Release of Thermophilic α-Amylase from Transformed Escherichia coli by Addition of Glycine

概要

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For the purpose of the efficient extraction of thermophilic α-amylase, we investigated the effect of glycine on the extracellular release of a foreign gene product from a recombinant Escherichia coli. Regardless of the medium, carbon source, growth phase and host tested, about 70-80% of α-amylase was released from E. coli HB101/pHI301 by the addition of glycine. Distribution of α-amylase activity in E. coli HB101/pHI301 revealed that the extracellular release of the enzyme significantly depended on a decrease of the activity in the periplasm. Based on the effect of the glycine concentration and the time-course of the release, the optimal condition of glycine treatment may be 3 h-incubation in 1% glycine. For simplification of the purification process, we tested the release of α-amylase from E. coli HB101/pHI301 in a solution containing only glycine instead of growth media containing glycine. The former was sufficiently effective for the release of the enzyme. This result suggests a simple and easy method for the purification of the enzyme.
社団法人日本生物工学会の論文
1989-10-25