Trichoderma viride의 cellobiohydrolase을 immunoaffinity chromatography를 제조하여 조효소로부터 일단계로 용이하게 분리할 수 있었다. 분리된 cellobiohydrolase는 전기영동과 isoelectrofocusing 상에서 단일단백질로 확인되었고, 분자량이 70,000,pI치는 3.8.인 산성단백질이었다. 면역친화 정제된 cellobiohydrolase는 무정형 섬유소보다는 고결정성 섬유소에 특성이 높았다.
A cellobiohydrolase was purified from the culture broth of Trichoderma uiride by using immunoaffinity chromatography. A single protein band in polyacylamide gel electrophoresis and isoelectrofocusing after immunoaffinity purification corresponded to cellobiohydrolase activity. A immunoaffinity purified cellobiohydrolase is more effective in the hydrolysis of highly crystalline cellulose than amorphous cellulose.
