Cellobiohydrolase from Trichoderma reesei.
A 1,4-beta-D-glucan cellobiohydrolase (EC 3.2.1.91) was purified from the culture liquid of Trichoderma reesei by using biospecific sorption on amorphous cellulose and immunoaffinity chromatography. A single protein band in polyacrylamide-gel electrophoresis and one arc in immunoelectrophoresis corresponded to the enzyme activity. The Mr was 65 000. The pI was 4.2-3.6. The purified enzyme contained about 10% hexose. The enzyme differs from previously described cellobiohydrolases in being more effective in the hydrolysis of cellulose.
D043366:Cellulose 1,4-beta-Cellobiosidase; D004591:Electrophoresis, Polyacrylamide Gel; D006026:Glycoside Hydrolases / Q000302:isolation & purification* / Q000378:metabolism; D006868:Hydrolysis; D005779:Immunodiffusion; D007163:Immunosorbent Techniques; D003904:Mitosporic Fungi / Q000201:enzymology*; D011134:Polysaccharides / Q000378:metabolism; D014242:Trichoderma / Q000201:enzymology*
D011134:Polysaccharides; D006026:Glycoside Hydrolases; D043366:Cellulose 1,4-beta-Cellobiosidase