Mutations enhance β-cyclodextrin specificity of cyclodextrin glycosyltransferase from Bacillus circulans.

doi:10.1016/j.carbpol.2014.03.015

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Article

Mutations enhance β-cyclodextrin specificity of cyclodextrin glycosyltransferase from Bacillus circulans.

Carbohydrate polymers - 8 Aug 2014

Li Zhaofeng, Ban Xiaofeng, Gu Zhengbiao, Li Caiming, Huang Min, Hong Yan, Cheng Li

Abstract excerpt

The effects of amino acid residue at position 31 in the neighborhood of calcium binding site I (CaI) on product specificity of cyclodextrin glycosyltransferase (EC 2.4.1.19, CGTase) were investigated by replacing Ala31 in the CGTase from Bacillus circulans STB01 with arginine, proline, threonine, serine and glycine. The results showed that the mutations A31R, A31P, and A31T resulted in the increases in...

Topics

Bacillus
Glucosyltransferases
Mutation
beta-Cyclodextrins

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PMID: 24751254
DOI: 10.1016/j.carbpol.2014.03.015

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