• The Korean Journal of Mycology
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• v.31 no.3
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• pp.181-186
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• 2003

The production of laccase by Fomitella fraxinea was studied. The addition of minerals were necessary far laccase production by Fomitella fraxinea. Jar fermentor and Air-sparging fermentor performed high productivity In laccase activity by F. fraxinea. Laccase activity reached 3,540 in 8 days (Jar fermentor) and 3,100 in 6 days (Air-sparging fermentor) respectively.

• Microbiology and Biotechnology Letters
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• v.34 no.3
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• pp.228-234
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• 2006

The culture conditions were investigated to maximize the production of laccase from Fomitella fraxinea mycelia. Among the tested media, mushroom complete medium (MCM) showed the highest production of the enzyme. The optimum culture medium was 2% dextrose, 0.4% $(NH_4)_{2}HPO_4$, 0.05% $Na_{2}HPO_{4}{\cdot}7H_{2}O$, and 0.05% KCl as carbon, nitrogen, phosphorus, and inorganic salt sources respectively. SDS-PAGE followed by laccase activity staining using 2,6-djmethoxyphenol as the substrate was performed to identify the laccase activity under culture conditions studied. Zymogram analysis of the culture supernatant showed a laccase band with a molecular mass of 50 kDa. The enzyme production from F. fraxinea was reached to the highest level after the cultivation for 10 days at $25^{\circ}C$ and initial pH 8. The enzyme activity of the culture supernatant was most active at $50^{\circ}C$ and pH 5.

• The Korean Journal of Mycology
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• v.26 no.2 s.85
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• pp.275-280
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• 1998

Factors affecting protoplasts isolation and regeneration of Fomitella fraxinea were investigated. Lytic enzyme mixture of Novozym 234, Cellulase onozuka R-10 and ${\beta}-Glucuronidase$ was found to be the best for the protoplasts isolation. Osmotic stabilizer of 0.6 M sucrose was observed as the best for protoplasts isolation. The highest number of protoplasts was obtained from the F. fraxinea mycelium with lytic enzyme mixture and osmotic stabilizer that had been cultured for 3 hours. The highest regeneration rate of 0.02 % was achieved when the 0.6 M sorbitol was employed as osmotic stabilizer.

• The Korean Journal of Mycology
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• v.29 no.1
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• pp.67-71
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• 2001

A steroid compound, F-l with antioxidative activity from the fruit bodies of Fomitella fraxinea was isolated by ethyl acetate extraction, silica gel column chromatography, and preparative silica thin layer chromatography. The structure of the compound was determined to be crgosta-7,22-diene-3-one-$16{\beta}-ol$ by IR, NMR, and GC-Mass. The compound exhibited inhibition on lipid peroxidation of rat liver microsomes, with $IC_{50}$ value of $3.8{\mu}g/ml$.

• IMMUNE NETWORK
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• v.7 no.4
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• pp.197-202
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• 2007

Background: Immunomodulators enhancing MHC-restricted antigen presentation would affect many cellular immune reactions mediated by T cells or T cell products. However, modulation of MHC-restricted antigen presentation has received little attention as a target for therapeutic immunoregulation. Here, we report that lectins isolated from mushroom Fomitella fraxinea enhance MHC-restricted exogenous antigen presentation in professional antigen presenting cells (APCs). Methods: Lectins, termed FFrL, were isolated from the carpophores of Fomitella fraxinea, and its effects on the class I and class II MHC-restricted presentation of exogenous ovalbumin (OVA) were examined in mouse dendritic cells (DCs) and mouse peritoneal macrophages. The effects of FFrL on the expression of total MHC molecules and the phagocytic activity were also examined in mouse DCs. Results: DCs cultured in the presence of FFrL overnight exhibited enhanced capacity in presenting exogenous OVA in association with class I and class II MHC molecules. FFrL increased slightly the total expression levels of both class I (H-$2K^b$) and class II (I-$A^b$) MHC molecules and the phagocytic activity of DCs. Antigen presentation-enhancing activity of FFrL was also observed in macrophages isolated from mouse peritoneum. Conclusion: Lectins isolated from the carpophores of Fomitella fraxinea increase MHC-restricted exogenous antigen presentation by enhancing intracellular processing events of phagocytosed antigens.

• The Korean Journal of Mycology
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• v.26 no.1 s.84
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• pp.69-77
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• 1998

Antioxidant activities of 80% ethanol extracts of 63 species of mushroom fruiting bodies were investigated. The ethanol extracts from Daedalea dickinsii, Armillariella mellea, and Fomitella fraxinea showed markedly inhibition on lipid peroxidation in rat liver microsome. The extracts from Daedaleopsis tricolor, Trametes suaveolens, Armillariella mellea, Trichaptium abietinum, Daedalea dickinsii, Fomitella fraxinea, Tylophilus neofelleus, Boletellus obscurecoccineus, and Xerocomus subtomentosus significantly inhibited the hepatic aldehyde oxidase activity, and the extracts from Daedaleopsis tricolor, Armillariella mellea, Daedalea dickinsii, and Fomitella fraxinea slightly stimulated the hepatic SOD activity. These results suggest that Daedalea dickinsii, Armillariella mellea, and Fomitella fraxinea contain the bioactive substances for natural antioxidant and may be useful for development of antioxidant from mushrooms.

