Construction of an α-Amylase/Glucoamylase Fusion Gene and Its Expression in Saccharomyces cerevisiae
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概要
- 論文の詳細を見る
A fusion gene which encoded a polypeptide comprised of 1116 amino acids was constructed using the α-amylase and glucoamylase cDNAs of Aspergillus shirousamii. When the fusion gene was expressed in Saccharomyces cerevisiae using a yeast expression plasmid under the control of the yeast ADH1 promoter, a bifunctional fusion protein (145kDa) having both α-amylase and glucoamylase activities was secreted into the culture medium. The fusion protein had higher raw-starch-digesting activity than those of the original α-amylase and glucoamylase, and adsorbed onto raw starch like the glucoamylase. It was suggested that the characteristics are a result of the raw-starch-affinity site in the glucoamylase domain of the fusion protein.
- 社団法人日本農芸化学会の論文
- 1992-06-23
著者
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Tamura G
Department Of Agricultural Chemistry The University Of Tokyo
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Tamura Gakuzo
Research Institute Of Brewing Resources Co. Ltd.
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Shibuya I
Nikka Distilling Co. Ltd. Chiba Jpn
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ISHIKAWA TAKEAKI
National Research Institute of Brewing
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HARA Shodo
National Research Institute of Brewing
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Tamura Gakuzo
Nuclear Receptor Institute Ksp
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SHIBUYA Ichiro
Research Institute of Brewing Resources Co., Ltd.
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SHIMA Harumasa
National Research Institute of Brewing
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Hara S
General Research Laboratory Of Kiku-masamune Sake Brewing Co. Ltd.
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Hara Shodo
Office Of Technical Officers Osaka Regional Taxation Bureau
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