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Title 

Construction of a chimeric series of Bacillus cyclomaltodextrin glucanotransferases and analysis of the thermal stabilities and pH optima of the enzymes

Authors 

Takahiro KanekoKi Bang SongTetsuo HamamotoToshiaki KudoKoki Horikoshi

Issue Date 

1989

Citation 

Journal of General Microbiology, vol. 135, no. 0, pp. 3447-3457

Keywords 

radioisotopebacillusescherichia colimolecular cloningnonhumanpriority journalsugar transportamino acid sequenceamino acidsbase sequence

Abstract 

The cyclomaltodextrin glucanotransferase (CGTase, EC 2.4.1.19) gene from the alkalophilic Bacillus sp. strain no. 17-1 was cloned in Escherichia coli. The cloned CGTase gene consisted of single open reading frame which would encode a polypeptide of 713 amino acids, and the first 27 amino acid residues comprised a signal peptide. The nucleotide sequence and the amino acid sequence of this CGTase (CGTase) 17-1) gene had strong homology with those of the CGTase (CGTase 38-2) gene previously cloned in our laboratory from the alkalophilic Bacillus sp. strain no. 38-2, although the enzymic properties of the CGTase 17-1 were distinct from those of the CGTase 38-2. To analyse those enzymic properties further, we constructed 12 chimeric CGTases using three restriction nuclease sites and compared the enzymic properties of the chimeric CGTases. The N-terminal part of the enzyme was important for heat stability, and the pH-activity profile was influenced by both the N- and the C-terminal parts. A third segment was less important for enzymic properties.

ISSN 

0022-1287

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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