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.
(Less)
- author
- Canet, Albert
LU
; Benaiges, M. Dolors
; Valero, Francisco
and Adlercreutz, Patrick
LU
- organization
- publishing date
- 2017-10
- 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
- pmid:28711520
- 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
- 2025-01-07 18:05:17
@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}},
keywords = {{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}},
doi = {{10.1016/j.nbt.2017.07.003}},
volume = {{39}},
year = {{2017}},
}