Immobilisation of lipases by adsorption and deposition : High protein loading gives lower water activity optimum
Persson, Mattias ; Wehtje, Ernst LU and Adlercreutz, Patrick LU
(2000)
In Biotechnology Letters
22(19).
p.1571-1575
- Abstract
Two different immobilisation techniques for lipases were investigated: adsorption on to Accurel EP-100 and deposition on to Celite. The specific activities were in the same order of magnitude, 2.9 (μmol min -1 mg protein) when Celite was used as support and 2.3 (μmol min -1 mg -1 protein) when Accurel EP-100 was used as support, even if the amount of lipase loaded differed by 2 orders of magnitude. Immobilisation on Accurel EP-100 was the preferred technique since 40-100 times more protein can be loaded/per g carrier, thus yielding a more active catalyst. The water activity profiles in lipase catalysed esterification were influenced by... (More)
Two different immobilisation techniques for lipases were investigated: adsorption on to Accurel EP-100 and deposition on to Celite. The specific activities were in the same order of magnitude, 2.9 (μmol min -1 mg protein) when Celite was used as support and 2.3 (μmol min -1 mg -1 protein) when Accurel EP-100 was used as support, even if the amount of lipase loaded differed by 2 orders of magnitude. Immobilisation on Accurel EP-100 was the preferred technique since 40-100 times more protein can be loaded/per g carrier, thus yielding a more active catalyst. The water activity profiles in lipase catalysed esterification were influenced by the amount of protein adsorbed to Accurel EP-100. Higher protein loading (40 mg g -1) resulted in a bell-shaped water activity profile with highest specific activity (6.1 μmol min -1 mg -1 protein) at a(w) = 0.11, while an enzyme preparation with low protein loading (4 mg g -1) showed highest specific activity at a(w) = 0.75.
(Less)
- author
- Persson, Mattias
; Wehtje, Ernst
LU
and Adlercreutz, Patrick
LU
- organization
- publishing date
- 2000-11-27
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- Immobilisation, Lipase, Protein loading, Water activity
- in
- Biotechnology Letters
- volume
- 22
- issue
- 19
- pages
- 5 pages
- publisher
- Springer
- external identifiers
-
- scopus:0033742181
- ISSN
- 0141-5492
- DOI
- 10.1023/A:1005689002238
- language
- English
- LU publication?
- yes
- id
- 8ca4d61c-52f1-44a1-a11e-c69ea4f91131
- date added to LUP
- 2019-06-20 15:58:41
- date last changed
- 2022-02-15 21:25:56
@article{8ca4d61c-52f1-44a1-a11e-c69ea4f91131,
abstract = {{<p>Two different immobilisation techniques for lipases were investigated: adsorption on to Accurel EP-100 and deposition on to Celite. The specific activities were in the same order of magnitude, 2.9 (μmol min <sup>-1</sup> mg protein) when Celite was used as support and 2.3 (μmol min <sup>-1</sup> mg <sup>-1</sup> protein) when Accurel EP-100 was used as support, even if the amount of lipase loaded differed by 2 orders of magnitude. Immobilisation on Accurel EP-100 was the preferred technique since 40-100 times more protein can be loaded/per g carrier, thus yielding a more active catalyst. The water activity profiles in lipase catalysed esterification were influenced by the amount of protein adsorbed to Accurel EP-100. Higher protein loading (40 mg g <sup>-1</sup>) resulted in a bell-shaped water activity profile with highest specific activity (6.1 μmol min <sup>-1</sup> mg <sup>-1</sup> protein) at a(w) = 0.11, while an enzyme preparation with low protein loading (4 mg g <sup>-1</sup>) showed highest specific activity at a(w) = 0.75.</p>}},
author = {{Persson, Mattias and Wehtje, Ernst and Adlercreutz, Patrick}},
issn = {{0141-5492}},
keywords = {{Immobilisation; Lipase; Protein loading; Water activity}},
language = {{eng}},
month = {{11}},
number = {{19}},
pages = {{1571--1575}},
publisher = {{Springer}},
series = {{Biotechnology Letters}},
title = {{Immobilisation of lipases by adsorption and deposition : High protein loading gives lower water activity optimum}},
url = {{http://dx.doi.org/10.1023/A:1005689002238}},
doi = {{10.1023/A:1005689002238}},
volume = {{22}},
year = {{2000}},
}