• Microbiology and Biotechnology Letters
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• v.30 no.4
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• pp.325-331
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• 2002

investigated to maximize the production of fibrinolytic enzyme from Fomitella fraxinea mycelia. Among the tested media, Coriolus versicolor medium (CVM) showed the highest production for the enzyme. 2% galactose, 0.6% yeast extract and 0.1% $NaNO_3$, 0.1% $K_2HPO_4$, and 0.05% $MgSO_4$.$7H_2O$ as carbon, nitrogen, phosphorus, and inorganic salt sources resulted in the maximum level of the enzyme activity, respectively. The enzyme production from F. fraxinea was reached to highest level after the cultivation for 10 days at $25^{\circ}C$ and pH 9. The enzyme activity of culture supernatant was most active at $40^{\circ}C$ and pH 10. The activity of the enzyme was inhibited by phenylmethylsulfonylfluoride and aprotinin, suggesting that it is a serine protease.

• The Korean Journal of Mycology
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• v.26 no.4 s.87
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• pp.502-510
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• 1998

The hot-water extract of fruiting bodies in Fomitella fraxinea had potent anti-complementary activities. After fractionation of water-soluble polysaccharides by DEAE-Sephadex A-25 column chromatography, major anti-complementary activity was concentrated into the FF-AP1 among three polysaccharides (FF-NP, FF-AP1, FF-AP2). FF-AP1 was fractionated into $FF-AP1{\alpha}$ and $FF-AP1{\beta}$ obtained from the adsorbed fraction and unadsorbed fraction by affinity chromatography using a ConA-sepharose 4B column, respectively. $FF-AP1{\beta}$, which exihibited the highest anti-complementary activities had an IR absorption peak of $890cm^{-1}$, and a M.W. of about 15,000 (gel filtration). Anti-complementary activity of FF-AP1 decreased greatly by pronase treatment and periodate oxidation. $FF-AP1{\beta}$ responsible for potent anti-complemenary activities of Fomitella fraxinea was an acidic protein-containing heteroglycan consisted of 48% glucose, 13% mannose, and 12% galactose as major component sugars, 9.6% protein, 6% uronic acids.

• Journal of Microbiology and Biotechnology
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• v.18 no.4
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• pp.670-675
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• 2008

A laccase was isolated from the culture filtrate of the basidiomycete Fomitella fraxinea. The enzyme was purified to electrophoretical homogeneity using ammonium sulfate precipitation, anion-exchange chromatography, and gel-filtration chromatography. The enzyme was identified as a monomeric protein with a molecular mass of 47 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and gel-filtration chromatography, and had an isoelectric point of 3.8. The N-terminal amino acid sequence for the enzyme was ATXSNXKTLAAD, which had a very low similarity to the sequences previously reported for laccases from other basidiomycetes. The optimum pH and temperature for 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonate) (ABTS) were 3.0 and $70^{\circ}C$, respectively. The enzyme also showed a much higher level of specific activity for ABTS and 2,6-dimethoxyphenol (DMP), where the $K_m$ values of the enzyme for ABTS and 2,6-DMP were 270 and $426{\mu}M$, respectively, and the $V_{max}$ values were 876 and $433.3{\mu}M/min$, respectively. The laccase activity was completely inhibited by L-cysteine, dithiothreitol (DTT), and sodium azide, significantly inhibited by $Ni^+,\;Mn^{2+}$, and $Ba^{2+}$, and slightly stimulated by $K^+$ and $Ca^{2+}$.

• The Korean Journal of Mycology
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• v.23 no.4 s.75
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• pp.340-347
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• 1995

Polysaccharide FHW was extracted from the fruiting bodies of Fomitella fraxinea with hot-water treatment and then fractionated into FHW-I and FHW-II on DEAE-Cellulose chromatography. FHW-I and FCW-II were further purified into FHW-Ia and Ib, FHW-IIa and IIb on gel permeation chromatography, respectively. A small amount of uronic acid was detected and glucose, galactose, fucose, and mannose were found to be main sugars in the polysaccharides. Protein was detected in FHW-Ia, FHW-IIa, and FHW-IIb, but not in FHW-Ib. FHW-Ia was identified to be a fuco-gluco-mannogalactan with molecular weight of 19,000 and FHW-Ib was a gluco-fuco-mannogalactan of 15,000. FHW-IIa and FHW-IIb were galacto-mannoglucan and their molecular weights were estimated to be 31,000 and 9,000, respectively. Both FHW-Ib and FHW-IIb did not show an absorption band characteristic of the ${\beta}-glycosidic$ linkage in IR spectra. FHW-IIb showed a strong immuno-stimulating activity but the other three polysaccharides showed a weak activity.