Dynamic interaction of Trichoderma reesei cellobiohydrolases Cel6A and Cel7A and cellulose at equilibrium and during hydrolysis

Article Abstract:

Interaction of Trichoderma reesei cellobiohydrolases Cel6A and Cel7A and their catalytic domains and cellulose has been investigated at equilibrium and in hydrolysis using tritium labeling by reductive methylation. Affinities of the cellulose-binding domains and the catalytic domains were compared to the affinities of the intact proteins. Affinity of the enzyme dilution of the sample showed hysteresis. Density of bound protein was found to increase with both Cel6A and Cel7A as hydrolysis went on. Adsorption points moved off the initial binding isotherms. The two enzymes were found to be different in reversibility of binding.

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Combined effects of the signal sequence and the major chaperone proteins on the export of human cytokines in Escherichia coli

Article Abstract:

The formation and export of human proteins in Escherichia coli is dependent on the attached signal peptide and expression of chaperone proteins. The synthesis of the human granulocyte-macrophage colony-stimulating factor increases when it is attached to the S3 signal peptide compared to S1. The synthesis of interleukin 13 is unaffected by the signal peptide but its export into the periplasma is more if S1 is present. The overexpression of the chaperone proteins, SecB or DnaK and DnaJ, increases the concentration of the proteins in the periplasma of Escherichia coli.

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Glucose transport by mixed ruminal bacteria from a cow

Article Abstract:

The mode and properties of major glucose transport systems in mixed ruminal bacteria were analyzed in the lumen of cows fed with grain-containing forage-based meals. Hydrogen-ion and glucose concentration in the rumen was affected by sucrose, fructose and mannose which inhibited glucose transport via a high-affinity, high-velocity system. The inhibitory effects of the sugars on the high-affinity system also indicated the role of the phosphoenolpyruvate-dependent phosphotransferase system in mediating glucose transport by ruminal bacteria.

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