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Article

Mutations at subsite -3 in cyclodextrin glycosyltransferase from Paenibacillus macerans enhancing alpha-cyclodextrin specificity.

Applied microbiology and biotechnology - 1 Jun 2009

Li Zhaofeng, Zhang Jiayu, Wang Miao, Gu Zhengbiao, Du Guocheng, Li Jianke, Wu Jing, Chen Jian

Abstract excerpt

A major disadvantage of cyclodextrin production is the limited cyclodextrin product specificity of cyclodextrin glycosyltransferase (CGTase). Here, we described mutations of Asp372 and Tyr89 at subsite -3 in the CGTase from Paenibacillus macerans strain JFB05-01. The results showed that Asp372 and Tyr89 played important roles in cyclodextrin product specificity of CGTase. The replacement of Asp372 by lysine and...

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PMID: 19190904
DOI: 10.1007/s00253-009-1865-3

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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