Abstract
Clostridium cellulovorans produces an efficient enzyme complex for the degradation of lignocellulosic biomass. In our previous study, we detected and identified protein spots that interacted with a fluorescently labeled cohesin biomarker via two-dimensional gel electrophoresis. One novel, putative cellulosomal protein (referred to as endoglucanase Z) contains a catalytic module from the glycosyl hydrolase family (GH9) and demonstrated higher levels of expression than other cellulosomal cellulases in Avicel-containing cultures. Purified EngZ had optimal activity at pH 7.0, 40°C, and the major hydrolysis product from the cellooligosaccharides was cellobiose. EngZ's specific activity toward crystalline cellulose (Avicel and acid-swollen cellulose) was 10-20-fold higher than other cellulosomal cellulase activities. A large percentage of the reducing ends that were produced by this enzyme from acid-swollen cellulose were released as soluble sugar. EngZ has the capability of reducing the viscosity of Avicel at an intermediate-level between exo- and endo-typing cellulases, suggesting that it is a processive endoglucanase. In conclusion, EngZ was highly expressed in cellulolytic systems and demonstrated processive endoglucanase activity, suggesting that it plays a major role in the hydrolysis of crystalline cellulose and acts as a cellulosomal enzyme in. C. cellulovorans.
Original language | English |
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Pages (from-to) | 365-371 |
Number of pages | 7 |
Journal | New Biotechnology |
Volume | 29 |
Issue number | 3 |
DOIs | |
Publication status | Published - 2012 Feb 15 |
Bibliographical note
Funding Information:We are grateful to Ka Young Shin for skillful technical assistance and Dr. Hyun Wook Jung for viscometric analysis. This work was supported in part by a grant from the Technology Development Program for Agriculture and Forestry, Ministry for Agriculture, Forestry and Fisheries, Republic of Korea (no. 309016-5) and the Mid-career Researcher Program via an NRF grant funded by the MEST, Republic of Korea (no. R01-2008-000-20438-0).
ASJC Scopus subject areas
- Biotechnology
- Bioengineering
- Molecular Biology