Abstract:
:A cyclodextrin glycosyltransferase (CGTase) gene of Brevibacillus brevis CD162 was cloned into Escherichia coli using pUC19 as a vector. Determination of the nucleotide sequence showed the presence of an open reading frame of 2079 bp encoding a polypeptide of 693 amino acid residues, composed of a 20-amino acid signal sequence and a 673-amino acid mature enzyme. Neither a TATA- nor a TTGA-like sequence was observed within the cloned DNA fragment. However, the fragment was expressed in Escherichia coli by the lac promoter of pUC19 and 74% of the total activity was secreted into the fermentation medium. The amino acid sequence of the mature CGTase showed the highest homology of 86% to that of Bacillus sp. KC201. The CGTase purified to homogeneity from the recombinant E. coli exhibited the same properties as those of native CGTase from Brevibacillus brevis CD162 in terms of molecular mass, reaction conditions, stability and the production of cyclodextrins.
journal_name
FEMS Microbiol Lettjournal_title
FEMS microbiology lettersauthors
Kim MH,Sohn CB,Oh TKdoi
10.1111/j.1574-6968.1998.tb13117.xsubject
Has Abstractpub_date
1998-07-15 00:00:00pages
411-8issue
2eissn
0378-1097issn
1574-6968pii
S0378-1097(98)00247-Xjournal_volume
164pub_type
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