Your browser doesn't support javascript.
loading
An oxidant and organic solvent tolerant alkaline lipase by P. aeruginosa mutant: downstream processing and biochemical characterization
Bisht, Deepali; Yadav, Santosh Kumar; Darmwal, Nandan Singh.
  • Bisht, Deepali; Dr. Ram Manohar Lohia Avadh University. Department of Microbiology. Centre of Excellence. Faizabad. IN
  • Yadav, Santosh Kumar; Dr. Ram Manohar Lohia Avadh University. Department of Microbiology. Centre of Excellence. Faizabad. IN
  • Darmwal, Nandan Singh; Dr. Ram Manohar Lohia Avadh University. Department of Microbiology. Centre of Excellence. Faizabad. IN
Braz. j. microbiol ; 44(4): 1305-1314, Oct.-Dec. 2013. ilus, tab
Article in English | LILACS | ID: lil-705271
ABSTRACT
An extracellular alkaline lipase from Pseudomonas aeruginosa mutant has been purified to homogeneity using acetone precipitation followed by anion exchange and gel filtration chromatography and resulted in 27-fold purification with 19.6% final recovery. SDS-PAGE study suggested that the purified lipase has an apparent molecular mass of 67 kDa. The optimum temperature and pH for the purified lipase were 45°C and 8.0, respectively. The enzyme showed considerable stability in pH range of 7.0-11.0 and temperature range 35-55 °C. The metal ions Ca2+, Mg2+ and Na+ tend to increase the enzyme activity, whereas, Fe2+ and Mn2+ ions resulted in discreet decrease in the activity. Divalent cations Ca+2 and Mg+2 seemed to protect the enzyme against thermal denaturation at high temperatures and in presence of Ca+2 (5 mM) the optimum temperature shifted from 45°C to 55°C. The purified lipase displayed significant stability in the presence of several hydrophilic and hydrophobic organic solvents (25%, v/v) up to 168 h. The pure enzyme preparation exhibited significant stability and compatibility with oxidizing agents and commercial detergents as it retained 40-70% of its original activities. The values of Km and Vmax for p-nitrophenyl palmitate (p-NPP) under optimal conditions were determined to be 2.0 mg.mL-1 and 5000 μg.mL-1.min-1, respectively.
Subject(s)


Full text: Available Index: LILACS (Americas) Main subject: Pseudomonas aeruginosa / Lipase Language: English Journal: Braz. j. microbiol Journal subject: Microbiology Year: 2013 Type: Article Affiliation country: India Institution/Affiliation country: Dr. Ram Manohar Lohia Avadh University/IN

Similar

MEDLINE

...
LILACS

LIS


Full text: Available Index: LILACS (Americas) Main subject: Pseudomonas aeruginosa / Lipase Language: English Journal: Braz. j. microbiol Journal subject: Microbiology Year: 2013 Type: Article Affiliation country: India Institution/Affiliation country: Dr. Ram Manohar Lohia Avadh University/IN