Stability-increasing mutants of glucose dehydrogenase

26Citations
Citations of this article
9Readers
Mendeley users who have this article in their library.

Abstract

Four stability-increasing mutants of glucose dehydrogenase from Bacillus megateriun were purified together with the wild-type enzyme; each has a single amino acid change of Glu-96 to Gly, Glu-96 to Ala, Gln-252 to Leu, or Tyr-253 to Cys. These mutant enzymes are more heat resistant at pH 6.5 than the wild-type enzyme; the replacement of Glu-96 by Ala increases the thermostability by about 20°C. The mutant enzymes are also resistant to inactivation in alkaline solutions. The replacement of Glu-96 by Gly or Ala protects the enzyme from alkaline inactivation almost completely. The kinetic constants for the activities of these mutant enzymes do not differ significantly from those of the wild-type enzyme. © 1989.

Cite

CITATION STYLE

APA

Nagao, T., Makino, Y., Yamamoto, K., Urabe, I., & Okada, H. (1989). Stability-increasing mutants of glucose dehydrogenase. FEBS Letters, 253(1–2), 113–116. https://doi.org/10.1016/0014-5793(89)80941-X

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free