Biochemical Characterization of Alkaliphilic Cyclodextran Glucanotransferase from an Alkaliphilic Bacterium, Paenibacillus daejeonensis

• Published in: Journal of microbiology and biotechnology Vol. 28; no. 12; pp. 2029 - 2035
• Main Authors: Yang, So-Jin, Ko, Jin-A, Kim, Hae-Soo, Jo, Min-Ho, Lee, Ha-Nul, Park, Bo-Ram, Kim, YoungMin
• Format: Journal Article
• Language: English
• Published: Korea (South) 한국미생물·생명공학회 28.12.2018
• Subjects: Amino Acid Sequence; Cloning, Molecular; Enzyme Assays; Enzyme Stability; Escherichia coli - genetics; Gene Expression Regulation, Bacterial; Glucosyltransferases - chemistry; Glucosyltransferases - genetics; Glucosyltransferases - isolation & purification; Hydrogen-Ion Concentration; Kinetics; Metals; Paenibacillus - enzymology; Paenibacillus - genetics; Recombinant Proteins - genetics; Solubility; Substrate Specificity; Temperature; 생물학; glycoside hydrolase family 66; Cyclodextran; Paenibacillus daejeonensis; cycloisomaltooligosaccharide glucanotransferase
• ISSN: 1017-7825; 1738-8872
• DOI: 10.4014/jmb.1810.10007

Cycloisomaltooligosaccharide glucanotransferase (CITase) was isolated from alkaliphilic via an amino acid homology search for the reported CITase. The recombinant alkaliphilic CITase (PDCITase) from was expressed in an expression system and purified as a single protein band of 111 kDa. PDCITase showed optimum activity at pH 8.0 and retained 100% of activity within a broad pH range (7.0-11.5) after 18 h, indicating alkaliphilic or alkalistable CITase properties. In addition, PDCITase produced CI-7 to CI-17, CI-18, and CI-19, which are relatively large cycloisomaltooligosaccharides yet to be reported. Therefore, these large cycloisomaltooligosaccharides can be applied to the improvement of water solubility of pharmaceutical biomaterials.