Water activity and substrate concentration effects on lipase activity.
Wehtje, Ernst LU and Adlercreutz, Patrick LU
(1997)
In Biotechnology and Bioengineering
55(5).
p.798-806
- Abstract
- Catalytic activity of lipases (from Rhizopus arrhizus, Canadida rugosa, and Pseudomonas sp. was studied in organic media, mainly diisopropyl ether. The effect of water activity (a(w)) on V(max) showed that the enzyme activity in general increased with increasing amounts of water for the three enzymes. This was shown both for esterification and hydrolysis reactions catalyzed by R. arrhizus lipase. In the esterification reaction the K(m) for the acid substrate showed a slight increase with increasing water activities. On the other hand, the K(m) for the alcohol substrate increased 10-20-fold with increasing water activity. The relative changes in K(m) were shown to be independent of the enzyme studied and solvent used. The effect was... (More)
- Catalytic activity of lipases (from Rhizopus arrhizus, Canadida rugosa, and Pseudomonas sp. was studied in organic media, mainly diisopropyl ether. The effect of water activity (a(w)) on V(max) showed that the enzyme activity in general increased with increasing amounts of water for the three enzymes. This was shown both for esterification and hydrolysis reactions catalyzed by R. arrhizus lipase. In the esterification reaction the K(m) for the acid substrate showed a slight increase with increasing water activities. On the other hand, the K(m) for the alcohol substrate increased 10-20-fold with increasing water activity. The relative changes in K(m) were shown to be independent of the enzyme studied and solvent used. The effect was attributed to the increasing competition of water as a nucleophile for the acyl-enzyme at higher water activities. In a hydrolysis reaction the K(m) for the ester was also shown to increase as the water activity increased. The effect of water in this case was due to the fact that increased concentration of one substrate (water), and thereby increased saturation of the enzyme, will increase the apparent K(m) of the substrate (ester) to be determined. This explained why the hydrolysis rate decreased with increasing water activity at a fixed, low ester concentration. The apparent V(max) for R. arrhizus lipase was similar in four of six different solvents that were tested; exceptions were toulene and trichloroethylene, which showed lower values. The apparent K(m) for the alcohol in the solvents correlated with the hydrophobicity of the solvent, hydrophobic solvents giving lower apparent K(m). (c) 1997 John Wiley & Sons, Inc. Biotechnol Bioeng 55: 798-806, 1997. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1181046
- author
- Wehtje, Ernst
LU
and Adlercreutz, Patrick
LU
- organization
- publishing date
- 1997
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Biotechnology and Bioengineering
- volume
- 55
- issue
- 5
- pages
- 798 - 806
- publisher
- John Wiley & Sons Inc.
- external identifiers
-
- pmid:18636590
- scopus:0031554889
- ISSN
- 1097-0290
- DOI
- 10.1002/(SICI)1097-0290(19970905)55:5<798::AID-BIT10>3.0.CO;2-8
- language
- English
- LU publication?
- yes
- id
- 832e8040-579e-40f6-ac86-b7c383749b4c (old id 1181046)
- date added to LUP
- 2016-04-01 12:14:56
- date last changed
- 2022-03-28 22:18:44
@article{832e8040-579e-40f6-ac86-b7c383749b4c,
abstract = {{Catalytic activity of lipases (from Rhizopus arrhizus, Canadida rugosa, and Pseudomonas sp. was studied in organic media, mainly diisopropyl ether. The effect of water activity (a(w)) on V(max) showed that the enzyme activity in general increased with increasing amounts of water for the three enzymes. This was shown both for esterification and hydrolysis reactions catalyzed by R. arrhizus lipase. In the esterification reaction the K(m) for the acid substrate showed a slight increase with increasing water activities. On the other hand, the K(m) for the alcohol substrate increased 10-20-fold with increasing water activity. The relative changes in K(m) were shown to be independent of the enzyme studied and solvent used. The effect was attributed to the increasing competition of water as a nucleophile for the acyl-enzyme at higher water activities. In a hydrolysis reaction the K(m) for the ester was also shown to increase as the water activity increased. The effect of water in this case was due to the fact that increased concentration of one substrate (water), and thereby increased saturation of the enzyme, will increase the apparent K(m) of the substrate (ester) to be determined. This explained why the hydrolysis rate decreased with increasing water activity at a fixed, low ester concentration. The apparent V(max) for R. arrhizus lipase was similar in four of six different solvents that were tested; exceptions were toulene and trichloroethylene, which showed lower values. The apparent K(m) for the alcohol in the solvents correlated with the hydrophobicity of the solvent, hydrophobic solvents giving lower apparent K(m). (c) 1997 John Wiley & Sons, Inc. Biotechnol Bioeng 55: 798-806, 1997.}},
author = {{Wehtje, Ernst and Adlercreutz, Patrick}},
issn = {{1097-0290}},
language = {{eng}},
number = {{5}},
pages = {{798--806}},
publisher = {{John Wiley & Sons Inc.}},
series = {{Biotechnology and Bioengineering}},
title = {{Water activity and substrate concentration effects on lipase activity.}},
url = {{http://dx.doi.org/10.1002/(SICI)1097-0290(19970905)55:5<798::AID-BIT10>3.0.CO;2-8}},
doi = {{10.1002/(SICI)1097-0290(19970905)55:5<798::AID-BIT10>3.0.CO;2-8}},
volume = {{55}},
year = {{1997}},
}