57
views
0
recommends
+1 Recommend
0 collections
    0
    shares
      • Record: found
      • Abstract: found
      • Article: found
      Is Open Access

      Isolation and identification of a novel, lipase-producing bacterium, Pseudomnas aeruginosa KM110

      research-article

      Read this article at

      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Abstract

          Background and Objectives

          Lipases are particularly important due to the fact that they specifically hydrolyze acyl glycerol, oils and greases, which is of great interest for different industrial applications.

          Materialst and Methods

          In this study, several lipase-producing bacteria were isolated from wastewater of an oil processing plant. The strain possessing the highest lipase activity was identified both biochemically and sequencing of 16S rRNA gene. Then we increase lipase activity by improving conditions of production medium. Also, lipase from this strain was preliminarily characterized for use in industrial application.

          Results

          The 16S rRNA sequensing revealed it as a new strain of Pseudomonas aeruginosa and the type strain was KM110. An overall 3-fold enhanced lipase production (0.76 U mL −1) was achieved after improving conditions of production medium. The olive oil and peptone was found to be the most suitable substrate for maximum enzyme production. Also the enzyme exhibited maximum lipolytic activity at 45°C where it was also stably maintained. At pH 8.0, the lipase had the highest stability but no activity. It was active over a pH range of 7.0–10.0. The lipase activity was inhibited by Zn 2+ & Cu 2+ (32 and 27%, respectively) at 1mM. The enzyme lost 29% of its initial activity in 1.0% SDS concentration, whereas, Triton X-100, Tween-80 & DMSO did not significantly inhibit lipase activity.

          Conclusions

          Based on the findings of present study, lipase of P. aeruginosa KM110 is a potential alkaline lipase and a candidate for industrial applications such as detergent, leather and fine chemical industries.

          Related collections

          Most cited references47

          • Record: found
          • Abstract: found
          • Article: not found

          Bacterial lipolytic enzymes: classification and properties.

          Knowledge of bacterial lipolytic enzymes is increasing at a rapid and exciting rate. To obtain an overview of this industrially very important class of enzymes and their characteristics, we have collected and classified the information available from protein and nucleotide databases. Here we propose an updated and extensive classification of bacterial esterases and lipases based mainly on a comparison of their amino acid sequences and some fundamental biological properties. These new insights result in the identification of eight different families with the largest being further divided into six subfamilies. Moreover, the classification enables us to predict (1) important structural features such as residues forming the catalytic site or the presence of disulphide bonds, (2) types of secretion mechanism and requirement for lipase-specific foldases, and (3) the potential relationship to other enzyme families. This work will therefore contribute to a faster identification and to an easier characterization of novel bacterial lipolytic enzymes.
            Bookmark
            • Record: found
            • Abstract: found
            • Article: not found

            Bacterial lipases: an overview of production, purification and biochemical properties.

            Lipases, triacylglycerol hydrolases, are an important group of biotechnologically relevant enzymes and they find immense applications in food, dairy, detergent and pharmaceutical industries. Lipases are by and large produced from microbes and specifically bacterial lipases play a vital role in commercial ventures. Some important lipase-producing bacterial genera include Bacillus, Pseudomonas and Burkholderia. Lipases are generally produced on lipidic carbon, such as oils, fatty acids, glycerol or tweens in the presence of an organic nitrogen source. Bacterial lipases are mostly extracellular and are produced by submerged fermentation. The enzyme is most commonly purified by hydrophobic interaction chromatography, in addition to some modern approaches such as reverse micellar and aqueous two-phase systems. Most lipases can act in a wide range of pH and temperature, though alkaline bacterial lipases are more common. Lipases are serine hydrolases and have high stability in organic solvents. Besides these, some lipases exhibit chemo-, regio- and enantioselectivity. The latest trend in lipase research is the development of novel and improved lipases through molecular approaches such as directed evolution and exploring natural communities by the metagenomic approach.
              Bookmark
              • Record: found
              • Abstract: found
              • Article: not found

              Production, purification, characterization, and applications of lipases

              Biotechnology Advances, 19(8), 627-662
                Bookmark

                Author and article information

                Journal
                Iran J Microbiol
                IJM
                Iranian Journal of Microbiology
                Tehran University of Medical Sciences
                2008-3289
                2008-4447
                June 2011
                : 3
                : 2
                : 92-98
                Affiliations
                Department of Biology, Alzahra University, Vanak, Tehran, Iran
                Author notes
                [* ]Corresponding author: Rouha Kasra-Kermanshahi Ph.D Address: Department of Biology, Alzahra University, Vanak, Tehran, Iran.Tel: +98-913-1150779. E-mail: rkasra@ 123456yahoo.com
                Article
                IJM-3-092
                3279805
                22347589
                cd517397-e58c-4bbd-a9d3-0f4b5e47bfab
                © 2011 Iranian Society of Microbiology & Tehran University of Medical Sciences

                This work is licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported License which allows users to read, copy, distribute and make derivative works for non-commercial purposes from the material, as long as the author of the original work is cited properly.

                History
                : February 2011
                : April 2011
                Categories
                Original Artical

                Microbiology & Virology
                pseudomonas aeruginosa,lipase,stability
                Microbiology & Virology
                pseudomonas aeruginosa, lipase, stability

                Comments

                Comment on this article