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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.

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organization
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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
2020-03-11 08:08:01
@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},
  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},
}