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Exploring Substrate Specificities of a Recombinant Rhizopus Oryzae Lipase in Biodiesel Synthesis

Exploring Substrate Specificities of a Recombinant Rhizopus Oryzae Lipase in Biodiesel Synthesis

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

N Biotechnol. 2017 Oct 25;39(Pt A):59-67.

PMID: 28711520

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.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP9001621-H	Lipase from Rhizopus oryzae		9001-62-1	Price
AP9016186-F	Esterase from Rhizopus oryzae		9016-18-6	Price

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