11 research outputs found
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Mechanisms of lignin biosynthesis during xylogenesis in Zinnia elegans. Final report, July 1, 1992--June 30, 1996
This project initially focused on identifying and characterizing three components of the extracellular lignification reaction: peroxidases, hydrogen peroxide production, and oxygen dependent oxidases. Zinnia elegans was utilized for the model organism. Laccase activity was found to be more tightly correlated with lignification than peroxidase activity
Comportamento respiratório e qualidade pós-colheita de graviola (Annona muricata L.) 'morada' sob temperatura ambiente
Lignin content and peroxidase activity in soybean seed coat susceptible and resistant to mechanical damage
New insights into the molecular architecture of hardwood lignins by chemical degradative methods
The Two Major Xylanases from Trichoderma Reesei: Characterization of Both Enzymes and Genes
As a first step to exploit the potential of Trichoderma reesei to produce hemicellulases, we have purified two endo-β-1,4-xylanases (1,4-β-D-xylan xylanohydrolase, EC 3.2.1.8) and cloned their genes. The enzymes were isolated from culture filtrates of T. reesei C 30 grown on xylan as a carbon source, using two steps of cation exchange chromatography. They exhibited molecular weights of 19 (XYN I) and 21 (XYN II) kD, and isoelectric points of 5.2 and 9.0, respectively. These enzymes differed in their pH optimum for activity and affinity for xylan, and accounted for more than 90% of the total xylanolytic activity of the fungus. The purified enzymes were subjected to N-terminal sequence analysis, and after cleavage with trypsin and endoproteinase Glu-C the resulting peptides were sequenced. Oligonucleotides based on these sequences were used to clone gene fragments via PCR, and these were used as probes to isolate full-length copies of xyn1 and xyn2 from a lambda gene bank of T. reesei. The products of xyn1 and xyn2 share considerable homology, but the enzyme encoded by xyn2 appears to more closely resemble several other bacterial and fungal xylanases than does that of xyn1.Peer reviewe