{Reference Type}: Journal Article
{Author}: Hironaka, Kazunori; Funato, Takuro; Koaze, Hiroshi
{Year}: 2010
{Title}: Enrichment of the antioxidant activity in potato tuber by ultrasound and electric treatments
{Tag}: 0
{Star}: 0
{Journal}: ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY
{Volume}: 240
{ISBN/ISSN}: 0065-7727
{Author Address}: Obihiro Univ Agr & Vet Med, Dept Food Sci, Obihro, Japan; Obihiro Univ Agr & Vet Med, Dept Food Sci, Obihro, Japan; Obihiro Univ Agr & Vet Med, Dept Food Sci, Obihro, Japan
{Database Provider}: Web of Science SCI
{Language}: English
{Country}: Japan

{Reference Type}: Journal Article
{Author}: Geoesel, A.; Sipos, L.; Stefanovits-Banyai, E.; Kokai, Z.; Gyorfi, J.
{Year}: 2011
{Title}: ANTIOXIDANT, POLYPHENOL AND SENSORY ANALYSIS OF AGARICUS BISPORUS AND AGARICUS SUBRUFESCENS CULTIVARS
{Tag}: 0
{Star}: 0
{Journal}: ACTA ALIMENTARIA
{Volume}: 401
{Number}: WOS:000294637000004
{Pages}: 33-40
{Cited Count}: 2
{Date Displayed}: 2011
SEP 2011
{ISBN/ISSN}: 0139-3006
{Abstract}: In the past decades many papers were published on the nutritional effect and bioactive components of edible mushrooms. The fungi are able to accumulate secondary metabolites, for example, phenolic compounds, polyketides, terpenes and steroids. In case of mushrooms the button mushrooms are preferred in the Eastern-European region. Therefore white and cream type button mushroom (Agaricus bisporus) and different A. subrufescens (syn. A. blazei) cultivars were cropped, total phenolic content and antioxidant capacity (FRAP) were measured in two years of experiments. To develop the description method of mushroom products, software-supported profile analysis was applied to characterize them. The aim of the research was to compare the sensory profiles of the samples, and to find those characteristics, they actually differ in.

{Reference Type}: Journal Article
{Author}: Sun, J.; Zhao, Y.; Chai, H.; Wang, H.; Ng, T. B.
{Year}: 2011
{Title}: A novel alkaline protease with antiproliferative activity from fresh fruiting bodies of the toxic wild mushroom Amanita farinosa
{URL}: http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=22146135&query_hl=1
{Tag}: 0
{Star}: 0
{Journal}: Acta Biochim Pol
{Volume}: 58
{Issue}: 4
{Pages}: 567-72
{Date Displayed}: 2011
{Date}: 2011-01-20
{Type of Work}: Journal Article; Research Support, Non-U.S. Gov't
{Accession Number}: 22146135
{Keywords}: Adsorption; Amanita/*enzymology; Amino Acid Sequence; Antineoplastic Agents, Phytogenic/chemistry/*isolation &
           purification/pharmacology; Cell Proliferation/drug effects; Cell Survival; Chromatography, Affinity; Chromatography, Gel; Chromatography, Ion Exchange/methods; Electrophoresis, Polyacrylamide Gel; Enzyme Activation; Enzyme Assays; Fruiting Bodies, Fungal/*enzymology; Fungal Proteins/chemistry/isolation & purification/pharmacology; Hep G2 Cells; Humans; Hydrogen-Ion Concentration; Peptide Hydrolases/chemistry/*isolation & purification/pharmacology; Temperature
{Abstract}: A novel protease with a molecular mass of 15 kDa was purified from fresh fruiting bodies of the wild mushroom Amanita farinosa. The purification protocol entailed   anion exchange chromatography on DEAE-cellulose, affinity chromatography on Affi-gel blue gel, cation exchange chromatography on SP-Sepharose, and gel filtration by fast protein liquid chromatography on Superdex 75. The protease was unadsorbed on DEAE-cellulose but adsorbed on Affi-gel blue gel and SP-Sepharose.   It demonstrated a single 15-kDa band in sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS/PAGE) and a 15-kDa peak in gel filtration. The optimal pH and optimal temperature of the protease were pH 8.0 and 65 degrees C, respectively. Proliferation of human hepatoma HepG2 cells was inhibited by the protease with an IC(50) of 25 microM. The protease did not have antifungal or ribonuclease activity.
{Author Address}: State Key Laboratory for Agrobiotechnology and Department of Microbiology, China   Agricultural University, Beijing, China.
{Language}: eng

{Reference Type}: Journal Article
{Author}: Zhang, G. Q.; Sun, J.; Wang, H. X.; Ng, T. B.
{Year}: 2009
{Title}: A novel lectin with antiproliferative activity from the medicinal mushroom Pholiota adiposa
{URL}: http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=19636442&query_hl=1
{Tag}: 0
{Star}: 0
{Journal}: Acta Biochim Pol
{Volume}: 56
{Issue}: 3
{Pages}: 415-21
{Date Displayed}: 2009
{Date}: 2009-01-20
{Type of Work}: Journal Article; Research Support, Non-U.S. Gov't
{Accession Number}: 19636442
{Keywords}: Agaricales/*chemistry; Aluminum/pharmacology; Antifungal Agents/chemistry/isolation & purification/pharmacology; Antineoplastic Agents/chemistry/isolation & purification/pharmacology; Cell Line, Tumor; Cell Proliferation/drug effects; Chromatography, Gel; Chromatography, Liquid; Copper/pharmacology; Electrophoresis, Polyacrylamide Gel; HIV Reverse Transcriptase/antagonists & inhibitors; Hemagglutination/drug effects; Humans; Hydrogen-Ion Concentration; Inulin/pharmacology; Lectins/chemistry/isolation & purification/*pharmacology; Protein Stability; Temperature
{Abstract}: Little was known about biological activities of compounds from the medicinal mushroom of the genus Pholiota. A lectin from the Pholiota adiposa has now been isolated and its properties tested. The isolation procedure included ion exchange chromatography on DEAE-cellulose and CM-cellulose, and fast protein liquid chromatography-gel filtration (FPLC) on Superdex 75. The lectin was composed of two identical subunits, each with a molecular mass of 16 kDa. Its N-terminal amino-acid sequence showed little similarity to sequences of other Agaricales lectins. The hemagglutinating activity of the lectin was stable at temperatures up to 50 degrees C, and in NaOH and HCl solutions with concentrations less than 25 mM. It was inhibited by inulin (12.5-200 mM), but enhanced by Cu(2+) (6.25-25   mM), Fe(2+) (12.5-25 mM), and Al(3+) (6.25-25 mM) ions. The lectin showed antiproliferative activity toward hepatoma Hep G2 cells and breast cancer MCF7 cells with an IC(50) of 2.1 microM and approximately 3.2 microM, respectively. It exhibited HIV-1 reverse transcriptase inhibitory activity with an IC(50) of 1.9 microM. When compared with P. aurivella lectin, the only Pholiota lectin published to date, P. adiposa lectin differs in chromatographic behavior, molecular mass, N-terminal sequence, and effect of cations on hemagglutinating activity. In the case of the lectin from P. aurivella, its antifungal, antiproliferative, and HIV-1 reverse transcriptase inhibitory activities have not been determined.
{Author Address}: State Key Laboratory for Agrobiotechnology and Department of Microbiology, China   Agricultural University, Beijing, China.
{Language}: eng