Cyclodextrin formation by the thermostable α-amylase of Thermoanaerobacterium thermosulfurigenes EM1 and reclassification of the enzyme as a cyclodextrin glycosyltransferase

R. D. Wind, W. Liebl, R. M. Buitelaar, D. Penninga, A. Spreinat, L. Dijkhuizen, H. Bahl

Research output: Contribution to journalArticlepeer-review

97 Scopus citations

Abstract

Extensive characterization of the thermostable α-amylase of Clostridium thermosulfurogenes EM1, recently reclassified as Thermoanaerobacterium thermosulfurigenes, clearly demonstrated that the enzyme is a cyclodextrin glycosyltransferase (CGTase). Product analysis after incubation of the enzyme with starch revealed formation of α-, β-, and γ-cyclodextrins, as well as linear sugars. The specific activity for cyclization of this CGTase was similar to those of other CGTases, whereas the specific activity for hydrolysis was relatively high in comparison with other CGTases. Alignment of the amino acid sequence of the T. thermosulfurigenes enzyme with sequences from known bacterial CGTases showed high homology. The four consensus regions of carbohydrate-converting enzymes, as well as a C-terminal raw-starch binding motif, could be identified in the sequence.

Original languageEnglish
Pages (from-to)1257-1265
Number of pages9
JournalApplied and Environmental Microbiology
Volume61
Issue number4
DOIs
StatePublished - 1995
Externally publishedYes

Fingerprint

Dive into the research topics of 'Cyclodextrin formation by the thermostable α-amylase of Thermoanaerobacterium thermosulfurigenes EM1 and reclassification of the enzyme as a cyclodextrin glycosyltransferase'. Together they form a unique fingerprint.

Cite this