Purification and Characterization of Cellobiohydrolase from Trichoderma viride

Trichoderma viride가 생산하는 Cellobiohydrolase의 분리 및 특성

Two isozymes of cellobiohydrolase and fifteen isozymes of endoglucanase from Trichodema viride QM 9414 were purified by ammonium sulfate fractionation, Sephadex G-100 column chromatography, DEAE-Sephadex A-50 column chromatography and preparative electrophoresis. The purified cellobiohydrolnse had a molecular weight of 71,000 estimated by electrophoresis and amino acid analysis showed its main amino acids to be in the form of aspartic acid and glutamic acid result-ing from its low pI point of 3.81. The optimum pH and temperature were 5.1 and 5$0^{\circ}C$ respectively.

Trichoderma viride가 분비하는 섬유소 분해효소를 황산암모늄침전, Sephadex G-100 및 DEAE Sephadex column을 통과시켜서 5개의 섬유소 분해 아이조자임을 분리하였으며 전기영동 방법에 의해서 2개의 celloblohydrolase와 15개의 endoglucanase로 분리하였다. 분리된 cellobiohydrolase는 분자량이 71,000, 최적 pH5.1, 최적온도 5$0^{\circ}C$, pI가 3.81이었으며 주종아미노산은 aspartric acid, glutamic acid. threonine, serine 및 glycine이었다.