Functional and molecular characterization of a cold-active lipase from Psychrobacter celer PU3 with potential antibiofilm property

Autor:	Palanichamy, Esakkiraj, Christian, Bharathi, Repally, Ayyanna, Natwar, Jha, Akshaya, Panigrahi, Ponnuraj, Karthe, Venkatesan, Arul
Rok vydání:	2022
Předmět:	Temperature Psychrobacter Lipase General Medicine Hydrogen-Ion Concentration Biochemistry Substrate Specificity Structural Biology Biofilms Enzyme Stability Escherichia coli Solvents Molecular Biology Phylogeny
Zdroj:	International Journal of Biological Macromolecules. 211:741-753
ISSN:	0141-8130
DOI:	10.1016/j.ijbiomac.2022.04.174
Popis:	The lipase gene from Psychrobacter celer PU3 was cloned into pET-28a(+) expression vector and overexpressed in E. coli BL21 (DE3) pLysS cells. The purified Psychrobacter celer lipase (PCL) was characterized as an alkaline active enzyme and has a molecular mass of around 30 kDa. The PCL was active even at a low temperature and the optimum range was observed between 10 and 40 °C temperatures. MALDI-TOF and phylogenetic analysis ensured that Psychrobacter celer PU3 lipase (PCL) was closely related to P. aureginosa lipase (PAL). MD simulation results suggest that temperature change did not affect the overall structure of PCL, but it might altered the temperature-dependent PCL functional changes. R
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d3c51f9f79ff022c3bf0cee0d5199afc https://doi.org/10.1016/j.ijbiomac.2022.04.174 Zobrazit plný text záznamu Full Text from ScienceDirect