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253 22 22 5 5 Shunjiro Sugimoto Masayuki Yabuta Tatsuji Seki Toshiomi Yoshida Hisaharu Taguchi International Center of Cooperative Research in Biotechnology Japan Faculty of Engineering Osaka University 565 Suita-shi, Osaka Japan Summary The gene pheA + coding chorismate niutase P-prephenate dehydratase, one of the regulatory enzymes of phenylalanine biosynthesis, was cloned into the down-stream of P R -P L tandem promoter. In this construction, both the native promoter-operator region and the attenuator region of pheA + operon were eliminated so as to avoid the repression and attenuation of pheA + gene expression. The expression of pheA + gene was directed by P R -P L tandem promoter of bacteriophage lambda and controlled by a temperature sensitive repressor, cI 857 . It was shown that the expression as well as phenylalanine production was regulated by temperature. Maximum production of phenylalanine, 170 mg/l, was obtained at 40°C. The host strain, MC1065, produced a trace (4 mg/l) of phenylalanine at the same temperature.
Applied Microbiology and Biotechnology – Springer Journals
Published: Sep 1, 1985
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