Mass transfer studies on immobilized α-chymotrypsin biocatalysts prepared by deposition for use in organic medium
Barros, Raúl J. LU ; Wehtje, Ernst LU and Adlercreutz, Patrick LU
(1998)
In Biotechnology and Bioengineering
59(3).
p.364-373
- Abstract
Mass transfer limitations were studied in enzyme preparations of α- chymotrypsin made by deposition on different porous support materials such as controlled pore glasses, Celite, and polyamides of different particle sizes. It is the onset of mass transfer limitations that determines the position of the activity optimum with respect to enzyme loading on each support. The evidence of various experiments indicates that internal diffusional limitations are the important mechanism for the observed mass transfer limitations. External diffusion was not found to play an important role under the conditions used, and it was also found that when immobilizing multilayers of enzyme the buried enzyme molecules are active to a large extent. An extreme... (More)
Mass transfer limitations were studied in enzyme preparations of α- chymotrypsin made by deposition on different porous support materials such as controlled pore glasses, Celite, and polyamides of different particle sizes. It is the onset of mass transfer limitations that determines the position of the activity optimum with respect to enzyme loading on each support. The evidence of various experiments indicates that internal diffusional limitations are the important mechanism for the observed mass transfer limitations. External diffusion was not found to play an important role under the conditions used, and it was also found that when immobilizing multilayers of enzyme the buried enzyme molecules are active to a large extent. An extreme situation is observed on Celite at very high loadings. Under these conditions, this support is expected to have its pores completely filled with packed enzyme molecules, and then it is the diffusion within the enzyme layer that determines the observed rate. As the enzyme loading increases, the area of contact between the deposited enzyme layers and the liquid solution inside the pores diminishes, causing a decrease on the observed rate of an intrinsically fast reaction which apparently is incongruous with the presence of more enzyme in the system. This work shows that mass transfer limitations can be an important factor when working with immobilized enzymes in organic media, and its study should be carried out in order to avoid undesired reduced enzyme activities and specificities.
(Less)
- author
- Barros, Raúl J.
LU
; Wehtje, Ernst
LU
and Adlercreutz, Patrick
LU
- organization
- publishing date
- 1998-08-05
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- Active site accessibility, Enzyme loading, Internal and external diffusion, Kinetically controlled dipeptide synthesis, Porous supports
- in
- Biotechnology and Bioengineering
- volume
- 59
- issue
- 3
- pages
- 10 pages
- publisher
- John Wiley & Sons Inc.
- external identifiers
-
- scopus:0032486748
- pmid:10099348
- ISSN
- 0006-3592
- DOI
- 10.1002/(SICI)1097-0290(19980805)59:3<364::AID-BIT13>3.0.CO;2-E
- language
- English
- LU publication?
- yes
- id
- cf026fe5-5c33-43c3-b0cb-d532c9a7cfa1
- date added to LUP
- 2019-06-20 16:06:34
- date last changed
- 2024-01-01 12:04:05
@article{cf026fe5-5c33-43c3-b0cb-d532c9a7cfa1,
abstract = {{<p>Mass transfer limitations were studied in enzyme preparations of α- chymotrypsin made by deposition on different porous support materials such as controlled pore glasses, Celite, and polyamides of different particle sizes. It is the onset of mass transfer limitations that determines the position of the activity optimum with respect to enzyme loading on each support. The evidence of various experiments indicates that internal diffusional limitations are the important mechanism for the observed mass transfer limitations. External diffusion was not found to play an important role under the conditions used, and it was also found that when immobilizing multilayers of enzyme the buried enzyme molecules are active to a large extent. An extreme situation is observed on Celite at very high loadings. Under these conditions, this support is expected to have its pores completely filled with packed enzyme molecules, and then it is the diffusion within the enzyme layer that determines the observed rate. As the enzyme loading increases, the area of contact between the deposited enzyme layers and the liquid solution inside the pores diminishes, causing a decrease on the observed rate of an intrinsically fast reaction which apparently is incongruous with the presence of more enzyme in the system. This work shows that mass transfer limitations can be an important factor when working with immobilized enzymes in organic media, and its study should be carried out in order to avoid undesired reduced enzyme activities and specificities.</p>}},
author = {{Barros, Raúl J. and Wehtje, Ernst and Adlercreutz, Patrick}},
issn = {{0006-3592}},
keywords = {{Active site accessibility; Enzyme loading; Internal and external diffusion; Kinetically controlled dipeptide synthesis; Porous supports}},
language = {{eng}},
month = {{08}},
number = {{3}},
pages = {{364--373}},
publisher = {{John Wiley & Sons Inc.}},
series = {{Biotechnology and Bioengineering}},
title = {{Mass transfer studies on immobilized α-chymotrypsin biocatalysts prepared by deposition for use in organic medium}},
url = {{http://dx.doi.org/10.1002/(SICI)1097-0290(19980805)59:3<364::AID-BIT13>3.0.CO;2-E}},
doi = {{10.1002/(SICI)1097-0290(19980805)59:3<364::AID-BIT13>3.0.CO;2-E}},
volume = {{59}},
year = {{1998}},
}