Macaúba (Acrocomia aculeata) cake from biodiesel processing: A low-cost substrate to produce lipases from Moniliella spathulata R25L270 with potential application in the oleochemical industry

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Abstract

Background: Biodiesel industry wastes were evaluated as supplements for lipase production by Moniliella spathulata R25L270, which is newly identified yeast with great lipolytic potential. Macaúba cake (MC), used for the first time in this work as inducer to produce lipases, and residual oil (RO) were mixed to maximise enzyme production. The lipase secreted was biochemically characterised. Results: The best ratio for the mixture (MC:RO) was 0.66:0.34 and the fitted values for lipase activity and total protein concentration were 0.98 U mL -1 and 0.356 mg mL -1, respectively. Maximum activity obtained (2.47 U mL -1) was achieved at 31.5°C and pH 6.7, and the enzyme was stable in this condition. A novel enzyme was purified and identified for the first time by mass spectrometry. The lipase efficiently hydrolysed different natural oils and exhibited selectivity in the production of eicosapentaenoic acid from fish oil. Conclusion: The use of MC and RO as a supplement to produce the new lipase from M. spathulata R25L270 may be one alternative for reducing lipase production costs and simultaneously adding value to biodiesel industry residues. The potential application of the lipase in the oleochemical industry was demonstrated by its pH and temperature stabilities and selective hydrolysis.

Figures

  • Table 1 Central composite design matrix used to study the influence of reactional temperature (°C) and pH on lipase activity (U  mL−1) and the respective observed (y) and fitted (ŷ) values and residual errors (ε)
  • Table 2 Effect of organic nitrogen source on lipase secretion and growth of M. spathulata R25L270
  • Table 3 Simplex lattice mixture design matrix used to study the influence of macaúba cake and residual oil mixture on lipase secretion by M. sphatulata R25L270 presenting the MC:RO proportions and the respective observed (y) and fitted (ŷ) values and residual errors (ε) for supernatant lipase activity (U  mL−1) and supernatant total protein (mg  mL−1) responses
  • Table 4 Peptides sequence of protein band 1 (>120 kDa)
  • Table 5 Peptides sequence of protein 2 (>50 kDa)
  • Table 7 Hydrolysis of sardine oil catalyzed by M. spathulata R25L270 lipase and ratio between the releases of EPA versus the release of DHA during the time

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Souza, L. T. A., Oliveira, J. S., Rodrigues, M. Q. R. B., dos Santos, V. L., Pessela, B. C., & Resende, R. R. (2015). Macaúba (Acrocomia aculeata) cake from biodiesel processing: A low-cost substrate to produce lipases from Moniliella spathulata R25L270 with potential application in the oleochemical industry. Microbial Cell Factories, 14(1). https://doi.org/10.1186/s12934-015-0266-9

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