A simple method to separate cellulose-binding domains of fungal cellulases after digestion by a protease

M. Adilia Lemos; J. A. Teixeira; M. Mota; F. M. Gama

doi:10.1023/A:1005691821173

A simple method to separate cellulose-binding domains of fungal cellulases after digestion by a protease

M. Adilia Lemos, J. A. Teixeira, M. Mota, F. M. Gama

Abertay University

Research output: Contribution to journal › Article

19 Citations (Scopus)

Abstract

Core-binding domains of fungal cellulases from Trichoderma reesei were purified using a new and simple technique. Cellulases were hydrolysed with papain and the binding domains were then separated from the digested mixture by ultrafiltration. The enzymatic digestion process was monitored using capillary electrophoresis. This methodology produced a yield of 85% of binding domains.

Original language	English
Pages (from-to)	703-707
Number of pages	5
Journal	Biotechnology Letters
Volume	22
Issue number	8
DOIs	https://doi.org/10.1023/A:1005691821173
Publication status	Published - 2000

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Lemos, M. A., Teixeira, J. A., Mota, M., & Gama, F. M. (2000). A simple method to separate cellulose-binding domains of fungal cellulases after digestion by a protease. Biotechnology Letters, 22(8), 703-707. https://doi.org/10.1023/A:1005691821173

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abstract = "Core-binding domains of fungal cellulases from Trichoderma reesei were purified using a new and simple technique. Cellulases were hydrolysed with papain and the binding domains were then separated from the digested mixture by ultrafiltration. The enzymatic digestion process was monitored using capillary electrophoresis. This methodology produced a yield of 85% of binding domains.",

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AB - Core-binding domains of fungal cellulases from Trichoderma reesei were purified using a new and simple technique. Cellulases were hydrolysed with papain and the binding domains were then separated from the digested mixture by ultrafiltration. The enzymatic digestion process was monitored using capillary electrophoresis. This methodology produced a yield of 85% of binding domains.

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10.1023/A:1005691821173