Bioscience, Biotechnology, and Biochemistry
Online ISSN : 1347-6947
Print ISSN : 0916-8451
Property of Taka-amylase A with Glu or Asp of the Catalytic Residue Replaced by the Corresponding Amine
Takuji OYAMAMiho MYOJINYasunori NITTAHiroko TODATadashi NAGASHIMAKatsuhiko KITAMOTO
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JOURNAL FREE ACCESS

1996 Volume 60 Issue 8 Pages 1351-1352

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Abstract

Compared with the enzyme activity of a recombinant Taka-amylase A (wild TAA) at 25°C and pH 5.3, those of two mutants (E230Q and D297N) were 1/10, 000 and 1/16, 000 for amylase activity, and 1/920 and less than 1/20, 000 for maltosidase activity, respectively. This indicates that all residual activities of E230Q are not due to contamination by wild-type TAA. The results from difference spectroscopy suggested that E230Q retains amylose binding ability.

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