Open AccessPurification, crystallization and preliminary crystallographic analysis of the catalytic domain of the extracellular cellulase CBHI from Trichoderma harzianum
Author(s) -
Colussi Francieli,
Textor Larissa C.,
Serpa Viviane,
Maeda Roberto Nobuyuki,
Pereira Nei,
Polikarpov Igor
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309110026886
Subject(s) - cellulase , trichoderma harzianum , microcrystalline cellulose , extracellular , crystallization , microcrystalline , hydrolysis , cellulose , chemistry , fermentation , materials science , biochemistry , crystallography , botany , biology , organic chemistry , biological pest control
The filamentous fungus Trichoderma harzianum has a considerable cellulolytic activity that is mediated by a complex of enzymes which are essential for the hydrolysis of microcrystalline cellulose. These enzymes were produced by the induction of T. harzianum with microcrystalline cellulose (Avicel) under submerged fermentation in a bioreactor. The catalytic core domain (CCD) of cellobiohydrolase I (CBHI) was purified from the extracellular extracts and submitted to robotic crystallization. Diffraction‐quality CBHI CCD crystals were grown and an X‐ray diffraction data set was collected under cryogenic conditions using a synchrotron‐radiation source.