{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,4]],"date-time":"2026-05-04T14:32:24Z","timestamp":1777905144970,"version":"3.51.4"},"reference-count":24,"publisher":"SAGE Publications","issue":"4","license":[{"start":{"date-parts":[[1998,4,1]],"date-time":"1998-04-01T00:00:00Z","timestamp":891388800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.sagepub.com\/page\/policies\/text-and-data-mining-license"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Textile Research Journal"],"published-print":{"date-parts":[[1998,4]]},"abstract":"<jats:p>We have characterized the activities of TC, EG-rich, and CBH-rich cellulases from T. reesei and have shown that their activities towards cotton fabrics are influenced by ionic strength and adsorbed ionic species as well as by temperature and pH. Adsorption and kinetic experiments confirm that increasing mechanical agitation favors EG attack by greatly increasing the availability of sites for EG adsorption. It is not clear whether this is a consequence of fiber fibrillation damage or of improved access to fiber surfaces deep within the fabric structure. The enhanced rate of cellulolytic hydrolysis of mer cerized cotton and the inhibitory effects on reactive and direct dyed fabrics are ex plained mainly in terms of increased or reduced availability of adsorption sites for CBHS and EGS. The implications for textile finishing are far-reaching. It is clear that a fabric's processing history (especially mercerizing and dyeing), construction, and level of ap plied mechanical agitation can be as important as the choice of enzyme composition and concentration in determining the consistency and quality of the end result.<\/jats:p>","DOI":"10.1177\/004051759806800405","type":"journal-article","created":{"date-parts":[[2008,3,31]],"date-time":"2008-03-31T16:14:57Z","timestamp":1206980097000},"page":"273-280","source":"Crossref","is-referenced-by-count":47,"title":["Hydrolysis of Cotton Cellulose by Engineered Cellulases from Trichoderma reesei"],"prefix":"10.1177","volume":"68","author":[{"given":"Artur","family":"Cavaco-Paulo","sequence":"first","affiliation":[{"name":"Departamento de Engenharia Textil, Universidade do Minho, P-4800 Guimar\u00e3es, Portugal"}]},{"given":"Luis","family":"Almeida","sequence":"additional","affiliation":[{"name":"Departamento de Engenharia Textil, Universidade do Minho, P-4800 Guimar\u00e3es, Portugal"}]},{"given":"David","family":"Bishop","sequence":"additional","affiliation":[{"name":"Department of Textiles and Fashion, De Montfort University, Leicester LEI 9BH, United Kingdom"}]}],"member":"179","published-online":{"date-parts":[[1998,4,1]]},"reference":[{"key":"atypb1","first-page":"404","volume":"74","author":"Almeida, L.","year":"1993","journal-title":"Melliand Textilber."},{"key":"atypb2","volume-title":"Physical Chemistry","author":"Atkins, P.","year":"1985","edition":"3"},{"issue":"1","key":"atypb3","first-page":"100","volume":"262","author":"Bailey, C.","year":"1989","journal-title":"Biochem. 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T., Knowles, J., The Molecular Biology of Trichoderma and Its Application to the Expression of Both Homologous and Heterologous Genes, in \"Molecular Industrial Mycology\u2014Systems and Applications for Filamentous Fungi,\" S. Leong & R. Berka. Eds. Marcel Dekker. Inc. NY 1991, pp. 129-148."},{"key":"atypb18","doi-asserted-by":"publisher","DOI":"10.1007\/BF00131556"},{"key":"atypb19","doi-asserted-by":"publisher","DOI":"10.1042\/bj2980705"},{"key":"atypb20","volume-title":"Cellulose-Binding Domain of Cellobiohydrolase 1 from Trichoderma reesei, Doctoral thesis","author":"Reinikainen, T.","year":"1994"},{"key":"atypb21","unstructured":"Saloheimo, A. , Henrissat, B., and Penttil\u00e4, M. Small Endoglucanase from Trichoderma reesei, Cloned by Expression in Yeast, in \"Trichoderma reesei Cellulases and Other Hydrolases,\" P. Suominen and T. Reinikainen, Eds. Foundation for Biotechnical and Industrial Fermentation Research, Finland, 1993, pp. 139-146."},{"key":"atypb22","volume-title":"Trichoderma reesei Containing Deleted and\/or Enriched Cellulase and Other Enzyme Genes and Cellulase Compositions Derived Therefrom, The Patent Cooperation Treaty","author":"Ward, M.","year":"1992"},{"key":"atypb23","unstructured":"Ward, M., Wu, S., Dauberman, J., Weiss, G., Larenas, E., Bower, B., Rey, M., Clarkson, K., and Bott, R., Cloning, Sequence and Preliminary Structural Analysis of a Small, High pH Endoglucanase (EG III) from Trichoderma reesei, in \"Trichoderma reesei Cellulases and Other Hydrolases, P. Suominen and T. Reinikainen, Eds. Foundation for Biotechnical and Industrial Fermentation Research, Finland, 1993, pp. 153-158. 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