Extraction and fractionation of proteins haying both chitinase and ${\beta}-1,3-glucanase$ canase activities from rice leaves

$Chitinase/{\beta}-1,3-glucanase$ 활성 동시보유 벼잎단백질 분획의 성질

Five electrophoretic bands of crude enzyme extracted from rice leaves were found to possess both chitinase and ${\beta}-1,3-glucanase$ activities. These $chitinase/{\beta}-1,3-glucanase$ were resolved into acidic and basic fractions of protein by DEAE-cellulose and chitin affinity column chromatography. The optimal pH and temperature for ${\beta}-1,3-glucanase$ activity of two fractions were in the same extent as pH 5 and $60^{\circ}C$, whereas those for chitinase activity differed from one another; pH 3 and $60^{\circ}C$ for the acidic and pH 4 and $50^{\circ}C$ for the basic fraction, respectively. In addition, lysozyme activity was found in both fractions.

벼잎의 산성 buffer(pH 2.8) 추출 조효소는 5개의 전기영동 band들이 PR protein으로 알려진 chitinase와 ${\beta}-1,3-glucanase$의 효소활성을 보유하고 있는 것으로 나타났다. 조효소는 DEAE-cellulose 및 chitin affinity chromatography로 염기성 및 산성 효소군으로 분획되었으며, 이들은 두 효소활성이외에도 lysozyme 활성을 보유하고 있었다. 분자량이 $14.3{\sim}66.0\;kd$ 범위인 이 두 효소군이 보유한 각 효소활성의 최적 pH와 온도를 조사해본 결과,${\beta}-1,3-glucanase$는 각각 pH 5와 $60^{\circ}C$로 동일하였으나, chitinase는 염기성 효소군에서 pH 4와 $50^{\circ}C$, 산성 효소군에서는 pH 3와 $60^{\circ}C$으로 다르게 나타나서, 전기영동 양상과 더불어 서로 상이한 효소분획인 것으로 추정되었다.