Expression of a Deschampsia antarctica Desv. Polypeptide with Lipase Activity in a Pichia pastoris Vector

The current study isolated and characterized the Lip3F9 polypeptide sequence of Deschampsia antarctica Desv. (GeneBank Accession Number JX846628), which was found to be comprised of 291 base pairs and was, moreover, expressed in Pichia pastoris X-33 cells. The enzyme was secreted after 24 h of P. pa...

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Bibliographic Details
Published in:International Journal of Molecular Sciences
Main Authors: Rabert, Claudia, Gutiérrez-Moraga, Ana, Navarrete-Gallegos, Alejandro, Navarrete-Campos, Darío, Bravo, León A., Gidekel, Manuel
Format: Text
Language:English
Published: Molecular Diversity Preservation International (MDPI) 2014
Subjects:
Short Note
Antarc*
Antarctica
Online Access:http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3958855
http://www.ncbi.nlm.nih.gov/pubmed/24514564
https://doi.org/10.3390/ijms15022359
Description
Summary:The current study isolated and characterized the Lip3F9 polypeptide sequence of Deschampsia antarctica Desv. (GeneBank Accession Number JX846628), which was found to be comprised of 291 base pairs and was, moreover, expressed in Pichia pastoris X-33 cells. The enzyme was secreted after 24 h of P. pastoris culture incubation and through induction with methanol. The expressed protein showed maximum lipase activity (35 U/L) with an optimal temperature of 37 °C. The lipase-expressed enzyme lost 50% of its specific activity at 25 °C, a behavior characteristic of a psychrotolerant enzyme. Recombinant enzyme activity was measured in the presence of ionic and non-ionic detergents, and a decrease in enzyme activity was detected for all concentrations of ionic and non-ionic detergents assessed.

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