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• W2734697441 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." @default.
• W2734697441 created "2017-07-21" @default.
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• W2734697441 date "2017-10-01" @default.
• W2734697441 modified "2023-10-18" @default.
• W2734697441 title "Exploring substrate specificities of a recombinant Rhizopus oryzae lipase in biodiesel synthesis" @default.
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• W2734697441 doi "https://doi.org/10.1016/j.nbt.2017.07.003" @default.
• W2734697441 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/28711520" @default.
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