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

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Immobilisation of lipases by adsorption and deposition : High protein loading gives lower water activity optimum. / Persson, Mattias; Wehtje, Ernst; Adlercreutz, Patrick.

In: Biotechnology Letters, Vol. 22, No. 19, 27.11.2000, p. 1571-1575.

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TY - JOUR

T1 - Immobilisation of lipases by adsorption and deposition

T2 - Biotechnology Letters

AU - Persson, Mattias

AU - Wehtje, Ernst

AU - Adlercreutz, Patrick

PY - 2000/11/27

Y1 - 2000/11/27

N2 - 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.

AB - 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.

KW - Immobilisation

KW - Lipase

KW - Protein loading

KW - Water activity

UR - http://www.scopus.com/inward/record.url?scp=0033742181&partnerID=8YFLogxK

U2 - 10.1023/A:1005689002238

DO - 10.1023/A:1005689002238

M3 - Article

VL - 22

SP - 1571

EP - 1575

JO - Biotechnology Letters

JF - Biotechnology Letters

SN - 0141-5492

IS - 19

ER -