• Journal of Life Science
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• v.10 no.6
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• pp.617-620
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• 2000

Methanol extract of Sarcodon aspratus Berk. (S. Ito) was analyzed by thi layer chromatography, gas chromatography and mass spectrophotometer. Nine fractions from primary methanol extract were observed by TLC. Six fractions were observed by the second TLC analysis of the second and the third fractions. 27,28-digydrolanosterol({TEX}$C_{30}H_{52}${/TEX}O), ergost-7-en-3-ol({TEX}$C_{28}H_{48}${/TEX}O) were identified from two fractions of the second TLC analysis by mass spectrophotometer. The molecular weights of 27,28-dihydrolanosterol and ergost-7-en-3-ol were 413 and 400 respectively.

• The Korean Journal of Mycology
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• v.14 no.1
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• pp.25-30
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• 1986

The purposes of this study were to investigate enzyme components and its physiological activities of Sarcodon aspratus (Berk.) S. Ito which grows wildly in Korea, belonging to the family Thelephoraceae. The carpophores of the fungus was extracted with cooling distilled water and salted out by ammonium sulfate. The precipitate was purified by dialysing through visking tube against distilled water and then dissolved with pH 7.8 ammonia aqua, and the extract was filterated. The fraction of filtrate was obtained as light brown powder after lyophilization and determined proteolytic activity. Protease activity of Sarcodon aspratus (Berk.) S. Ito was about two-third of that of pepsin on casein by cup method. The proteolytic potency of this enzyme was found to be 500 unit/mg. This proved the efficacy of the mushroom when it was used as a folk medicine for treating indigestion of beef.

• 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.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.

• 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.

• The Korean Journal of Mycology
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• v.11 no.2
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• pp.85-89
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• 1983

The aims of this study were to investigate various components and their physiological activities of Sarcodon aspratus (Berk.) S. Ito which grows wildly in Korea, belonging to the family Thelephoraceae. The analysis of the powered carpophore of this fungus by TLC and an amino acid autoanalyzer revealed that it contained twenty-one free amino acids and that twenty­two total amino acids were identified in its acid hydrolysate. These amino acids were also quantified.

• Journal of Pharmaceutical Investigation
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• v.19 no.4
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• pp.203-212
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• 1989

A proteolytic enzyme was extracted from Sarcodon aspratus (Berk) S. Ito by percolation method. Proteolytic activity of the extracted proteolytic enzyme (SAP) was compared with several digestives containing proteolytic enzymes. Potency of SAP was higher than that of the other digestives except for protease. The optimum pH ranse of SAP was similar to that of pancveatin and protease. SAP was more stable than pancreatin and protease under various temperature, alkaline pH, and metal ions. Bovine serum albumin hydrolysing activity of SAP was equivalent to that of pancreatin and protease in small intestine of rats. SAP demonstrated lower adsorption to antacids than pancreatin and protease. Among the mixtures of SAP and several antacids, magnesium oxide-SAP showed the highest proteolytic activity.

• Korean journal of food and cookery science
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• v.17 no.5
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• pp.497-502
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• 2001

능이버섯 〔Sarcodon aspratus(Berk.) S.Ito〕으로부터 단백질 가수분해 효소를 추출하여 75%(NH$_4$)$_2$SO$_4$ 염석과 DE52 anion exchange column chromatography 와 sepharyl-S 200 column 및 Mono s column chromatography 에 의해 정제하였는데 조 효소의 특이 활성은 55.2U/mg protein으로 조효소액에 비하여 11.26배 증가하였고 수율은 49.5%로 나타났다. 정제된 효소는 전기영동을 행한 결과 단일 band를 나타내었으며 분자량은 29,300으로 추정되었다. pH의 안정성은 4$^{\circ}C$에서 48시간 보존하였을 때 pH 8.5에서 가장 안정하였고, pH 5.5~10.5까지 높은 활성을 유지하였다. 온도에 대한 안정성은 30분간 보존 한 후 활성을 검토한 결과 단백분해능은 5$0^{\circ}C$까지 비교적 처음활성을 유지하다가 6$0^{\circ}C$에서는 53%정도의 활성이 유지되었으나 그 이상의 온도에서는 급격히 실화하여 7$0^{\circ}C$에서는 완전히 실화하였다. 금속 이온에 의해서는 크게 저해를 받지 않았으나 PMSF 저해제에 대하여 저해되어 본 효소가 serine protease임을 시사하였다.

• Korean Journal of Pharmacognosy
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• v.33 no.3 s.130
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• pp.224-229
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• 2002

Sarcodon aspratus (Thelephoraceae), a native mushroom distributed in Korea and Japan has been widely used as a traditional food and folk medicines. Two proteoglycan polysaccharides, named SAP-A and SAP-B were isolated from the fruitbody of S. aspratus. Their molecular weight were determined as 6184.9 D, and 25749.2 D, respectively, by maldi-tof ms. The composition of sugar and amino acid of these compounds was also determined. The SAP-A showed potent antitumor activity. The $ID_{50}$ value of SAP-A was 8.2 mg/kg/day for ICR mice transplanted with solid sarcoma-180, and the elongation of lifespan effect was 167.4% for ICR mice transplanted with ascitic sarcoma-180. Moreover, the elongation life-span effect of SAP-A increased dose-dependently.