Mutants of D-Aminopeptidase with Increased Thermal Stability
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概要
- 論文の詳細を見る
Mutant D-aminopeptidases from Ochrobactrum anthropi with increased thermal stability were obtained by random mutagenesis. One of the mutants, no. 65,was derived from E. coli cells transformed with DNA treated with sodium nitrite. The remaining activity of the purified mutant enzyme no. 65 after heat treatment at 52℃ for 10 min was 20% that of the untreated mutant enzyme no. 65,whereas the native enzyme showed 5% of the untreated native enzyme activity after the same treatment. The gene for the mutant enzyme no. 65 was sequenced and it was found that Gly155 and Gly279 in the native enzyme were replaced by Ser and Asp, respectively. Five mutants carrying one or two mutations were generated from the native gene by site-specific mutagenesis. The enhancement of the thermal stability of mutant enzyme no. 65 was attributed to the substitution of Gly155 to Ser.
- 公益社団法人日本生物工学会の論文
- 1995-06-25
著者
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YAMAGUCHI Kaori
Sagami Chemical Research Center
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Asano Yasuhisa
Biotechnology Res. Center And Dep. Of Biotechnology Toyama Prefectural Univ.
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