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Comparative study on four amylosucrases from Bifidobacterium species
Sun-Young Kim1, Dong-Ho Seo2, Se-Hyun Kim1
1Graduate School of Biotechnology and Institute of Life Science and Resources, Kyung Hee University, Yongin 17104, Republic of Korea.
International Journal of Biological Macromolecules
|March 30, 2020
Summary
Four amylosucrases (ASases) from Bifidobacterium sp. were characterized, showing varied optimal temperatures and pH levels. These enzymes exhibit versatile properties for producing valuable biomaterials.
Area of Science:
- Enzymology
- Biotechnology
- Microbial Biochemistry
Background:
- Amylosucrase (ASase) is an enzyme responsible for α-glucan production.
- Bifidobacterium species are known producers of various enzymes with industrial applications.
Purpose of the Study:
- To clone and express four putative amylosucrase genes (bdas, blas, bpas, btas) from Bifidobacterium sp.
- To characterize the enzymatic properties of the expressed Bifidobacterium ASases (BASs).
Main Methods:
- Gene cloning and expression in Escherichia coli.
- Enzyme activity assays at different temperatures and pH values.
- Analysis of glucan synthesis, including isomerization and polymerization.
Main Results:
- All four BASs exhibited typical ASase activity with distinct characteristics.
- Optimal temperatures ranged from 30°C to 50°C, and optimal pH from 5.0 to 8.0.
- BlAS showed high trehalulose production, while BtAS produced α-1,4-glucans with a lower degree of polymerization.
Conclusions:
- The characterized BASs possess versatile enzymatic properties.
- These enzymes have potential for efficient production of valuable biomaterials in agriculture, food, and pharmaceutical industries.
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