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

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Bibtex

@article{8ca4d61c52f144a1a11ec69ea4f91131,
title = "Immobilisation of lipases by adsorption and deposition: High protein loading gives lower water activity optimum",
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.",
keywords = "Immobilisation, Lipase, Protein loading, Water activity",
author = "Mattias Persson and Ernst Wehtje and Patrick Adlercreutz",
year = "2000",
month = "11",
day = "27",
doi = "10.1023/A:1005689002238",
language = "English",
volume = "22",
pages = "1571--1575",
journal = "Biotechnology Letters",
issn = "0141-5492",
publisher = "Springer",
number = "19",

}