Exploring substrate specificities of a recombinant Rhizopus oryzae lipase in biodiesel synthesis

Albert Canet, M. Dolors Benaiges, Francisco Valero, Patrick Adlercreutz

Research output: Contribution to journalArticleResearchpeer-review

5 Citations (Scopus)

Abstract

© 2017 Elsevier B.V. The alcoholysis of triolein was used to explore the specific features of a recombinant Rhizopus oryzae lipase (rROL) for biodiesel synthesis. For this purpose, different acylglycerols were compared as substrates in lipase-catalysed transesterification. rROL was shown to exhibit a higher specificity towards 1-monoolein than triolein compared to other R. oryzae lipases, being more than 4-fold more specific; in contrast, rROL did not accept 2-monoolein as substrate, concluding that it is highly 1,3-positional specific. Comparing ethanol and methanol as acyl-acceptors, it was observed that the latter caused more lipase inactivation. Regarding alcohols, it was also demonstrated that acyl migration occurred in moderate alcohol concentrations.
Original languageEnglish
Pages (from-to)59-67
JournalNew Biotechnology
Volume39
DOIs
Publication statusPublished - 25 Oct 2017

Keywords

  • Acylglycerols
  • Biodiesel
  • Lipase
  • Rhizopus oryzae
  • Transesterification

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