H. Kitano et al., THERMOLYSIN-CATALYZED PEPTIDE-SYNTHESIS IN AQUEOUS POLYMER 2-PHASE SYSTEMS, Macromolecular chemistry and physics, 197(12), 1996, pp. 4173-4181
A proteolytic enzyme, thermolysin, was covalently immobilized to dextr
an which has a small number of carboxyl groups. Enzymatic synthesis of
aspartame derivative (Boc-Asp-Phe-OMe) using the dextran-conjugated t
hermolysin was carried out in an aqueous polymer two-phase system, whe
re poly(ethylene glycol) (PEG) and dextran dissolved in water make a p
hase separation. The yield of the peptide catalyzed by the dextran-con
jugated thermolysin was higher than that using a native enzyme in the
aqueous polymer two-phase system partly due to the effect of the micro
environment around the modified enzyme and partly due to the ''mass-la
w'' effect (the preferential dissolution of the peptide product into t
he PEG phase). The aqueous polymer two-phase system would be very usef
ul to carry out enzymatic organic syntheses in high yields.