Document Type

Article

Rights

Available under a Creative Commons Attribution Non-Commercial Share Alike 4.0 International Licence

Disciplines

1. NATURAL SCIENCES, Organic Chemistry, 1.6 BIOLOGICAL SCIENCES, Biochemistry and molecular biology, Biochemical research methods, Biology

Publication Details

Protein Expression and Purification, 153, 121-130 (2019)

https://doi.org/10.1016/j.pep.2018.08.007

Abstract

The Pseudomonas sp. have been long recognized for their exogenous lipolytic activities yet the genus still contains a lot of unexplored strains. Due to the versatile metabolic machinery and their potential for adaptation to fluctuating environmental conditions Pseudomonas sp. are of great interest for biotechnological applications. In this study, a new extracellularly produced lipolytic enzyme from Pseudomonas sp. (P. reinekei) was purified and characterized. The production of lipase from P. reinekei (H1) was enhanced 10-fold by optimizing the nitrogen source. The 50 kDa H1 lipase was purified using negative and positive mode anion exchange chromatography. The purified lipase was active over a broad pH range (5.0-9.0) and was stable for 24h at 40°C. The lipase showed significant stability, and indeed activation, in the presence of organic solvents with log P≥ 2.0. These features render this lipase of interest as a biocatalyst for applications such as biodiesel production, detergent formulations and biodegradation of oil in the environment.

DOI

https://doi.org/10.1016/j.pep.2018.08.007

Funder

Technological University Dublin

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