Amylase Action in Maltodextrin-Sodium Dodecylsulfate Solution

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概要

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• Enzyme catalyzed hydrolysis of maltodextrin was studied with enzyme-maltodextrin and enzyme-maltodextrin-sodium dodecylsulfate systems. Sodium dodecylsulfate (SDS) is a complex forming agent for maltodextrin. When endo-enzyme such as Taka-amylase A was used as the enzyme, ratio of the initial velocity of the hydrolysis of the system containing SDS to that without SDS decreases with the increase of degree of polymerization (D.P.) of the maltodextrin and becomes zero with the maltodextrin of D.P. above about 60. When the liquefying α-amylase of Bacillus subtilis was used as an endo-enzyme, a similar result was also obtained. When exo-enzyme such as Glucoamylase of Rh. Delemar was used, the ratio decreases gradually with the increase of D.P. of maltodextrin, and remains in a relatively high level even in the case of maltodextrin of D.P. above 60. In the case of Taka-amylase A, the enzyme action is suppressed by the presence of the stiff helical segments of SDS complex and the initial velocity of the system with SDS decreases compared with the one without SDS. In the case of Glucoamylase, the presence of the stiff helical segment does not distinctively induce such a depression of the enzyme action as that in the case of Taka-amylase A. The depression is partly dependent on the inhibitory interaction of SDS with the enzyme.

• 公益社団法人 日本化学会の論文

著者

• Ono Sozaburo

  Laboratory Of Bio-physical Chemistry Department Of Agvicultural Chemistry

• Watanabe Takehiko

  Laboratory Of Bio-physical Chemistry Department Of Agvicultural Chemistry

• Sakon Ken-ichi

  Laboratory of Biophysical Chemistry, College of Agriculture, University of Osaka Prefecture

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