{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,10]],"date-time":"2026-03-10T09:23:05Z","timestamp":1773134585568,"version":"3.50.1"},"reference-count":36,"publisher":"Wiley","issue":"1","license":[{"start":{"date-parts":[[2005,3,3]],"date-time":"2005-03-03T00:00:00Z","timestamp":1109808000000},"content-version":"vor","delay-in-days":11537,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["European Journal of Biochemistry"],"published-print":{"date-parts":[[1973,8]]},"abstract":"<jats:p>\n<jats:list list-type=\"explicit-label\">\n<jats:list-item><jats:p>A cellulolytic enzyme (\u201cC<jats:sub>1<\/jats:sub>\u201d enzyme) has been isolated from a commercial cellulase preparation derived from culture filtrates of the fungus <jats:italic>Trichoderma viride<\/jats:italic>.<\/jats:p><\/jats:list-item>\n<jats:list-item><jats:p>The purification method is a four\u2010step procedure including chromatography on Bio\u2010Gel P\u201010, DEAE\u2010Sephadex chromatography, isoelectric focusing and chromatography on Bio\u2010Gel P\u201060.<\/jats:p><\/jats:list-item>\n<jats:list-item><jats:p>A yield of 144 mg enzyme was obtained per 100 g commercial cellulase.<\/jats:p><\/jats:list-item>\n<jats:list-item><jats:p>The isolated enzyme was homogeneous in polyacrylamide gel electrophoresis at pH 5.0 and at pH 8.0 by isoelectric focusing in a polyacrylamide gel and also in the ultracentrifuge.<\/jats:p><\/jats:list-item>\n<jats:list-item><jats:p>No enzyme activity towards carboxymethylcellulose could be detected in the purified material under the assay conditions used. Similarly, there was no \u03b2\u2010glucosidase activity.<\/jats:p><\/jats:list-item>\n<jats:list-item><jats:p>The purified enzyme was associated with 3.3% carbohydrate and is assumed to be a glycoprotein. The enzyme was isoelectric at pH 3.79 (10\u00b0C). A molecular weight of 46000 was determined by chromatography of the reduced and alkylated enzyme on a calibrated column of Sepharose 6B in 6 M guanidine\u2010HCl.<\/jats:p><\/jats:list-item>\n<jats:list-item><jats:p>Crystalline cellulose (Avicel), phosphoric acid\u2010swollen Avicel and cellotetraose were degraded by the enzyme and in each case the principle reaction product was cellobiose.<\/jats:p><\/jats:list-item>\n<jats:list-item><jats:p>Evidence indicates that the purified enzyme is a \u03b2\u20101,4\u2010glucan cellobiohydrolase.<\/jats:p><\/jats:list-item>\n<\/jats:list>\n<\/jats:p>","DOI":"10.1111\/j.1432-1033.1973.tb02952.x","type":"journal-article","created":{"date-parts":[[2005,3,3]],"date-time":"2005-03-03T15:24:25Z","timestamp":1109863465000},"page":"21-30","source":"Crossref","is-referenced-by-count":225,"title":["The Mechanism of Enzymatic Cellulose Degradation"],"prefix":"10.1111","volume":"37","author":[{"given":"Lars E. 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