Effect of different parameters on the hydrolytic activity of cross-linked enzyme aggregates (CLEAs) of lipase from Thermomyces lanuginosa

M.P. GUAUQUE TORRES; M.L. FORESTI; M.L. FERREIRA

BIOCHEMICAL ENGINEERING JOURNAL

ELSEVIER SCIENCE SA

Lugar: Amsterdam; Año: 2013 vol. 72 p. 18 - 23

1369-703X

Cross-linked enzyme aggregates (CLEAs) of lipase from Thermomyces lanuginosa (TLL) were synthesizedusing (NH4)2SO4 as precipitant and glutaraldehyde as cross-linking agent. CLEAs were assayed for theirhydrolytic activity in a reaction performed in an emulsioned medium. The effects of the amount of precipitant,cross-linker, and different additives such as protein cofeeder, oleic acid, n-heptane, sodium dodecylsulfate (SDS), polyethylenglicol (PEG) and ethylendiamine were studied at selected ratios with respectto TLL mass. Traditional non-layered CLEAs of TLL showed recovered activities between 3 and 31% whencompared with native lipase. Novel TLL layered CLEAs consisting of a protein cofeeder core and successivelayers of target lipase showed an important increase in their retained activity. The highest recoveredactivity was found for the one-layered non-additivated CLEAs of TLL which showed a recovered activityof 75%.