반부후(半腐朽) 아까시아나무(Robinia Pseudacacia Linne)에서 분리(分離)한Trichoclerma viride $(O_2-1)$가 생성(生成)하는 조효소(粗酵素)의 성질(性質)을 실험(實驗)하여 다음과 같은 결과(結果)를 얻었다. 1) 각종(各種)의 섬유소기질(纖維素基質)에 반응(反應)시켜본 결과(結果) 수종류(數種類)의 cellulase가 혼존(混存)함을 알았다. 2) C.M.C 및 ${eta}-glucoside$ 분해효소(分解酵素)는 기질(基質)의 농도(濃度)가 증가(增加)함에 따라 분해율(分解率)이 낮았으며 여지당화효소(濾紙糖化酵素)는 기질(基質) 및 효소량(酵素量)이 증가(增加)되고 시간(時間)의 경과(經過)에 따라 분해율(分解率)이 상대적(相對的)으로 증가(增加)되었다. 3) 각효소(各酵素)의 최적활성(最適浩性) pH는 5.0이였으며 pH 안정성(安定性)은 대체(大體)로 pH $3{sim}6$ 이였다. 4) 최상활성온도(最適活性溫度)는 여지붕괴력(濾紙崩壞力)이 $50^{circ}C$ C.M.C.및 $p-nitro-phenyl-{eta}-glucoside$ 분해력(分解力)이 $60^{circ}C$ 여지당화력(濾紙糖化力)이 $65^{circ}C$에서 최고활성(最高活性)을 나타내었다. 열(熱)에 대(對)한 안정성(安定性)은 여지당화력(濾紙糖化力), C.M.C 당화력(糖化力), 여지붕괴력(濾紙崩壞力), ${eta}-glucoside$ 당화력(糖化力)의 순위(順位)였다. 5) 금속(金屬) Ion에 대(對)한 영향(影響)은 $Hg^{++},;Ag^+$ 각효소(各酵素)에 대(對)하여 조해(阻害)하였으며 $K^+$는 각효소(各酵素)를 활성화(活性化)하였다.
The characteristics of crude enzyme produced from Trichoderma viride($O_2-1$) which isolated from half spoiled Locust acacia wood (Robinia Pseudacacia Linne) were examined in this paper. The results obtained were summarized as follows: 1) As a results of enzymatic action on several cellulose substrate it was found that there were some sorts of cellulase in crude enzyme. 2) The activity of C.M.C. ase and ${eta}-glucosidase$ were decreased in accordance with increasing concentration of substrate, and filter paper saccharifying enzyme relatively increased in accordance with increasing concentration of substrate and enzyme in couse of time. 3) The optimal pH of each enzyme was 5.0 and the range of stability on pH generally from 3 to 6. 4) In disintegrating activity on filter paper, in decomposing activity on C.M.C. and $p-nitrophenyl-{eta}-D-glucoside$, and in saccharifying activity on filter paper, the optimal temperatures were $50^{circ}C.,;60^{circ}C,;and;65^{circ}C$. 5) The order of stability on temperature was as follow; saccharifying activity on filter paper decomposing activity on C.M.C. disintegrating activity on filter paper>decomposing activity on $p-nitrophenyl-{eta}-D-glucoside$. 6) The activity of the enzymes was inhibited with mercuric and silver ion, and activated with potassium.
