An alkaline pectate lyase, Bsp165PelA, was purified to homogeneity from the culture broth of alkaliphilic Bacillus sp. N16-5. The enzyme showed a specific activity as high as 1000 U/mg and had optimum activity at pH 11.5 and 50 degrees . It was composed of a single polypeptide chain with a molecular of 42 kDa deduced from SDS-PAGE, and its isoelectric point was around pH 6.0. It could efficient...

Treating Arabidopsis roots with exogenous auxin results in dramatic changes in cellular processes including de novo induction of lateral roots which later emerge through the overlying cells. Microarray experiments reveal approximately 80 genes that are substantially up-regulated in the root over the first 12 h following auxin treatment. We hypothesize that the observed increase in expression of...

Production of different pectinolytic enzymes was attempted using the actinomycete strain Streptomyces lydicus in submerged fermentation. Polygalacturonase and pectin lyase activities were detected in the culture supernatant, but the strain was not able to produce pectin esterase. Polygalacturonase production was studied in submerged, slurry-state and solid-state fermentation systems. All the ex...

Sclerenchyma fibre bundles and pectin were simultaneously segregated from wood bark under a tailored pectin-degrading enzyme consortium alone.

Clostridium cellulovorans uses not only cellulose but also xylan, mannan, pectin, and several other carbon sources for its growth and produces an extracellular multienzyme complex called the cellulosome, which is involved in plant cell wall degradation. Here we report a gene for a cellulosomal subunit, pectate lyase A (PelA), lying downstream of the engY gene, which codes for cellulosomal enzym...

The hydrolysis of p-nitrophenyl acetate catalysed by pectin methylesterase is competitively inhibited by pectin and does not require metal ions to occur. The results suggest that the activastion by metal ions may be explained by assuming that they interact with the substrate rather than with the enzyme. With pectin used as substrate, metal ions are required in order to allow the hydrolysis to o...

The pectin lyase gene pnl-zj5a from Aspergillus niger ZJ5 was identified and expressed in Pichia pastoris. PNL-ZJ5A was purified by ultrafiltration, anion exchange and gel chromatography. The Km and Vmax values determined using citrus pectin were 0.66 mg ml(-1) and 32.6 μmol min(-1) mg(-1) , respectively. PNL-ZJ5A exhibited optimal activity at 43°C and retained activity over 25-50°C. PNL-ZJ5A w...