Effects of acid concentration and solvent choice on enzymatic acrylation by Candida antarctica lipase B
Nordblad, Mathias LU and Adlercreutz, Patrick LU
(2008)
In Journal of Biotechnology
133(1).
p.127-133
- Abstract
- Lipase-mediated acrylation is an attractive alternative to more traditional chemical processes, since it provides specific catalysis under mild conditions. A detailed study of the effects of solvent choice and substrate concentrations on the acrylation of octanol by Candida antarctica lipase B (Novozyme(R) 435) is presented. Acrylic acid was found to have a pronounced inhibitory effect. Partial neutralisation of the acid substrate by addition of an organo-soluble base markedly altered the activity profile, indicating the inhibitory mechanism to be related to acid-base interactions. The concentration of acrylic acid to be employed was found to be important in the choice of an appropriate solvent. At low acrylic acid concentrations, the... (More)
- Lipase-mediated acrylation is an attractive alternative to more traditional chemical processes, since it provides specific catalysis under mild conditions. A detailed study of the effects of solvent choice and substrate concentrations on the acrylation of octanol by Candida antarctica lipase B (Novozyme(R) 435) is presented. Acrylic acid was found to have a pronounced inhibitory effect. Partial neutralisation of the acid substrate by addition of an organo-soluble base markedly altered the activity profile, indicating the inhibitory mechanism to be related to acid-base interactions. The concentration of acrylic acid to be employed was found to be important in the choice of an appropriate solvent. At low acrylic acid concentrations, the highest rates and conversions were obtained using hydrophobic solvents, whereas at higher acrylic acid concentrations more polar solvents were advantageous. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1200273
- author
- Nordblad, Mathias
LU
and Adlercreutz, Patrick
LU
- organization
- publishing date
- 2008
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- protonation effects, acrylate synthesis, lipase, acrylic acid
- in
- Journal of Biotechnology
- volume
- 133
- issue
- 1
- pages
- 127 - 133
- publisher
- Elsevier
- external identifiers
-
- wos:000251853100018
- scopus:36048967970
- pmid:17945372
- ISSN
- 1873-4863
- DOI
- 10.1016/j.jbiotec.2007.09.002
- language
- English
- LU publication?
- yes
- id
- 268fbcda-4b48-4455-a9e7-d8caf9f75390 (old id 1200273)
- date added to LUP
- 2016-04-01 12:02:39
- date last changed
- 2022-01-26 22:01:45
@article{268fbcda-4b48-4455-a9e7-d8caf9f75390,
abstract = {{Lipase-mediated acrylation is an attractive alternative to more traditional chemical processes, since it provides specific catalysis under mild conditions. A detailed study of the effects of solvent choice and substrate concentrations on the acrylation of octanol by Candida antarctica lipase B (Novozyme(R) 435) is presented. Acrylic acid was found to have a pronounced inhibitory effect. Partial neutralisation of the acid substrate by addition of an organo-soluble base markedly altered the activity profile, indicating the inhibitory mechanism to be related to acid-base interactions. The concentration of acrylic acid to be employed was found to be important in the choice of an appropriate solvent. At low acrylic acid concentrations, the highest rates and conversions were obtained using hydrophobic solvents, whereas at higher acrylic acid concentrations more polar solvents were advantageous.}},
author = {{Nordblad, Mathias and Adlercreutz, Patrick}},
issn = {{1873-4863}},
keywords = {{protonation effects; acrylate synthesis; lipase; acrylic acid}},
language = {{eng}},
number = {{1}},
pages = {{127--133}},
publisher = {{Elsevier}},
series = {{Journal of Biotechnology}},
title = {{Effects of acid concentration and solvent choice on enzymatic acrylation by Candida antarctica lipase B}},
url = {{http://dx.doi.org/10.1016/j.jbiotec.2007.09.002}},
doi = {{10.1016/j.jbiotec.2007.09.002}},
volume = {{133}},
year = {{2008}},
}