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Heterologous Expression And Characterization Of A High Redox Potential Laccase Fromcoriolopsis Polyzona Mucl 38443, Orkun Pi̇nar, Candan Tamerler Behar, Ayten Karataş
Heterologous Expression And Characterization Of A High Redox Potential Laccase Fromcoriolopsis Polyzona Mucl 38443, Orkun Pi̇nar, Candan Tamerler Behar, Ayten Karataş
Turkish Journal of Biology
In this study, a novel laccase gene, named as Cplcc1, and its corresponding cDNA were isolated and characterized from the Coriolopsis polyzona MUCL 38443 strain. The Cplcc1 gene consists of a 1563-bp open reading frame encoding a protein of 520 amino acids with a 20-residue putative signal peptide. The size of the Cplcc1 gene is 2106 bp and it contains ten introns and five potential N-glycosylation sites. Additionally, the isolated full-length Cplcc1 cDNA was successfully expressed in Pichia pastoris. The heterologous expression conditions were also optimized and the highest activity value increased to 800 U L-1 with 1.5% methanol, 0.8 …
Cloning, Expression, And Activity Analysis Of Human Cathepsin C In The Yeast Pichia Pastoris, Cenk Dağlioğlu
Cloning, Expression, And Activity Analysis Of Human Cathepsin C In The Yeast Pichia Pastoris, Cenk Dağlioğlu
Turkish Journal of Biology
The yeast Pichia pastorisexpression system was investigated for the production of human cathepsin C (CatC) recombinant protein. The full-length CatC cDNA, corresponding to amino acids 12-475, was synthesized from interleukin-2 (IL-2) stimulated human peripheral blood mononuclear cells and subcloned in the pGEM-T cloning vector. After confirming the DNA sequence of the insert, the gene was cloned into the pPICZ\alphaA expression vector under the control of the methanol-inducible alcohol oxidase (AOX1) promoter and transformed to P. pastoris X-33 cells. The expressed protein was secreted into the culture medium through the alpha-factor mating signal sequence of the expression vector. Analysis of the …