AI Article Synopsis
- The study focuses on cloning and expressing a lipase gene from Trichosporon coremiiforme V3, revealing a gene sequence of 1,692 bp that codes for a 563 amino acid protein.
- The lipase was overexpressed in Pichia pastoris X33, achieving a maximum activity of 5,000 U/ml after methanol induction in a bioreactor.
- The purified enzyme exhibits high temperature stability, retaining 45% activity at 70 °C, along with specific activity towards certain fatty acids.
Article Abstract
The present study describes the gene cloning and high-level expression of an alkaline and thermostable lipase gene from Trichosporon coremiiforme V3. Nucleotide analysis revealed that this lipase gene has an open reading frame of 1,692 bp without any introns, encoding a protein of 563 amino acid residues. The lipase gene without its signal sequence was cloned into plasmid pPICZαA and overexpressed in Pichia pastoris X33. The maximum lipase activity of recombinant lipase was 5,000 U/ml, which was obtained in fed-batch cultivation after 168 h induction with methanol in a 50 L bioreactor. The purified lipase showed high temperature tolerance, and being stable at 60 °C and kept 45% enzyme activity after 1 h incubation at 70 °C. The stability, effects of metal ions and other reagents were also determined. The chain length specificity of the recombinant lipase showed high activity toward triolein (C18:1) and tripalmitin (C16:0).
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| http://dx.doi.org/10.4014/jmb.1408.08039 | DOI Listing |
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