Article 2021 · 34 citations

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

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 degrees C), and showed optimum activity at pH 9 and 60 degrees C. Km and Vmax for pNPP hydrolysis were 0.88 mM and 34.2 U/mg protein, respectively. Ba2+, Ca2+, Co2+, Cu2+, Fe3+, and Mg2+ increased activity, while Mn2+, Mo2+, Ni2+, Zn2+, 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.

Keywords

Aeromonas caviae Thermoactive lipase Alkaline lipase Purification Detergent SOLVENT-TOLERANT LIPASE PSEUDOMONAS-AERUGINOSA STRAIN THERMOSTABLE LIPASE STABLE LIPASE BACTERIUM EXPRESSION

WoS Categories

Biochemical Research Methods Biochemistry & Molecular Biology Biotechnology & Applied Microbiology

Citation

Journal: PROTEIN EXPRESSION AND PURIFICATION
Year: 2021
Volume: 180
ISSN: 1046-5928
eISSN: 1096-0279
DOI: 10.1016/j.pep.2021.105819
WoS UID: WOS:000754982600007

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