysis, which resulted in between-species similarity values of less than 48%, and by electrophoretic karyotyping. The two new species   are C. jaroonii sp. nov. (type strain, ST-300(T) = NBRC 103209(T) = BCC 11783(T)   = CBS 10790(T)) and C. songkhlaensis sp. nov. (type strain, ST-328(T) = NBRC 103214(T) = BCC 11804(T) = CBS 10791(T)).
{Author Address}: NITE Biological Resource Center (NBRC), National Institute of Technology and Evaluation (NITE), 2-5-8, Kazusakamatari, Kisarazu-shi, Chiba 292-0818, Japan. imanishi-yumi@nite.go.jp
{Language}: eng

{Reference Type}: Journal Article
{Author}: Amore, A.; Honda, Y.; Faraco, V.
{Year}: 2012
{Title}: Enhanced green fluorescent protein expression in Pleurotus ostreatus for in vivo   analysis of fungal laccase promoters
{URL}: http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=22893518&query_hl=1
{Tag}: 0
{Star}: 0
{Journal}: Appl Biochem Biotechnol
{Volume}: 168
{Issue}: 4
{Pages}: 761-9
{DOI}: 10.1007/s12010-012-9816-3
{Date Displayed}: 2012 Oct
{Date}: 2012-10-01
{Type of Work}: Journal Article
{Accession Number}: 22893518
{Keywords}: Gene Expression Regulation, Fungal/*genetics; Green Fluorescent Proteins/*genetics; Hyphae/cytology/enzymology/genetics; Intracellular Space/genetics; Laccase/*genetics; Molecular Imaging; Plasmids/genetics; Pleurotus/cytology/*enzymology/*genetics; Polyethylene Glycols/chemistry; Promoter Regions, Genetic/*genetics; Transformation, Genetic
{Abstract}: The laccase family of Pleurotus ostreatus has been widely characterized, and studies of the genes coding for laccase isoenzymes in P. ostreatus have so far led to the identification of four different genes and the corresponding cDNAs, poxc, pox1, poxa1b and poxa3. Analyses of P. ostreatus laccase promoters poxc, pox1, poxa1b and poxa3 have allowed identification of several putative response elements, and sequences of metal-responsive elements involved in the formation of complexes with fungal proteins have been identified in poxc and poxa1b promoters. In this work, development of a system for in vivo analysis of P. ostreatus laccase promoter poxc by enhanced green fluorescent protein expression is performed, based on a poly ethylene glycol-mediated procedure for fungal transformation. A quantitative measurement of fluorescence expressed in P. ostreatus transformants is hereby reported for the first time for this fungus.
{Author Address}: Department of Chemical Sciences, University of Naples Federico II, Complesso Universitario Monte S. Angelo, via Cintia 4, 80126 Naples, Italy.
{Language}: eng

{Reference Type}: Journal Article
{Author}: Iandolo, D.; Piscitelli, A.; Sannia, G.; Faraco, V.
{Year}: 2011
{Title}: Enzyme production by solid substrate fermentation of Pleurotus ostreatus and Trametes versicolor on tomato pomace
{URL}: http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=20582639&query_hl=1
{Tag}: 0
{Star}: 0
{Journal}: Appl Biochem Biotechnol
{Volume}: 163
{Issue}: 1
{Pages}: 40-51
{DOI}: 10.1007/s12010-010-9014-0
{Date Displayed}: 2011 Jan
{Date}: 2011-01-01
{Type of Work}: Evaluation Studies; Journal Article; Research Support, Non-U.S. Gov't
{Accession Number}: 20582639
{Keywords}: *Fermentation; Fungal Proteins/genetics/*metabolism; Industrial Microbiology/*methods; Laccase/genetics/metabolism; Lycopersicon esculentum/*microbiology; Peptide Hydrolases/genetics/metabolism; Pleurotus/*enzymology/genetics/metabolism; Refuse Disposal/*methods; Trametes/*enzymology/genetics/metabolism
{Abstract}: A process of solid state fermentation (SSF) on tomato pomace was developed with the white-rot fungi Pleurotus ostreatus and Trametes versicolor, using sorghum stalks as support. Operative parameters (humidity, water activity, and size of substrate particles) guaranteeing a good colonization of tomato pomace by both fungi were defined and conditions for production at high titers of the industrially relevant enzymes laccase, xylanase and protease were identified. Significant laccase activity levels (up to 36 U g(-1) dry matter) were achieved without any optimization of culture conditions, neither by nutrient addition nor   by O(2) enrichment. Furthermore, protease activity levels up to 34,000 U g(-1) dry matter were achieved, being higher than those reported for the fungi typically considered as the best protease producers such as Aspergillus strains.   Moreover, as one of the most significant results of this study, analysis of P. ostreatus tomato SSF samples by zymogram revealed two bands with laccase activity which had not been detected so far.
{Author Address}: Department of Organic Chemistry and Biochemistry, University of Naples Federico II, Complesso Universitario Monte S. Angelo, via Cintia 4, Naples, Italy.
{Language}: eng

{Reference Type}: Journal Article
{Author}: Choi, J. H.; Kim, S.; Sapkota, K.; Park, S. E.; Kim, S. J.
{Year}: 2011
{Title}: Expression and production of therapeutic recombinant human platelet-derived growth factor-BB in Pleurotus eryngii
{URL}: http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=21594593&query_hl=1
{Tag}: 0
{Star}: 0
{Journal}: Appl Biochem Biotechnol
{Volume}: 165
{Issue}: 2
{Pages}: 611-23
{DOI}: 10.1007/s12010-011-9279-y
{Date Displayed}: 2011 Sep
{Date}: 2011-09-01
{Type of Work}: Journal Article; Research Support, Non-U.S. Gov't
{Accession Number}: 21594593
{Keywords}: Agrobacterium tumefaciens/*genetics/metabolism; Animals; Blotting, Southern; Blotting, Western; Dimerization; Escherichia coli; Fibroblasts/*drug effects/metabolism; Genomics/*methods; Humans; Mice; NIH 3T3 Cells; Organisms, Genetically Modified/*genetics/metabolism; Plasmids; *Platelet-Derived Growth Factor/genetics/isolation &
           purification/metabolism/pharmacology; Pleurotus/*genetics/metabolism; Polymerase Chain Reaction; Protein Engineering/*methods; Proto-Oncogene Proteins c-sis; Recombinant Proteins/genetics/isolation & purification/metabolism/pharmacology; Transduction, Genetic; Transformation, Bacterial
{Abstract}: Recombinant human platelet-derived growth factor-BB (rhPDGF-BB) is widely used in many therapeutic applications. Until now, there has been no report on rhPDGF-BB expressed in fungi. In this study, we tested whether Pleurotus eryngii could support the expression of human therapeutic rhPDGF-BB protein. A binary vector pCAMBIA1304 containing the hPDGF-BB gene was constructed and introduced into P. eryngii via Agrobacterium tumefaciens-mediated transformation. The transformation of hPDGF-BB gene was confirmed by Southern blot and PCR, whereas the expression was confirmed by Western blot analysis. The recombinant hPDGF-BB reached a maximum expression level of 1.98% of total soluble protein in transgenic mycelia   and was in dimeric form. A bioassay revealed that hPDGF-BB expressed in P. eryngii increased proliferation of NIH-3T3 cells similarly to standard material.   These results suggest that P. eryngii can be a robust system for the production of human therapeutic proteins including the hPDGF-BB.
{Author Address}: Department of Biotechnology, Chosun University, 375 Seosuk-dong, Dong-gu, Gwangju 501-759, Republic of Korea.
{Language}: eng