BIOCHEMICAL AND IN-SILICO STRUCTURAL ASSESSMENTS OF AN Acinetobacter haemolyticus LIPASE KV1 ISOLATED FROM AN OIL PALM MILL EFFLUENT

Authors

  • KALAIVANI BATUMALAIE Department of Chemistry, Faculty of Science, Universiti Teknologi Malaysia, 81310 UTM Johor Bahru, Malaysia
  • NAJI ARAFAT MAHAT Department of Chemistry, Faculty of Science, Universiti Teknologi Malaysia, 81310 UTM Johor Bahru, Malaysia
  • FAHRUL HUYOP Department of Biotechnology and Medical Engineering, Faculty of Biosciences and Medical Engineering, Universiti Teknologi Malaysia, 81310 UTM Johor, Malaysia
  • ROSWANIRA ABDUL WAHAB Department of Chemistry, Faculty of Science, Universiti Teknologi Malaysia, 81310 UTM Johor Bahru, Malaysia

Keywords:

Acinetobacter haemolyticus, lipase, purification, biochemical characterization, reducing agents

Abstract

The use of microbial enzymes as biocatalysts for a myriad of commercial processes are currently trending owing to their versatility and, their use is considerably greener than the chemically-assisted methods. In this regard, this study reports the comprehensive biochemical characterization of a lipase from novel Acinetobacter haemolyticus KV1 bacteria. The intracellular lipase was purified to ~3.5-fold using consecutive treatments of ammonium sulfate precipitation, dialysis and DEAE-cellulose ion exchange chromatography. The purified lipase exhibited maximum relative activity at 40°C and pH 8.0, respectively. Lipase KV1 was significantly activated (p < 0.05) in reactions supplemented with metal ions, Na+, Ca2+, K+ and Mg2+ (112– 128%) as well as surfactants, Tween 20–80 (110–143%). The lipase hydrolyzed a wide range of oils with tributyrin (140%) being the preferred ones. Reducing (PMSF, DTT, b-mercaptoethanol) and chelating (EDTA) agents significantly inhibited the lipase (p < 0.05) and, significant inhibition was also evident for Triton-X100, SDS, SLS and CTAB (p < 0.05). Interestingly, lipase KV1 retained its relative activities at > 50% for up to 24 h for pH between pH 7-11. Therefore, the full characterization of lipase KV1 reported in this study deserves scientific and economic considerations.

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Published

30-06-2018

How to Cite

BATUMALAIE, K. ., MAHAT, N. A. ., HUYOP, F. ., & ABDUL WAHAB, R. . (2018). BIOCHEMICAL AND IN-SILICO STRUCTURAL ASSESSMENTS OF AN Acinetobacter haemolyticus LIPASE KV1 ISOLATED FROM AN OIL PALM MILL EFFLUENT. Malaysian Applied Biology, 47(3), 59–69. Retrieved from https://jms.mabjournal.com/index.php/mab/article/view/2043

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Section

Research Articles