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Production of Trichoderma reesei Cel7B and its catalytic core on glucose medium and its application for the treatment of secondary fibers

Paper ID Volume ID Publish Year Pages File Format Full-Text
36065 45119 2006 5 PDF Available
Title
Production of Trichoderma reesei Cel7B and its catalytic core on glucose medium and its application for the treatment of secondary fibers
Abstract

Application of cellulolytic enzymes for upgrading of secondary fibers has extensively been studied during the last decades. In many cases, research has been carried out with industrial enzyme preparations which often consist of several enzyme components. The presence of various enzymes makes the determination of the role of each of them difficult in changes of pulp and paper properties. Therefore, investigations using single enzyme preparations are necessary to understand and optimize this complex process. One of the possibilities to produce individual cellulase components is repression of undesired genes. In this work, two recombinants of Trichoderma reesei strain QM9414 were used to produce intact Cel7B (endoglucanase I, EGI) and the catalytic core of Cel7B selectively under glucose repression of other cellulases. For homologous expression in glucose medium the gpdA promoter from Aspergillus nidulans was used. Culture filtrates containing the intact Cel7B or Cel7B core were applied for secondary fiber treatment. The treatments caused improved drainage as shown by 16–17% decrease of the Schopper–Riegler (SR) values. The effects of cellulase treatment on pulp and paper properties showed that presence or absence of a cellulose-binding module (CBM) on Cel7B does not play a determinative role.

Keywords
Biotechnology; Trichoderma reesei Cel7B (endoglucanase I); Cellulose-binding module (CBM); Recycled fiber; Drainage; Strength properties
First Page Preview
Production of Trichoderma reesei Cel7B and its catalytic core on glucose medium and its application for the treatment of secondary fibers
Publisher
Database: Elsevier - ScienceDirect
Journal: Process Biochemistry - Volume 41, Issue 9, September 2006, Pages 2092–2096
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering