Maraite, A., Hoyos, P., Carballeira, J.D., Cabrera, A.C., Ansorge-Schumacher, M.B. and Alcantara, A.R. (2013) Lipase from Pseudomonas stutzeri: Purification, Homology Modelling and Rational Explanation of the Substrate Binding Mode. Journal of Molecular Catalysis B-Enzymatic, 87, 88-98.
http://dx.doi.org/10.1016/j.molcatb.2012.11.005

has been cited by the following article:

• TITLE: Characterization of a Novel Pseudomonas stutzeri Lipase/Esterase with Potential Application in the Production of Chiral Secondary Alcohols

  AUTHORS: Sven C. Lehmann, Andy Maraite, Max Steinhagen, Marion B. Ansorge-Schumacher

  KEYWORDS: Pseudomonas, Screening, Lipase, Esterase, Kinetics

  JOURNAL NAME: Advances in Bioscience and Biotechnology, Vol.5 No.13, November 12, 2014

  ABSTRACT: The search for new enzymes is facilitated by the rapidly growing number of genome sequences from different organisms. However, the discovery of functional proteins is still time intensive and complex alignments have to be performed. Herein, a genome database search identified a new, until now undescribed, putative lipase from Pseudomonas stutzeri strain A1501. The gene was cloned and expressed as functional protein in E. coli. A biochemical characterization provided an indication that the enzyme could be classified as an esterase with an alkaline pH optimum and a temperature optimum at 50°C. The enzyme was able to perform the kinetic resolution of racemic esters and could therefore be an interesting candidate for chiral synthesis.