| Characterization and immobilization of liposome-bound cellulase for hydrolysis of insoluble cellulose. | |
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MedLine Citation:
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PMID: 16822673 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The liposome-bound cellulase was prepared by covalently coupling cellulase with the enzyme-free liposomes bearing aldehyde groups so that cellulase was located solely on the outer membrane of liposomes. The modified cellulase possessed the higher activity efficiency and lipid-based specific activity than the cellulase-containing liposomes reported previously. The enzyme-free liposomes bearing aldehyde groups were covalently immobilized with the chitosan gel beads and the free cellulase was coupled with the treated gel beads to prepare the immobilized liposome-bound cellulase. The activity efficiency of the immobilized liposome-bound cellulase was much higher than that of the conventionally immobilized cellulase. The results on reusability of the immobilized liposome-bound cellulase in the hydrolysis of either soluble or insoluble cellulose showed that the immobilized liposome-bound cellulase had the higher remaining cellulase activity and reusability than the conventionally immobilized cellulase for the hydrolysis of either type of cellulose. The liposomal membrane was suggested to be efficient in maintaining the cellulase activity during the hydrolysis. |
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Authors:
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Chengzhou Li; Makoto Yoshimoto; Kimitoshi Fukunaga; Katsumi Nakao |
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Publication Detail:
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Type: Comparative Study; Journal Article; Research Support, Non-U.S. Gov't Date: 2006-07-05 |
Journal Detail:
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Title: Bioresource technology Volume: 98 ISSN: 0960-8524 ISO Abbreviation: Bioresour. Technol. Publication Date: 2007 May |
Date Detail:
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Created Date: 2007-01-03 Completed Date: 2007-05-16 Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 9889523 Medline TA: Bioresour Technol Country: England |
Other Details:
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Languages: eng Pagination: 1366-72 Citation Subset: IM |
Affiliation:
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Department of Applied Chemistry and Chemical Engineering, Faculty of Engineering, Yamaguchi University, 2-16-1 Tokiwadai, Ube 755-8611, Japan. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Aldehydes
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metabolism Cellulase / isolation & purification*, metabolism* Cellulose / metabolism* Chitosan Enzymes, Immobilized / metabolism* Hydrolysis Kinetics Liposomes / metabolism* |
| Chemical | |
Reg. No./Substance:
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0/Aldehydes; 0/Enzymes, Immobilized; 0/Liposomes; 9004-34-6/Cellulose; 9012-76-4/Chitosan; EC 3.2.1.4/Cellulase |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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