AGGREGATE OF A PEPTIDE-CONTAINING BLOCK-COPOLYMER WITH A LIPASE

The peptide-containing block copolymer N-acetyliminoethylene)-block-po ly(L-phenylalanine) (1) formed large water-soluble aggregates in water due to the hydrophobic and hydrogen-bonding character of the poly(L-p henylalanine) block-The solution proper ties of 1 were compared with t hose of the block copolymer liminoethylene)-block-poly(N-benzoyliminoe thylene) (2) with an analogous structure. 1 formed aggregates even tho ugh the poly(phenylalanine) segment was short as compared with 2 in wh ich hydrophobic interaction may be the only driving force to form aggr egates. The aggregates have strong capability of incorporating Lipase P and largely increase the hydrolysis activity against p-nitrophenyl p ropionate as compared with that of free Lipase P.