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

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논문

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

학술지

New biotechnology

저자명

Canet, A.; Benaiges, M.D.; Valero, F.; Adlercreutz, P.

초록

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.

발행연도

2017

발행기관

Elsevier

ISSN

1871-6784

권

호

페이지

pp.59-67

DOI

10.1016/j.nbt.2017.07.003