Summary
The properties of various forms of lipoprotein lipase (powder, adsorbed onto Celite, covalently linked to PEG, with additives) in toluene were investigated. The form of the enzyme dramatically influenced the activity and stability of the enzyme with the highest activity obtained with PEG-lipase and the highest stability with Celite-immobilized lipase. By contrast, the enantioselectivity was only marginally affected.
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Ottolina, G., Carrea, G., Riva, S. et al. Effect of the enzyme form on the activity, stability and enantioselectivity of lipoprotein lipase in toluene. Biotechnol Lett 14, 947–952 (1992). https://doi.org/10.1007/BF01020635
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DOI: https://doi.org/10.1007/BF01020635