NDLI: A recombinant cyclodextrin glycosyltransferase cloned from Paenibacillus sp. strain RB01 showed improved catalytic activity in coupling reaction between cyclodextrins and disaccharides

Content Provider	Springer Nature Link
Author	Charoensakdi, Ratiya Iizuka, Masaru Ito, Kazuo Rimphanitchayakit, Vichien Limpaseni, Tipaporn
Copyright Year	2007
Abstract	Recombinant cyclodextrin glycosyltransferase (CGTase) was obtained by cloning the PCR gene fragment from thermotolerant Paenibacillus sp. strain RB01 screened from hot spring area in Thailand and cloned into the Escherichia coli expression vector. The nucleotide sequence was analyzed and aligned. Nucleotide sequence of the recombinant CGTase contained an open reading frame of 2139 bp encoding 713 amino acid residues. The recombinant required one-third of culture time and neutral pH to produce CGTase compared to wild type. CGTases from both wild type and transformant were purified in parallel by starch adsorption and DEAE cellulose column. Their biochemical properties such as molecular weight, optimum pH and temperature were quite similar. However, the recombinant enzyme showed improved catalytic activity in the coupling reaction between cyclodextrins (CDs) and some disaccharides. Among several sugars tested with excess βCD, cellobiose was the best substrate followed by leucrose. Very low activity was observed with trehalose, lactose and mellibiose. Sucrose and raffinose showed no activity. The K $_{m}$ and other kinetic parameters of recombinant enzyme were determined for cellobiose and several cyclodextrin derivatives. Recombinant CGTase showed lower K $_{m}$ for βCD and its derivatives, with improved activity compared to wild type enzyme.
Starting Page	53
Ending Page	59
Page Count	7
File Format	PDF
ISSN	09230750
Journal	Journal of Inclusion Phenomena and Macrocyclic Chemistry
Volume Number	57
Issue Number	1-4
e-ISSN	15731111
Language	English
Publisher	Kluwer Academic Publishers
Publisher Date	2007-02-13
Publisher Place	Dordrecht
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Recombinant CGTase Improved coupling activity Crystallography Food Science Organic Chemistry
Content Type	Text
Resource Type	Article
Subject	Chemistry Condensed Matter Physics Food Science

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A recombinant cyclodextrin glycosyltransferase cloned from Paenibacillus sp. strain RB01 showed improved catalytic activity in coupling reaction between cyclodextrins and disaccharides

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