# Characterization of two GH10 enzymes with ability to hydrolyze pretreated Sorghum bicolor bagasse

**Authors:** Camila Bruno Baron, María Laura Mon, Rubén Marrero Díaz de Villegas, Andrea Cattaneo, Paola Di Donato, Annarita Poli, Maria Emilia Negri, Mariana Alegre, Marcelo A. Soria, María Cecilia Rojo, Mariana Combina, Ilaria Finore, Paola M. Talia

PMC · DOI: 10.1007/s00253-025-13484-4 · Applied Microbiology and Biotechnology · 2025-04-28

## TL;DR

Two new enzymes from termite gut microbes can break down sorghum waste and produce antioxidant compounds.

## Contribution

Discovery and characterization of two novel GH10 xylanases from termite gut microbiome with potential industrial applications.

## Key findings

- Xyl10 C and Xyl10E showed xylanase activity on pretreated Sorghum bicolor bagasse and other substrates.
- Xyl10E produced xylo-oligosaccharides with antioxidant activity from sorghum bagasse.
- Both enzymes exhibited optimal activity under different pH and temperature conditions.

## Abstract

In this study, we characterized two novel enzymes of the glycoside hydrolase family 10 (GH10), Xyl10 C and Xyl10E, identified in the termite gut microbiome. The activities of both enzymes were assayed using beechwood xylan, barley β-glucan, and pretreated Sorghum bicolor bagasse (SBB) as substrates. Both enzymes, assessed individually and in combination, showed activity on beechwood xylan and pretreated SBB, whereas Xyl10E also showed activity on barley β-glucan. The composition of pretreated SBB mainly consisted of xylose and arabinose content. Purified Xyl10 C showed optimum xylanase activity in the pH range 7.0–8.0 and at a temperature of 50–60 °C, while Xyl10E was active at a wider pH range (5.0–10.0) and at 50 °C. The residual activities of Xyl10 C and Xyl10E after 8 h of incubation at 40 °C were 85% and 70%, respectively. The enzymatic activity of Xyl10 C increased to 115% in the presence of 5 M NaCl, was only inhibited in the presence of 0.5% sodium dodecyl sulfate (SDS), and decreased with β-mercaptoethanol. The xylanase and glucanase activities of Xyl10E were inhibited only in the presence of MnSO4, NaCl, and SDS. The main hydrolysis enzymatic product of Xyl10 C and Xyl10E on pretreated SBB was xylobiose. In addition, the xylo-oligosaccharides produced by xylanase Xyl10E on pretreated SBB demonstrated promising antioxidant activity. Thus, the hydrolysis products using Xyl10E on pretreated SBB indicate potential for antioxidant activity and other valuable industrial applications.

• Two novel GH10 xylanases from the termite gut microbiome were characterized.

• Xylo-oligosaccharides obtained from sorghum bagasse exhibited antioxidant potential.

• Both enzymes and their hydrolysis product have potential to add value to agro-waste.

The online version contains supplementary material available at 10.1007/s00253-025-13484-4.

## Linked entities

- **Chemicals:** NaCl (PubChem CID 5234), sodium dodecyl sulfate (PubChem CID 3423265), MnSO4 (PubChem CID 24580)
- **Species:** Sorghum bicolor (taxon 4558)

## Full-text entities

- **Chemicals:** arabinose (MESH:D001089), xylose (MESH:D014994), NaCl (MESH:D012965), MnSO4 (-), SDS (MESH:D012967), Xylo-oligosaccharides (MESH:C570991), xylobiose (MESH:C004173)
- **Species:** gut metagenome (species) [taxon 749906], Sorghum bicolor (broomcorn, species) [taxon 4558]

## Full text

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## Figures

7 figures with captions in the complete paper: https://tomesphere.com/paper/PMC12037437/full.md

## References

5 references — full list in the complete paper: https://tomesphere.com/paper/PMC12037437/full.md

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Source: https://tomesphere.com/paper/PMC12037437