Immobilisation of lipases by adsorption and deposition: High protein loading gives lower water activity optimum

Mattias Persson, Ernst Wehtje, Patrick Adlercreutz

Research output: Contribution to journalArticlepeer-review

38 Citations (SciVal)

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 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.

Original languageEnglish
Pages (from-to)1571-1575
Number of pages5
JournalBiotechnology Letters
Volume22
Issue number19
DOIs
Publication statusPublished - 2000 Nov 27

Subject classification (UKÄ)

  • Biocatalysis and Enzyme Technology

Keywords

  • Immobilisation
  • Lipase
  • Protein loading
  • Water activity

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