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Aims: This study aimed to isolate and characterize thermostable xylanases from the thermophilic bacterium Geobacillus stearothermophilus CFH 71344, screened from Yunnan hot springs, for their potential in lignocellulosic biomass conversion and xylooligosaccharide (XOS) production.
Methods And Results: Two xylanases, Xyn2415 and Xyn2429, were heterologously expressed and biochemically characterized. Biochemical characterization revealed that enzyme Xyn2415 exhibited optimal activity at pH 9.0 and 70°C, while enzyme Xyn2429 showed optimal activity at pH 6.0 and 80°C. Both enzymes demonstrated significant thermostability, retaining considerable activity even after prolonged exposure to high temperatures. The kinetic parameters indicated that Xyn2429 had higher catalytic efficiency than Xyn2415. The enzymes also exhibited distinct substrate preferences and metal ion sensitivities. When applied to beechwood xylan hydrolysis, Xyn2415 and Xyn2429 produced different XOS profiles, with Xyn2415 preferentially generating short-chain XOS and Xyn2429 producing longer-chain XOS.
Conclusions: The coexistence of these enzymes in one bacterium highlights their adaptability to varying environmental conditions, offering potential for cost-effective and efficient industrial applications in lignocellulosic biorefining and prebiotic production.
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http://dx.doi.org/10.1093/jambio/lxaf212 | DOI Listing |
Int J Biol Macromol
August 2025
School of Food Science and Engineering, South China University of Technology, Guangzhou 510640, China; State Key Laboratory of Pulp and Paper Engineering, South China University of Technology, Guangzhou 510640, China; Guangdong Youmei Institute of Intelligent Bio-manufacturing Co., Ltd, Foshan 52820
Xylanases from glycoside hydrolases family 11 (GH11) are widely used due to their substrate selectivity and broad optimal pH range. With the increasing demands in industrial production, the development of xylanases with multiple stress resistances and high thermostability has become a research focus. We heterologously expressed and characterized a novel GH11 xylanase (HWxyn11) from Hortaea werneckii.
View Article and Find Full Text PDFFoods
August 2025
Department of Animal Production and Food Science, AgriFood Institute of Aragon (IA2), Faculty of Veterinary, University of Zaragoza-CITA, Miguel Servet 177, 50013 Zaragoza, Spain.
The genera and comprise thermophilic, spore-forming bacteria. The extraordinary heat resistance of their spores, together with their ability to form biofilms and produce thermostable enzymes, makes them a relevant cause of spoilage in shelf-stable, heat-treated products like dairy and canned foods. However, these same biological traits offer valuable opportunities for the food industry.
View Article and Find Full Text PDFBioTech (Basel)
August 2025
Department of Chemistry and Environmental Sciences, Institute of Biosciences, Humanities and Exact Sciences, São Paulo State University (IBILCE-UNESP), São José do Rio Preto 15054-000, SP, Brazil.
Industrial applications of xylanases in high-temperature settings are limited by enzyme instability. This study evaluated glycerol and phenolic compounds as modulators of the catalytic and structural properties of a recombinant endoxylanase (rMhXyn) expressed in . Glycerol (20% /) significantly improved thermostability (5-fold increase in half-life at 55 °C), decreased the activation energy for catalysis, and enhanced structural rigidity as evidenced by molecular dynamics simulations (reduced RMSD and Rg).
View Article and Find Full Text PDFJ Appl Microbiol
September 2025
Synthetic Biology Engineering Lab of Henan Province, School of Life Science and Technology, Henan Medical University, No. 601 Jinsui Road, Xinxiang 453003, PR China.
Aims: This study aimed to isolate and characterize thermostable xylanases from the thermophilic bacterium Geobacillus stearothermophilus CFH 71344, screened from Yunnan hot springs, for their potential in lignocellulosic biomass conversion and xylooligosaccharide (XOS) production.
Methods And Results: Two xylanases, Xyn2415 and Xyn2429, were heterologously expressed and biochemically characterized. Biochemical characterization revealed that enzyme Xyn2415 exhibited optimal activity at pH 9.
Int J Mol Sci
July 2025
National Glycoengineering Research Center, Shandong University, Qingdao 266237, China.
Thermostable cellulases and xylanases have broad acceptance in food, feed, paper and pulp, and bioconversion of lignocellulosics. Thermophilic fungi serve as an excellent source of thermostable enzymes. This study characterized four endo-β-1,4-glucanases (two glycoside hydrolase (GH) family 5 and two GH7 members) and four endo-β-1,4-xylanases (two GH10 and two GH11 members) from thermophilic fungus , along with one GH10 endo-β-1,4-xylanase each from thermophilic fungus and mesophilic fungus .
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