to determine the extracellular enzyme activity for 1,4-β-cellobiohydrolase[2]
to assay the activity of bound enzyme, endoglucanase I (EGIc) Trichoderma reesei class II hydrophobins (HFBI)[3]
Biochem/physiol Actions
4-Methylumbelliferyl β-D-cellobioside is used as a substrate for cellulase assays. It is mainly used for activity staining of cellulases in polyacrylamide gels.
Archives of microbiology, 168(4), 321-327 (1997-09-23)
The gram-negative bacterium Myxobacter sp. AL-1 produces chitosanase-cellulase activity that is maximally excreted during the stationary phase of growth. Carboxymethylcellulase zymogram analysis revealed that the enzymatic activity was correlated with two bands of 32 and 35 kDa. Ion-exchange-chromatography-enriched preparations of
Biochimica et biophysica acta, 1073(3), 481-485 (1991-04-09)
Using 4-methylumbelliferyl (MUF) beta-D-cellobioside as a substrate, the ability of cellobiohydrolase I from Trichoderma longibrachiatum to catalyze transglycosylation has been demonstrated. At substrate concentrations greater than 2 mM, the formation of MUF-tetrasaccharide was detected using HPLC. In the course of
Biochemistry and molecular biology international, 44(2), 283-292 (1998-04-08)
A Clostridium thermocellum xylanase gene, designated xynX, was cloned in Escherichia coli and was categorized a novel gene as a result of the comparison of restriction patterns of the C. thermocellum xylanase genes so far reported. The xynX gene encodes
Surface adhesion of fusion proteins containing the hydrophobins HFBI and HFBII from Trichoderma reesei
Linder M, et al.
Protein Science, 11(9), 2257-2266 (2002)
Reconciling opposing soil processes in row-crop agroecosystems via soil functional zone management
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