Kinetic and thermodynamic characterization of lipase produced by Cellulomonas flavigena UNP3. (26th May 2013)

• Record Type: Journal Article
• Authors: Prajapati, Vimal; Patel, Honey; Trivedi, Ujjval; Patel, Kamlesh
• Is Part Of: Journal of basic microbiology. Volume 54:issue 9(2014:Sep.)
• Page Start: 976
• Page End: 983
• Publication Date: 2013-05-26
• Subjects: Microbiology -- Periodicals; 579
• DOI: 10.1002/jobm.201300065
• Languages: English
• ISSNs: 0233-111X

Abstract

<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <sec id="jobm201300065-sec-0001" sec-type="section"> <p>Lipase of <italic>Cellulomonas flavigena</italic> UNP3 was purified by two‐step purification process comprising ammonium sulfate precipitation followed by gel permeation chromatography (GPC). The recovery of lipase after GPC was found to be 1.70% with 20.98‐fold increase in specific activity. The molecular weight of lipase protein was found to be 45.2 kDa by SDS–PAGE. Activation energy for <italic>p</italic>‐nitrophenol palmitate (pNPP) hydrolysis was 26.45 kJ mol⁻¹, while temperature quotient (<italic>Q</italic>₁₀) was found to be 1.64. The enzyme was found to be stable over wide pH range and thermally stable at 30–40 °C up to 60 min of incubation while exhibited maximum activity at 30 °C with pH 7.0. <italic>V</italic>_max, <italic>K</italic>_m, and <italic>K</italic>_cat for pNPP were found to be 666.71 U ml⁻¹, 1.33 mM (pNPP) and 433 min⁻¹, respectively. Activation energy for irreversible inactivation <italic>E</italic>_a(d) of lipase was 64.32 kJ mol⁻¹. Thermodynamic parameters of irreversible inactivation of lipase and pNPP hydrolysis were also determined.</p> </sec> </abstract>