Purification and characterization of a novel extracellular, alkaline, thermoactive, and detergent-compatible lipase from Aeromonas caviae LipT51 for application in detergent industry.

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  • Author(s): Gurkok S;Gurkok S; Ozdal M; Ozdal M
  • Source:
    Protein expression and purification [Protein Expr Purif] 2021 Apr; Vol. 180, pp. 105819. Date of Electronic Publication: 2021 Jan 05.
  • Publication Type:
    Journal Article; Research Support, Non-U.S. Gov't
  • Language:
    English
  • Additional Information
    • Source:
      Publisher: Academic Press Country of Publication: United States NLM ID: 9101496 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1096-0279 (Electronic) Linking ISSN: 10465928 NLM ISO Abbreviation: Protein Expr Purif Subsets: MEDLINE
    • Publication Information:
      Publication: Orlando, FL : Academic Press
      Original Publication: San Diego : Academic Press, c1990-
    • Subject Terms:
      Bacterial Proteins*/chemistry ; Bacterial Proteins*/genetics ; Bacterial Proteins*/isolation & purification ; Lipase*/chemistry ; Lipase*/genetics ; Lipase*/isolation & purification; Aeromonas caviae/*genetics; Aeromonas caviae/enzymology ; Chemical Industry ; Detergents ; Enzyme Stability ; Recombinant Proteins/chemistry ; Recombinant Proteins/genetics ; Recombinant Proteins/isolation & purification
    • Abstract:
      Lipase producer bacterium isolated from Erzurum was identified as Aeromonas caviae LipT51 (GenBank ID: MN818567.1) by 16S rDNA sequencing and conventional methods. Extracellular lipase was purified by ammonium sulphate precipitation, centrifugal filtration, and anion-exchange chromatography resulting in 6.1-fold purification with 28% final yield. Molecular weight was 31.6 kDa on SDS-PAGE. Lipase was stable over a broad range of pH (6-11) and temperature (25-70 °C), and showed optimum activity at pH 9 and 60 °C. Km and Vmax for pNPP hydrolysis were 0.88 mM and 34.2 U/mg protein, respectively. Ba 2+ , Ca 2+ , Co 2+ , Cu 2+ , Fe 3+ , and Mg 2+ increased activity, while Mn 2+ , Mo 2+ , Ni 2+ , Zn 2+ , and other additives partially decreased. Activity and stability increased with laundry detergent and slightly decreased with handwash and dishwashing detergents. Alkaline and thermostable lipase from newly isolated A. caviae has been shown for the first time to be remarkably compatible with laundry detergent and improve washing performance by enhanced oil-stain removal.
      (Copyright © 2021 Elsevier Inc. All rights reserved.)
    • Contributed Indexing:
      Keywords: Aeromonas caviae; Alkaline lipase; Detergent; Purification; Thermoactive lipase
    • Accession Number:
      0 (Bacterial Proteins)
      0 (Detergents)
      0 (Recombinant Proteins)
      EC 3.1.1.3 (Lipase)
    • Publication Date:
      Date Created: 20210108 Date Completed: 20210805 Latest Revision: 20210805
    • Publication Date:
      20240829
    • Accession Number:
      10.1016/j.pep.2021.105819
    • Accession Number:
      33418059