Cellulose hydrolysis by the cellulases from Trichoderma reesei : a new model for synergistic interaction

Bibliographic Details
Title:	Cellulose hydrolysis by the cellulases from Trichoderma reesei : a new model for synergistic interaction
Authors:	Nidetzky, B, Steiner, W, Hayn, M, Claeyssens, M
Superior Title:	Biochemical Journal ; volume 298, issue 3, page 705-710 ; ISSN 0264-6021 1470-8728
Publisher Information:	Portland Press Ltd.
Publication Year:	1994
Subject Terms:	Cell Biology, Molecular Biology, Biochemistry
Description:	The hydrolysis of Whatman no. 1 filter paper by purified cellulolytic components from Trichoderma reesei and the synergistic action of binary combinations of these enzymes on the same substrate were investigated. At 20 milligrams filter paper, enzyme concentrations needed to obtain half-maximal hydrolysis rates (KE values) were in the 3-4 microM range for the cellobiohydrolases (CBHs) and 0.05-0.10 microM for the endoglucanases (EGs). Catalytic-core proteins of CBH I and EG III, lacking the cellulose-binding domain, exhibit KE values 2.3 and 5.1 times higher than those of the intact enzymes. In synergistic combinations of two cellulases, the KE value of at least one enzyme was 3-10-fold reduced. CBH I/CBH II and CBH I/EG III combinations showed the most powerful synergism, and optimal ratios were a function of the total protein concentration. Results obtained in activity and adsorption assays using filter paper pretreated with one component, followed by inactivation and subsequent hydrolysis with the same or another cellulase component, point to a sequential enzymic attack of the cellulose and seems consistent with the mathematical model presented.
Document Type:	article in journal/newspaper
Language:	English
DOI:	10.1042/bj2980705
Availability:	https://doi.org/10.1042/bj2980705 https://portlandpress.com/biochemj/article-pdf/298/3/705/612952/bj2980705.pdf
Accession Number:	edsbas.F93F0FAF
Database:	BASE

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