earticle

영어

In order to determine the characteristics of β-glucosidase associated with cellulose degradation, the enzyme produced extracellularly by the mycelia of Tricholoma matsutake DGUM 26001 in culture broth was partially purified. The enzyme activity was maintained in the range of temperatures from 55 to 70℃ and its optimum temperature was 65℃. The β -glucosidase enzyme showed relatively high activity in the range of pH 3.0-5.0 and its optimum pH was 4.0. Under the optimal conditions, the specific activity of β-glucosidase for salicin as a substrate was 18.7 unit/mg protein. After thermal treatment of the enzyme at 55℃ for 60 min, more than 90% of the enzyme activity was still sustained. Iron(Fe++) stimulated enzyme activity, whereas mercury(Hg++) and copper(Cu++) inhibited. Compared to salicin as a substrate, the relative activity
for cellobiose was observed to be 48.6%. The apparent Km and Vmax of the enzyme with cellobiose were 0.12 mM and 0.02 umol/min, respectively.

한국어

Cellulose 분해에 관련된 β-glucosidase 효소 활성의 특성 파악을 위하여, 송이균사(Tricholoma matsutake DGUM 26001)의 액체배양시 세포외로 분비되는 β-glucosidase 효소를 부분정제하여 그 특성을 조사하였다. 효소 활성에 미치는 적정 온도는 55-70℃이었고 최적 온도는 65℃이었다. 적정효소활성에 영향을 주는 적정 pH는 3.0-5.0 범위였으며 최적 pH는 4.0이었다. Salicin을 기질로 최적 조건하에서 β-glucosidase 효소의 비활성도는 18.7 unit/㎎ protein이었다.
열안정성은 60℃ 이하의 온도에 60분간 열처리시 약 90% 이상의 효소활성을 유지하였다. Fe++ 이온은 효소활성을 촉진하였으나, Hg++ 및 Cu++ 이온은 효소활성을 매우 억제하였다.
Salicin에 대한 효소활성을 100으로 하였을 때, cellobiose는 48.6%의 상대적 효소활성을 나타내었으며, cellobiose에 대한 Km값 및 Vmax값은 각각 0.12 mM과 0.02 umol/min었다.