枯草菌Marburg株の生産するα-アミラーゼの性質(ノート)〔英文〕

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α-Amylase produced by Bacillus subtilis 168,a typical Marburg strain, was purified to an electrophoretically homogeneous state with acrylamide gel, and its characteristics were compared with saccharifying and liquefying types of α-amylase. The following results were obtained. Its molecular weight was estimated to be 53,000,larger than the 47,500^<1)> and 42,000^<2)> which had been reported as the molecular weights of saccharifying α-amylase and the 48,700 reported for liquefying α-amylase.^<3)> During agar gel electrophoresis at pH 6.3 the enzyme travelled toward the cathode faster than the liquefying type α-amylase. At the same pH, saccharifying α-amylase travelled in another direction. The Marburg strain α-amylase had a heat stability similar to that of the saccharifying type enzyme and was much less stable than the liquefying α-amylase. There is no reaction between liquefying α-amylase and antiserum for Marburg α-amylase but a spur reaction was observed among saccharifying α-amylase, Marburg α-amylase and the antiserum. From these results it was concluded that the Marburg α-amylase is quite different from the liquefying type α-amylase, but closely resembles the saccharifying type, although the two are not identical.
社団法人日本生物工学会の論文
1972-12-25