Summary
Lipase fromPseudomonas sp. was modified with the new amphipathic polymer poly(acryloylmorpholine)- succinimidyl ester. The lipase derivative, which carried about 4.5 polymer chains per enzyme molecule, retained 54% of the original activity and showed a single symmetrical peak in gel filtration chromatography. The derivative displayed high transesterification activity in several chlorinated solvents. Compared to methoxypoly(ethylen glycol)-modified lipase, it showed lower solubility but better catalytic properties in organic media.
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Bovara, R., Ottolina, G., Carrea, G. et al. Modification of lipase fromPseudomonas sp. with poly(acryloylmorpholine) and study of its catalytic properties in organic solvents. Biotechnol Lett 16, 1069–1074 (1994). https://doi.org/10.1007/BF01022405
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DOI: https://doi.org/10.1007/BF01022405