Effect of surface hydrophobicity on activity of immobilized Taq DNA polymerase, its reusability and storage.

Effect of surface hydrophobicity on activity of immobilized Taq DNA polymerase, its reusability and storage.

Oriented methods and activity-preserved immobilization of biologically active proteins based on the concept of active-site masking and previously reported kinetic control. We extended our research and found that hydrophobic surfaces have a noticeable effect on the activity of the active-protected site move (PIM) Taq DNA polymerase in a mixture of assembled monolayer (SAM) is produced on the Au surface. Hydrophobic SAM created using 12-mercaptododecanoic acid and 1-heptanethiol.

Taq DNA polymerase activity generated is measured by PCR amplification and compared with previously reported values ​​obtained with the hydrophilic SAM. The maximum activity of the immobilized Taq DNA polymerase was achieved in 17.5% of 12-mercaptododecanoic acid and within 90 minutes of reaction time is higher than that obtained with the hydrophilic SAM; The maximum activity by 5% 12-mercaptododecanoic acid and at 10 minutes. To apply to a commercial level, moving enzymes have to be stable, reusable and can be stored. PIM stable Taq DNA polymerase attached to the surface and can be used for as many as 10 runs PCR comparable with enzyme-phase solution. Even after 56 days of storage at 4 ° C, the immobilized enzyme classified as 70% of the initial PIM enzyme activity. These data indicate that the PIM Taq DNA polymerase can be used for a variety of commercial applications.


DNA polymerases are enzymes that play an important role in DNA metabolism such as replication, repair, transcription, recombination, and chromosome segregation during mitosis. Here we report the isolation of a new iridoid (6-epi-catalpol, 2) and the per-O-acetyl-verbascoside (11) of the aerial parts of Buddleja cordobensis Grisebach (Buddlejaceae). Of the compound 2, we have obtained eight compounds with chemical transformations. This group of compounds at a concentration of 500μM tested against Taq DNA polymerase.

Compound 11 (per-O-acetyl-verbascoside) was the most active with IC50 of 1.21 ± 0.18μM; Compound 9, 2 and 8 are strong inhibitors with IC50 values ​​of 5:57 ± 0.70, 21.62 ± 0.22 and 78.13 ± 0.93μM, respectively. Compound 11 and 9 could be the structure of a new leader for the development of anticancer drugs chemotherapy and useful tools to investigate the activity of DNA polymerase.

 Effect of surface hydrophobicity on activity of immobilized Taq DNA polymerase, its reusability and storage.
Effect of surface hydrophobicity on activity of immobilized Taq DNA polymerase, its reusability and storage.

The stability of Taq DNA polymerase result of folding entropic penalty is reduced; identification of other thermophilic proteins with a similar folding thermodynamics.

The thermal stability of Taq DNA polymerase known, and is the basis for use in PCR. A comparison of the thermodynamic characterization of a large fragment of Taq domain (Klentaq) and E. coli (Klenow) of DNA polymerase has done by getting the Gibbs-Helmholtz stability curve full folding free energy (AG) versus temperature. This analysis provides temperature dependencies folding enthalpy and entropy (ΔH and ΔS), and heat capacity (ΔCp) fold.

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If increased or enhanced non-covalent bonding in the original state is responsible for increasing the thermal stabilization of proteins, such as frequently asked questions, then folding enthalpy enhanced benefit should, in general, observed for thermophilic proteins. However, for Klenow-Klentaq homologous pairs, folding enthalpy (ΔHfold) of Klentaq far less profitable than Klenow at all temperatures. Instead, it was found that the free energy of folding extreme Klentaq (ΔGfold) comes from the entropic penalty significantly reduces the fold (ΔSfold). In addition, the heat capacity change at a similar fold for Klenow and Klentaq.

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