Exploring substrate specificities of a recombinant Rhizopus oryzae lipase in biodiesel synthesis
Research output: Contribution to journal › Article
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.
|Research areas and keywords||
Subject classification (UKÄ) – MANDATORY
|Early online date||2017 Jul 12|
|Publication status||Published - 2017 Oct|