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  • Canet, Albert, et al. (author)
  • Exploring substrate specificities of a recombinant Rhizopus oryzae lipase in biodiesel synthesis
  • 2017
  • In: New Biotechnology. - : Elsevier BV. - 1871-6784. ; 39, s. 59-67
  • Journal article (peer-reviewed)abstract
    • 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.
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Type of publication
journal article (1)
Type of content
peer-reviewed (1)
Author/Editor
Adlercreutz, Patrick (1)
Canet, Albert (1)
Benaiges, M. Dolors (1)
Valero, Francisco (1)
University
Lund University (1)
Language
English (1)
Research subject (UKÄ/SCB)
Engineering and Technology (1)
Year

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