Two-polymer aqueous phase systems are described in which ribosomes selectively partition into one of the phases. One of the phase systems is used to determine rapidly and conveniently binding of thiostrepton and erythromycin to Escherichia co/i ribosomes under equilibrium conditions.
Thermolysin-catalyzed peptide synthesis in aqueous polymer two-phase systems
โ 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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โฆ Synopsis
Abstract
A proteolytic enzyme, thermolysin, was covalently immobilized to dextran which has a small number of carboxyl groups. Enzymatic synthesis of aspartame derivative (BocโAspโPheโOMe) using the dextranโconjugated thermolysin was carried out in an aqueous polymer twoโphase system, where poly(ethylene glycol) (PEG) and dextran dissolved in water make a phase separation. The yield of the peptide catalyzed by the dextranโconjugated thermolysin was higher than that using a native enzyme in the aqueous polymer twoโphase system partly due to the effect of the microenvironment around the modified enzyme and partly due to the โmassโlawโ effect (the preferential dissolution of the peptide product into the PEG phase). The aqueous polymer twoโphase system would be very useful to carry out enzymatic organic syntheses in high yields.
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