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

Canet, Albert LU ; Benaiges, M. Dolors; Valero, Francisco and Adlercreutz, Patrick LU (2017) In New Biotechnology 39. p.59-67
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... (More)

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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organization
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type
Contribution to journal
publication status
published
subject
keywords
Acylglycerols, Biodiesel, Lipase, Rhizopus oryzae, Transesterification
in
New Biotechnology
volume
39
pages
59 - 67
publisher
Elsevier
external identifiers
  • scopus:85024472783
  • wos:000410912900009
ISSN
1871-6784
DOI
10.1016/j.nbt.2017.07.003
language
English
LU publication?
yes
id
f9b1a7a3-cab3-4f6b-b0f0-f0b8114fb087
date added to LUP
2017-07-31 13:30:11
date last changed
2018-02-20 11:11:27
@article{f9b1a7a3-cab3-4f6b-b0f0-f0b8114fb087,
  abstract     = {<p>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.</p>},
  author       = {Canet, Albert and Benaiges, M. Dolors and Valero, Francisco and Adlercreutz, Patrick},
  issn         = {1871-6784},
  keyword      = {Acylglycerols,Biodiesel,Lipase,Rhizopus oryzae,Transesterification},
  language     = {eng},
  pages        = {59--67},
  publisher    = {Elsevier},
  series       = {New Biotechnology},
  title        = {Exploring substrate specificities of a recombinant Rhizopus oryzae lipase in biodiesel synthesis},
  url          = {http://dx.doi.org/10.1016/j.nbt.2017.07.003},
  volume       = {39},
  year         = {2017},
}