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Carboxy-Terminal Region of a Thermostable CITase from Thermoanaerobacter thermocopriae Has the Ability to Produce Long Isomaltooligosaccharides

Journal of Microbiology and Biotechnology 2019년 29권 12호 p.1938 ~ 1946
정우수 ( Jeong Woo-Soo ) - Rural Development Administration National Institute of Sgricultural Science Department of Agro-food Resources

 ( Kim Yu-Ri ) - Chonnam National University Department of Food Science and Technology
홍성진 ( Hong Seong-Jin ) - Chonnam National University Department of Food Science and Technology
 ( Choi Su-Jeong ) - Chonnam National University Department of Food Science and Technology
최지호 ( Choi Ji-Ho ) - Rural Development Administration National Institute of Sgricultural Science Department of Agro-food Resources
 ( Park Shin-Young ) - Rural Development Administration National Institute of Sgricultural Science Department of Agro-food Resources
 ( Woo Eui-Jeon ) - Korea Research Institute of Bioscience and Biotechnology
김영민 ( Kim Young-Min ) - Chonnam National University Department of Food Science and Technology
박보람 ( Park Bo-Ram ) - Rural Development Administration National Institute of Sgricultural Science Department of Agro-food Resources

Abstract


Isomaltooligosaccharides (IMOs) have good prebiotic effects, and long IMOs (LIMOs) with a degree of polymerization (DP) of 7 or above show improved effects. However, they are not yet commercially available, and require costly enzymes and processes for production. The Nterminal region of the thermostable Thermoanaerobacter thermocopriae cycloisomaltooligosaccharide glucanotransferase (TtCITase) shows cyclic isomaltooligosaccharide (CI)-producing activity owing to a catalytic domain of glycoside hydrolase (GH) family 66 and carbohydrate-binding module (CBM) 35. In the present study, we elucidated the activity of the C-terminal region of TtCITase (TtCITase-C; Met740?Phe1,559), including a CBM35-like region and the GH family 15 domain. The domain was successfully cloned, expressed, and purified as a single protein with a molecular mass of 115 kDa. TtCITase-C exhibited optimal activity at 40°C and pH 5.5, and retained 100% activity at pH 5.5 after 18-h incubation. TtCITase-C synthesized α-1,6 glucosyl products with over seven degrees of polymerization (DP) by an α-1,6 glucosyl transfer reaction from maltopentaose, isomaltopentaose, or commercialized maltodextrins as substrates. These results indicate that TtCITase-C could be used for the production of α-1,6 glucosyl oligosaccharides with over DP7 (LIMOs) in a more cost-effective manner, without requiring cyclodextran.

키워드

Cycloisomalto-oligosaccharide glucanotransferase; cyclodextran; long isomaltooligosaccharides; Thermoanaerobacter thermocopriae
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