• Journal of Pharmaceutical Investigation
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• v.18 no.3
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• pp.125-131
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• 1988

This study was undertaken to investigate the proteolytic enzyme from Neungee mushroom [Sarcodon aspratus (Berk) S. Ito]. The proteolytic activity of Neungee was higher than other several edible mushrooms under various pHs. The potency of proteolytic enzyme of Neungee was same as the digestive drugs containing protease. So the proteolytic activity of the enzyme was increased in neutral or weak alkaline pH, whose characteristics would be alkaline protease. The specific activity of the purified enzyme obtained by using Tris acryl CM-cellulose ion exchange increased 20 times as compared with that of the crude extract. The proteolytic enzyme was stable at room temperature, but decomposition was fast when incubated at higher temperature more than $40^{\circ}C$. The half life of the enzyme was longest in neutral pH and rate constant was increased in acidic or alkaline solution.

• Journal of the Korean Society of Food Science and Nutrition
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• v.20 no.1
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• pp.35-39
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• 1991

Properties of a protease purified from Neungee[Sarcodon aspratus(Berk, ) S. Ito] have been investigated. The enzyme displays a glycosylated serine protease. The enzyme is able to hydrolyze alanine glycine methionine glutamine and cysteine of N-CBZ and N-t-BOC-L-amino acid derivatibes relatively strongly but splits valine proline and isoleucine derivatives with low affinity which means the enzyme has the broad substrate spectrum toward the amino acids. Interestingly the enzyme was inhibited by bromelain inhibitor. That is the active site environ-ment of the enzyme is believed to be similar to that of bromelain However peptide mapping studies show that the two enzymes have distinct different cleavage sites.

• Journal of Pharmaceutical Investigation
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• v.19 no.2
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• pp.81-86
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• 1989

The proteolytic enzyme extracted from Neungee [Sarcodon aspratus (Berk.) S. Ito] was purified by using Tris-acryl CM-cellulose column chromatography and chromatofocusing. The specific activity of the purified enzyme increased 15.8 times as compared with that of the crude enzyme. The enzyme was homogeneous on polyacrylamide gel electrophoresis and stable at pH values ranging from 4.0 to 10.8. The enzyme activity remained unchanged when the mushroom and the purified enzyme were stored for 3 years and 6 months at 4°C, respectively. The enzyme was found to be an endogeneous protease.

• Mycobiology
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• v.36 no.4
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• pp.249-254
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• 2008

Minimal growth inhibitory concentrations (MICs) of chitosan acetate (M.W. 60 kDa) on heterotrophic bacteria (strains MK1, S, and R) isolated from the soft-rotten tissues of Neungee mushroom (Sarcodon aspratus) were measured. The slimy substance produced by the MK1 strain was responsible for the diseased mushroom’s appearance. The S and R strains were members of the Burkholderia cepacia complex. These strains showed different levels of susceptibility toward chitosan acetate. The MIC of chitosan acetate against the MK1 and S strains was 0.06%. The MIC against the R strain was greater than 0.10%. Survival fractions of the MK1 and S strains at the MIC were $3\;{\times}\;10^{-4}$ and $1.4\;{\times}\;10^{-3}$ after 24 h, and $2\;{\times}\;10^{-4}$ and $7\;{\times}\;10^{-4}$ after 48 h, respectively. Survival fractions of the R strain after 24 and 48 hr at 0.1% chitosan acetate were $1\;{\times}\;10^{-2}$ and $6.9\;{\times}\;10^{-3}$, respectively. Compared to the MK1 and S strains, the low susceptibility of the R stain towards chitosan acetate could be due to the ability of the R strain to utilize chitosan as a carbon source. Thirty-eight percent of Neungee pieces treated in a 0.06% chitosan acetate solution for $2{\sim}3$ second did not show any bacterial growth at 4 days, whereas bacterial growth around untreated mushroom pieces occurred within 2 days. These data suggest that chitosan acetate is highly effective in controlling growth of indigenous microorganisms on Neungee. The scanning electron micrographs of the MK1 strain treated with chitosan revealed a higher degree of disintegrated and distorted cellular structures.

• Food Science and Preservation
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• v.15 no.6
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• pp.864-871
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• 2008

The chemical components and physiological activities of Neungee mushroom (Sarcodon aspratus) were investigated to assess its nutritional and functional value. The moisture, total protein, crude fat and ash contents of Neungee mushroom were 85.73%, 1.78%, 1.87% and 1.27%, respectively. The alanine, linoleic acid, tartaric acid and glucose concentrations in Neungee mushrooms were 90.11, 39.09, 75.47 and 1,680 mg%, respectively. The radical and nitrate scavenging activities in Neungee mushroom extracts were 46.2% and 77.8% on $800{\mu}g/mL$ depending on the extract concentration. The lipid peroxidation inhibitory effect of Neungee mushroom extract ($1,500\;{\mu}g/mL$) was $2,347\;{\mu}mol$ MDA/g liver. We also observed that an extract concentration of $1,500\;{\mu}g/mL$ was more effective than the control at 7 d. The cytotoxicity of the Neungee mushroom extract ($100\;{\mu}g/mL$) for the A549 (lung carcinoma) cells was 96.0%.

