Abstract

Lipase from Aspergillus flavus was purified in a single step purification using MnFeO4 magnetic nano particles to achieve a 20.53- fold purification with specific activity of 11.29 U/mg and a 59% recovery yield. SDS-PAGE of lipase showed a single pure band with corresponding molecular weight of 35 kDa. The optimal temperature and pH for the enzyme activity were 45°C and 7.0 respectively. Addition of olive oil (1 %w/v) enhanced pH stability of the lipase with 86% residual activity at pH 7.0 after 6 h of incubation while the lipase was thermostable with 79% residual activity after 4 h of incubation. The enzyme activity was enhanced by Ca 2+ , Mg 2+ and Mn2+ while the presence of Cu 2+ , Co 2+ and Zn 2+ exhibited inhibitory effect on the enzyme. The study therefore presented lipase from Aspergillus flavus PW2961 with potential in industrial and biotechnological application. Key words : Lipase, purification, Aspergillus flavus PW2961, magnetic nanoparticles

Highlights

  • Lipases (EC 3.1.1.3) are enzymes capable of catalyzing the hydrolysis of fatty acids and glycerol into its monomeric units (Sharma et al, 2001)

  • This purification fold is higher than previous report on a single step technique (Kareem and Akpan, 2003)

  • This pH range was reported to offer wide industrial application (Romero et al, 2007). This findings is similar to that reported by Kamini et al, (1998) for lipase activity from Aspergillus niger MTCC 2594

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Summary

Introduction

Lipases (EC 3.1.1.3) are enzymes capable of catalyzing the hydrolysis of fatty acids and glycerol into its monomeric units (Sharma et al, 2001). Lipase from Aspergillus flavus was purified using magnetic nanoparticles (MNPs). Crude enzyme extract was filtered using filter paper (Whatman, 125 mm), centrifuged at 8000 rpm for 20 min and the enzyme activity was determined.

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