Journal
BIORESOURCES
Volume 17, Issue 2, Pages 3067-3081Publisher
NORTH CAROLINA STATE UNIV DEPT WOOD & PAPER SCI
DOI: 10.15376/biores.17.2.3067-3081
Keywords
Athe_0181; CbMan5C; Cel5A; Glycoside hydrolase; Lignocellulose hydrolysis; Noncatalytic protein; Synergism
Categories
Funding
- National Natural Science Foundation of China [21706089]
- Universities Natural Science Research Project of Jiangsu Province [19KJA430016]
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The noncatalytic protein Athe_0181 secreted by Caldicellulosiruptor bescii was shown to have high affinity to lignocellulose and played a role in the synergism of glycoside hydrolases for efficient hydrolysis of lignocellulose.
Caldicellulosiruptor bescii is a cellulolytic bacterium that secretes multifunctional glycoside hydrolases for efficient hydrolysis of lignocellulose into fermentable sugars. Additionally, some abundant noncatalytic proteins accompanying multifunctional glycoside hydrolases are also secreted by C. bescii , but its function has not yet been demonstrated. In this study, noncatalytic protein Athe_0181 and multifunctional glycoside hydrolases CbMan5C/Cel5A were expressed and purified from Escherichia coli BL21(DE3). Effective binding capacity of Athe_0181 to lignocellulose was displayed, and it showed preferential affinity to rice straw. Athe_0181 was shown to be a cellulase synergistic protein. It exhibited high synergistic activity of 523% in the presence of 25 ??g/mL of CbMan5C/Cel5A with microcrystalline cellulose as the substrate. The structure-modifying activity of Athe_0181 to microcrystalline cellulose was demonstrated by scanning electron microscopy and X-ray diffraction analysis. These characteristics demonstrated that Athe_0181 played a role in the synergism of glycoside hydrolases from C. bescii for efficient hydrolysis of lignocellulose.
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