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Thermolysin-catalyzed peptide synthesis in aqueous polymer two-phase systems

โœ Scribed by Hiromi Kitano; Yasushi Maeda; Masayo Yamamoto; Rie Izumida


Publisher
John Wiley and Sons
Year
1996
Tongue
English
Weight
458 KB
Volume
197
Category
Article
ISSN
1022-1352

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โœฆ Synopsis


Abstract

A proteolytic enzyme, thermolysin, was covalently immobilized to dextran which has a small number of carboxyl groups. Enzymatic synthesis of aspartame derivative (Bocโ€Aspโ€Pheโ€OMe) using the dextranโ€conjugated thermolysin was carried out in an aqueous polymer twoโ€phase system, where poly(ethylene glycol) (PEG) and dextran dissolved in water make a phase separation. The yield of the peptide catalyzed by the dextranโ€conjugated thermolysin was higher than that using a native enzyme in the aqueous polymer twoโ€phase system partly due to the effect of the microenvironment around the modified enzyme and partly due to the โ€œmassโ€lawโ€ effect (the preferential dissolution of the peptide product into the PEG phase). The aqueous polymer twoโ€phase system would be very useful to carry out enzymatic organic syntheses in high yields.


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