• 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.

• 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.

• 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 $3.8{\mu}g/ml$.

• The Korean Journal of Mycology
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• v.23 no.3 s.74
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• pp.238-245
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• 1995

A good mycelial growth of F. fraxinea was observed on CDA medium. The optimum temperature and pH for the mycelial growth of F. fraxinea was at $30^{\circ}C$ and pH 6.0, respectively. Glucose was found to be the best carbon source and arginine was favored as nitrogen source. When the basal medium was supplemented with organic acids, the best growth was shown in succinic acid and the poor growth was shown in oxalic acid. Thiamine.HCl showed the best results on the growth of this fungus on basal medium. Mycelial growth of F. fraxinea was quite good when oak tree sawdust was used to cultural substrates. The best mycelial growth was observed when 20% of rice bran was added as a supplement on sawdust substrates. Higher yield of F. fraxinea was observed on the medium with oak tree and acacia sawdust.

• 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.

• 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.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.

• Food Science and Biotechnology
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• v.16 no.6
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• pp.935-942
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• 2007

The stem bark of Rhus verniciflua (RVSB) has been used in herbal medicine to treat diabetes mellitus and stomach ailments for thousands of years in Korea, despite its content of the plant allergen, urushiol. A new biological approach for the removal of urushiol from RVSB using mushrooms is described. All mushroom species (11 sp.) employed in this study were able to grow on RVSB, although the growth rate (mm/day) was lower than the control (sawdust). The components of urushiol congeners [C15 triene (m/z 314), C15 diene (m/z 316), C15 monoene (m/z 318), and C15 saturated (m/z 320)] were purified by HPLC and identified by GC-MS. A C15:3 (3-pentadecatrienly catechol) was found to be most abundant in RVSB. Urushiol analogues decreased remarkably from 154.15 to 10.73 mg/100 g (approximately 93%) by Fomitella fraxinea, whereas Trametes vercicolor showed only a 1.46% degradation capacity despite its 2 fold higher growth rate. Similarly, laccase activity was found to be high for F. fraxinea and low for T. vercicolor. Moreover, approximately 98% detoxification was accomplished by F. fraxinea cultivated on RVSB supplemented with 20%(w/w) rice bran. These findings suggest that mushrooms can be used in the detoxification of RVSB.

• Journal of Microbiology and Biotechnology
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• v.16 no.2
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• pp.264-271
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• 2006

Two fibrinolytic enzymes were purified from the culture supernatant of Fomitella fraxinea mycelia by ion-exchange and gel filtration chromatographies, and were designated as F. fraxenia proteases 1 and 2 (FFP1 and FFP2). The apparent molecular masses of the enzymes were estimated to be 32 kDa and 42 kDa, respectively, by SDS-PAGE and gel filtration chromatography. Both enzymes had the same optimal temperature ($40^{\circ}C$), but different pH optima (10.0 and 5.0 for FFP1 and FFP2, respectively). FFP1 was relatively stable at pH 7.0-9.0 and temperature below $30^{\circ}C$, whereas FFP2 was very stable in the pH range of 4-11 and temperature below $40^{\circ}C$. FFPI activity was completely inhibited by phenylmethylsulfonyl fluoride (PMSF) and aprotinin, indicating that this enzyme is a serine protease. The activity of FFP2 was enhanced by the addition of $CO^{2+}$ and $Zn^{2+}$ and inhibited by $Cu^{2+},\;Ni^{2+}$, and $Hg^{2+}$. Furthermore, FFP2 activity was strongly inhibited by EDTA and 1,10-phenanthroline, implying that the enzyme is a metalloprotease. Both enzymes readily hydrolyzed fibrinogen, preferentially digesting the $A{\alpha}$- and $B{\beta}$-chains of fibrinogen over ${\gamma}$-chain. FFP1 showed broad substrate specificity for synthetic substrates, but FFP2 did not. $K_{m}$ and $V_{max}$ values of FFP1 for a synthetic substrate, N-succinyl-Ala-Ala-Pro-Phe-pNA, were 0.213 mM and 39.68 units/ml, respectively. The first 15 amino acids of the N-terminal sequences of both enzymes were APXXPXGPWGPQRIS and ARPP(G)VDGQ(R,I)SK(L)ETLPE, respectively.