Abstract
Two kind of ${\beta}-glucosidase$, tightly-bound enzyme(TBE) and loosely-bound enzyme(LBE), were obtained from the conidia of Aspergillus nidulans. The existence of enzymes in conidia was conformed by the fact that these enzyme activities were proportional to the number of conidia. The levels of enzyme activities were independent of aging of the conidia. Enzymes were characterized partially. In spite of the physical and chemical treatments of conidia, there was no significant change in TBE activity. The optimum pH and temperature was 6.0 and $55^{\circ}C$, respectively. Thermostability of the TBE was remarkably higher than that of mycelial ${\beta}-glucosidase$. The electrophoretic pattern of LBE was identical to that of mycelial ${\beta}-glucosidase$. These results suggest that conidial ${\beta}-glucosidase$ are involved in adaptation process of the conidia to variable environments.
Aspergillus nid$\mu$tans 의 분생포지에는 두 종류의 $\beta$.glucosidase, 즉 tightly-bound enzyme(TBE)과 loosely-bound enzyme(LBE)이 존재한다. 포자수와 효소활성도가 정비례함을 보아 이 효소의 존재을 확인할 수 있었으며, 배양조건 하에서 의 오랜기잔 방치에도 얼정 수준의 활성을 유치하는 높은 안정성을 보였다. 분생포자에 여러가지 물리.화학적 처리를 한 뒤에도 TBE의 환성도에는 큰 변화가 없었으며, TBE의 최적 pH 및 온도는 각각 6.0, $55^{\circ}C$였다.TBE의 열안정성은 균사체의 $\beta$-glucosidase보다 높았으며, $H^{2+}$이온에 대한 내성도 비교적 높은 수준을 보였다. LBE와 균사체 $\beta$-glucosidase의 전기영동 양상이 유사한 것으후 보아 율사체와 동일한 효소가 포자의 표면에 존재후L을 알 수있었다.