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Characterization of a unique pH-dependent amylosucrase from Deinococcus cellulosilyticus.
Lee, Chang-Young; So, Yun-Sang; Lim, Min-Cheol; Jeong, Soyoung; Yoo, Sang-Ho; Park, Choen-Seok; Jung, Jong-Hyun; Seo, Dong-Ho.
Afiliación
  • Lee CY; Department of Food Science and Technology, College of Agriculture and Life Sciences, Jeonbuk National University, Jeonju 54896, Republic of Korea.
  • So YS; Department of Food Science & Biotechnology and Carbohydrate Bioproduct Research Center, Sejong University, Seoul 05006, Republic of Korea.
  • Lim MC; Research Group of Consumer Safety, Korea Food Research Institute (KFRI), Jeollabuk-do 55365, Republic of Korea.
  • Jeong S; Radiation Biotechnology Division, Korea Atomic Energy Research Institute, Jeongeup 56212, Republic of Korea; Department of Food and Animal Biotechnology, Seoul National University, Seoul 08826, Republic of Korea.
  • Yoo SH; Department of Food Science & Biotechnology and Carbohydrate Bioproduct Research Center, Sejong University, Seoul 05006, Republic of Korea.
  • Park CS; Department of Food Science and Biotechnology, Graduate School of Biotechnology and Institute of Life Science and Resources, Kyung Hee University, Yongin 17104, Republic of Korea.
  • Jung JH; Radiation Biotechnology Division, Korea Atomic Energy Research Institute, Jeongeup 56212, Republic of Korea. Electronic address: jungjh83@kaeri.re.kr.
  • Seo DH; Department of Food Science and Technology, College of Agriculture and Life Sciences, Jeonbuk National University, Jeonju 54896, Republic of Korea; Department of Food Science & Biotechnology and Carbohydrate Bioproduct Research Center, Sejong University, Seoul 05006, Republic of Korea; Department
Int J Biol Macromol ; 269(Pt 2): 131834, 2024 Jun.
Article en En | MEDLINE | ID: mdl-38688341
ABSTRACT
The amylosucrase (ASase, EC 2.4.1.4) utilizes sucrose as the sole substrate to catalyze multifunctional reactions. It can naturally synthesize α-1,4-linked glucans such as amylose as well as sucrose isomers with more favorable properties than sucrose with a lower intestinal digestibility and non-cariogenic properties. The amino acid sequence of the asase gene from Deinococcus cellulosilyticus (DceAS) exhibits low homology with those of other ASases from other Deinococcus species. In this study, we cloned and expressed DceAS and demonstrated its high activity at pH 6 and pH 8 and maintained stability. It showed higher polymerization activity at pH 6 than at pH 8, but similar isomerization activity and produced more turanose and trehalulose at pH 6 than at pH 8 and produced more isomaltulose at pH 8. Furthermore, the molecular weight of DceAS was 226.6 kDa at pH 6 and 145.5 kDa at pH 8, indicating that it existed as a trimer and dimer, respectively under those conditions. Additionally, circular dichroism spectra showed that the DceAS secondary structure was different at pH 6 and pH 8. These differences in reaction products at different pHs can be harnessed to naturally produce sucrose alternatives that are more beneficial to human health.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Deinococcus / Glucosiltransferasas Idioma: En Revista: Int J Biol Macromol Año: 2024 Tipo del documento: Article Pais de publicación: Países Bajos
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Deinococcus / Glucosiltransferasas Idioma: En Revista: Int J Biol Macromol Año: 2024 Tipo del documento: Article Pais de publicación: Países Bajos