Lipase from Rhizopus oryzae R1: in-depth characterization, immobilization, and evaluation in biodiesel production
Shimaa E. Helal | Hemmat M. Abdelhady | Khadiga A. Abou-Taleb | Mervat G. Hassan | Mahmoud M. Amer
Abstract Background Rhizopus species is among the most well-known lipase producers, and its enzyme is suitable for use in many industrial applications. Our research focuses on the production of lipase utilizing waste besides evaluating its applications. Results An extracellular lipase was partially purified from the culture broth of Rhizopus oryzae R1 isolate to apparent homogeneity using ammonium sulfate precipitation followed by desalting via dialysis. The partially purified enzyme was non-specific lipase and the utmost activity was recorded at pH 6, 40 °C with high stability for 30 min. The constants K m and V max, calculated from the Lineweaver-Burk plot, are 0.3 mg/mL and 208.3 U/mL, respectively. Monovalent metal ions such as Na+ (1 and 5 mM) and K+ (5 mM) were promoters of the lipase to enhance its activity with 110, 105.5, and 106.5%, respectively. Chitosan was used as a perfect support for immobilization via both adsorption and cross-linking in which the latter method attained immobilization efficiency of 99.1% and reusability of 12 cycles. The partially purified enzyme proved its ability in forming methyl oleate (biodiesel) through the esterification of oleic acid and transesterification of olive oil. Conclusion The partially purified and immobilized lipase from Rhizopus oryzae R1 approved excellent efficiency, reusability, and a remarkable role in detergents and biodiesel production.
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