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1	A disulfide bridge in the calcium binding site of a polyester hydrolase increases its thermal stability and activity against polyethylene terephthalate Then, Johannes, Wei, Ren, Oeser, Thorsten, Gerdts, André, Schmidt, Juliane, Barth, Markus, Zimmermann, Wolfgang 23 June 2016 (has links) (PDF) Elevated reaction temperatures are crucial for the efficient enzymatic degradation of polyethylene terephthalate (PET). A disulfide bridge was introduced to the polyester hydrolase TfCut2 to substitute its calcium binding site. The melting point of the resulting variant increased to 94.7°C (wild-type TfCut2: 69.8 °C) and its half-inactivation temperature to 84.6 °C (TfCut2: 67.3 °C). The variant D204C-E253C-D174R obtained by introducing further mutations at vicinal residues showed a temperature optimum between 75 and 80 °C compared to 65 and 70 °C of the wild-type enzyme. The variant caused a weight loss of PET films of 25.0 +/- 0.8% (TfCut2: 0.3 +/-0.1%) at 70 °C after a reaction time of 48 h. The results demonstrate that a highly efficient and calcium-independent thermostable polyester hydrolase can be obtained by replacing its calcium binding site with a disulfide bridge. Biokatalyse Kalzium Disulfidbrücke Polyethylenterephthalat Protein-Engineering Proteinstabilität biocatalysis calcium disulfide bridge polyethylene terephthalate protein engineering protein stability ddc:540 ddc:570
2	Localization and Stability of the Transcriptional Activator Gcn4p of Saccharomyces cerevisiae / Lokalisierung und Stabilität des Transkriptionsaktivators Gcn4p in Saccharomyces cerevisiae Pries, Ralph 28 January 2003 (has links) No description available. 570 Biowissenschaften, Biologie Mathematics and Computer Science Saccharomyces cerevisiae Gcn4p Zellkern Proteinstabilität Saccharomyces cerevisiae Gcn4p Nucleus protein stability 42.13 Molekularbiologie WU Mikrobiologie WU Mikrobiologie
3	Gezielte Modifikation sowie Analyse der Bindungseigenschaften des Histidin Bindeproteins aus Escherichia coli und des GCN4 Leucinzippers aus Saccharomyces cerevisiae / Modification and analysis of the binding properties of the histidine-binding protein from Escherichia coli and the GCN4-Leucine zipper from Saccharomyces cerevisiae Wittmann, Julia 31 October 2002 (has links) No description available. 570 Biowissenschaften, Biologie Mathematics and Computer Science Rezeptor-Liganden-Wechselwirkung Protein-Protein-Wechselwirkun direkte Mutagenese Proteinstabilität Receptor-ligand interaction protein-protein interaction direct mutagenesis protein stbility 42.13 42.20 42.30 WJ 000: Genetik {Biologie}
4	A disulfide bridge in the calcium binding site of a polyester hydrolase increases its thermal stability and activity against polyethylene terephthalate Then, Johannes, Wei, Ren, Oeser, Thorsten, Gerdts, André, Schmidt, Juliane, Barth, Markus, Zimmermann, Wolfgang January 2016 (has links) Elevated reaction temperatures are crucial for the efficient enzymatic degradation of polyethylene terephthalate (PET). A disulfide bridge was introduced to the polyester hydrolase TfCut2 to substitute its calcium binding site. The melting point of the resulting variant increased to 94.7°C (wild-type TfCut2: 69.8 °C) and its half-inactivation temperature to 84.6 °C (TfCut2: 67.3 °C). The variant D204C-E253C-D174R obtained by introducing further mutations at vicinal residues showed a temperature optimum between 75 and 80 °C compared to 65 and 70 °C of the wild-type enzyme. The variant caused a weight loss of PET films of 25.0 +/- 0.8% (TfCut2: 0.3 +/-0.1%) at 70 °C after a reaction time of 48 h. The results demonstrate that a highly efficient and calcium-independent thermostable polyester hydrolase can be obtained by replacing its calcium binding site with a disulfide bridge. info:eu-repo/classification/ddc/540 ddc:540 info:eu-repo/classification/ddc/570 ddc:570

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