Extracellular Production of Yeast Protease |
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Authors: | Koji Mitsugi Toru Takami Sadanobu Tobe Michiko Kimura Takashi Nakase Kazuo Komagata |
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Affiliation: | Central Research Laboratories of Ajinomoto Co, Inc., Kawasaki |
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Abstract: | The groEL gene of the alkaliphilic Bacillus sp. strain C-125 was cloned in Escherichia coli and sequenced. The groEL gene encoded a polypeptide of 544 amino acids and was preceded by the incomplete groES gene, lacking its 5′-end. The sequence of the derived amino acids was 87.5% identical to that of B. subtilis, 85.4% identical to that of B. stearothemophilus, and 60.9% identical to that of E. coli. The GroEL protein was expressed in E. coli. Purified GroEL protected yeast a-glucosidase from irreversible aggregation at a high temperature and the addition of Mg-ATP was essential for reactivation of the a-glucosidase. The addition of E. coli GroES increased recovery of the enzyme activity, indicating that C-125 GroEL could function in coordination with E. coli GroES. |
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Keywords: | alkaliphilic Bacillus GroES GroEL |
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