• Korean Journal of Microbiology
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• v.45 no.4
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• pp.324-331
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• 2009

MK1 strain, an obligate aerobic heterotrophic bacterium isolated from the rotten tissue of Neungee mushroom (Sarcodon aspratus), produces a copious amount of exopolysaccharide (EPS), which could evoke macrophage activation. Investigations on optimal culture conditions of MK1 and physical properties of MK1 EPS were made. Glucose, galactose, fructose, and sucrose supported well growth of MK1, but potato starch and dextrin did not. However, lactose seemed to be a less favorable carbon source. Optimal growth of MK1 was obtained at pH 7.0, $30^{\circ}C$, and 200 rpm with 2% glucose, and 0.2~0.05% $(NH_4)_2SO_4$. $EPS_{opt}$ obtained from an optimal growth condition constituted of carbon (37.1%), nitrogen (2.2%), oxygen (49.3%), and hydrogen (6.4%), but no sulfur. Paper chrogromatogram of the acid-hydrolysate of $EPS_{opt}$ suggested that MK1 EPS seemed to be hetropolysaccharide composed of a few number of monosaccharides including amino- and acidic-sugars. Its molecular mass determined by SDS-polyacrylamide gel electrophoresis varied from 14.8 to 47.9 kDa. Physical properties of $EPS_{glu}$ obtained from cell grown in glucose medium, such as relative viscosity ($_{rel}$) and crystalline morphology were rather affected by pH of the growth medium. Relative viscosity ($_{rel}$) of exopolysaccaride (0.1 g/ml) harvested from cells grown at medium pH ranging from 6.0 and 7.5 was 1.23 and 1.39, respectively. The freeze-dried exopolysaccharide obtained at low pH (6.0 and 6.5) was fine crystaloid and water-soluble, whereas those obtained at high pH (7.0 and 7.5) was rather gluey and less water-soluble.

• Korean Journal of Food Science and Technology
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• v.33 no.3
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• pp.307-312
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• 2001

Flavor compounds in Neungee (sarcodon aspratus) were extracted by simutaneous distillation and extraction (SDE), supercritical fluid extraction (SFE) and headspace method. Flavor compounds obtained by various extraction methods were analyzed with GC and GC-MS. The funtionality of flavor compounds were determined by aroma extract dilution analysis (AEDA) of GC-ofactometry methods. Fifty one flavor compounds were totally identified in Neungee mushroom. However, the numbers of flavor extracted SDE, SFE and headspace were 33, 26 and 17 respectively. The major flavor compounds obtained by SDE, SFE and headspace were 1-octen-3-ol, 1-octen-3-one, 3-octanone, 2-octen-1-ol, 3-octanol, 1-octanol and benzenealdehyde. As the results of sniffing test, the major flavor compounds were found to be fresh mushroom flavor, wood flavor, refreshing sweet flavor, mold flavor, bitter-mushroom and metalic-flavor.

• Journal of the Korean Society of Food Science and Nutrition
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• v.22 no.6
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• pp.811-814
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• 1993

Properties of a protease purified from Sarcodon asparatus(Berk.) S. Ito have been investigated. The enzyme displays as a glycosylated serine protease. The sequence for the 21 amino acids of the N-terminal side in the enzyme was determined by automated sequence analysis. The sequence was V-T-T-K-Q-T-N-A-P-W-G-L-G-N-I-S-T-T-N-K-L-.

• Journal of the Korean Society of Food Science and Nutrition
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• v.33 no.7
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• pp.1230-1236
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• 2004

This study was conducted to investigate the changes in physical properties of the Neungee (Sarcodon aspratus) during dehydration and rehydration. The drying of the sample was completed within 4 hours at 5$0^{\circ}C$ with the air velocity of 1.5 m/s. The reduction in the thickness of the sample were two-fold compared with those in the surface area of the sample. During the drying period, the values of compression distance, break down, deformation rate, distortion, alleviation rate and softness decreased, whereas the values of hardness and alleviation time increased. However, the values of surrender were not changed. The color of the sample during the drying was changed to black with decreased L, a, and b values. The rehydration rate increased rapidly during first 60 min and remained constant after that. The recovery ratio after rehydration of the dried sample was about 30％ and the rheological properties recovered about 44％.

• Journal of the Korean Society of Food Science and Nutrition
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• v.15 no.3
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• pp.276-285
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• 1986

This study was undertaken to investigate the characteristics of the proteolytic enzyme extracted from Neungee mushroom [Sarcodon aspratus (Berk.) S. Ito]. The enzyme was purified by using Tris-acryl CM-cellulose ion exchange, gel filtration on Ultrogel AcA 54, Hydroxy apatite column chromatography and preparative isoelectic focusing. The specific activity of the purified enzyme increased 8 times as compared with that of the crude enzyme. The enzyme was homogeneous on polyacrylamide gel electrophoresis (PAGE). The optimum pH was 10.1, indicating the enzyme to be alkaline protease and the optimum temperature was $57^{\circ}C$. The enzyme was stable at temperatures lower than $50^{\circ}C$and at pH values ranging from 4.0 to 10.8. However, the enzyme activity decreased by 26 and 65% at 60 and $65^{\circ}C$, respectively, when incubated for 30 minutes. The enzyme activity was activated by $Mn^{++}$ and inhibited by $Cu^{++}$ and $Hg^{++}$. The enzyme was consisted of monomer and its molecular weight estimated to be about 30,100 when determined by sodium dodecyl sulfate PAGE. Isoelectric point of the enzyme was determined to be 9.80.