We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
Enhanced thermal stability and specific activity of Pseudomonas aeruginosa lipoxygenase by fusing with self-assembling amphipathic peptides.
- Authors
Lu, Xinyao; Liu, Song; Zhang, Dongxu; Zhou, Xiaoman; Wang, Miao; Liu, Yi; Wu, Jing; Du, Guocheng; Chen, Jian
- Abstract
Self-assembling amphipathic peptides (SAPs) are a category of peptides that have unique sequences with alternating hydrophobic and hydrophilic residues that can spontaneously assemble into ordered nanostructures. In this study, we investigated the potential of fusion technique with SAPs to improve the thermal stability of lipoxygenase (LOX) from Pseudomonas aeruginosa. Six SAPs were individually fused to the N terminus of the LOX that resulted to the SAP-LOX fusions with approximately 2.3- to 4.5-fold enhanced thermal stability at 50 °C. The specific activities of the SAP-LOX fusions were also increased by 1.0- to 2.8-fold as compared with the wild-type LOX. This is the first report on the improvement of the thermal stability and specific activity of an enzyme by the fused SAPs, suggesting a simple technique to improve the catalytic properties of the recombinant enzymes by fusion expression.
- Subjects
PSEUDOMONAS aeruginosa; BACTERIAL enzymes; THERMAL stability; LIPOXYGENASES; ENZYME activation; GENE expression in bacteria
- Publication
Applied Microbiology & Biotechnology, 2013, Vol 97, Issue 21, p9419
- ISSN
0175-7598
- Publication type
Academic Journal
- DOI
10.1007/s00253-013-4751-y