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Heteroxylan hydrolysis by a recombinant cellulase-free GH10 xylanase from the alkaliphilic bacterium Halalkalibacterium halodurans C-125

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Abstract

The search for affordable enzymes with exceptional characteristics is fundamental to overcoming industrial and environmental constraints. In this study, a recombinant GH10 xylanase (Xyn10-HB) from the extremely alkaliphilic bacterium Halalkalibacterium halodurans C-125 cultivated at pH 10 was cloned and expressed in E. coli BL21(DE3). Removal of the signal peptide improved the expression, and an overall activity of 8 U/mL was obtained in the cell-free supernatant. The molecular weight of purified Xyn10-HB was estimated to be 42.6 kDa by SDS-PAGE. The enzyme was active across a wide pH range (5–10) with optimal activity recorded at pH 8.5 and 60 °C. It also presented good stability with a half-life of 3 h under these conditions. Substrate specificity studies showed that Xyn10-HB is a cellulase-free enzyme that conventionally hydrolyse birchwood and oat spelts xylans (Apparent Km of 0.46 mg/mL and 0.54 mg/mL, respectively). HPLC analysis showed that both xylans hydrolysis produced xylooligosaccharides (XOS) with a degree of polymerization (DP) ranging from 2 to 9. The conversion yield was 77% after 24 h with xylobiose and xylotriose as the main end-reaction products. When assayed on alkali-extracted wheat straw heteroxylan, the Xyn10-HB produced active XOS with antioxidant activity determined by the DPPH radical scavenging method (IC50 of 0.54 mg/mL after 4 h). Owing to its various characteristics, Xyn10-HB xylanase is a promising candidate for multiple biotechnological applications.

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Acknowledgements

The authors gratefully acknowledge the Tunisian Ministry of Higher Education and Scientific Research LR11ES24, The University of Carthage for concession of a research grant which has allowed to Jihene Maati to perform this research. The present work was also partially supported by FCT-Fundação para a Ciência e a Tecnologia, grant numbers UIDB/BIO/04565/2020, and LA/P/0140/2020. The authors kindly thank Mr Foued Balti for the English checking and correction.

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Experimentations, methodology, interpretation and writing [Jihene Maati]; supervision, expression experiments, data processing, manuscript revision: [Duarte Miguel Prazeres]; purification, data interpretation, [Marcin Graz]; methodology, xylooligosaccharides analysis, manuscript revision: [Adrian Wiater]; supervision, data processing, manuscript revision [Anna Jaroscz-Wilkołazka], conceptualization, resources, supervision, manuscript revision: [Issam Smaali].

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Correspondence to Issam Smaali.

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Communicated by PANKAJ BHATT.

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Maati, J., Prazeres, D.M., Grąz, M. et al. Heteroxylan hydrolysis by a recombinant cellulase-free GH10 xylanase from the alkaliphilic bacterium Halalkalibacterium halodurans C-125. Arch Microbiol 206, 261 (2024). https://doi.org/10.1007/s00203-024-03982-w

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  • DOI: https://doi.org/10.1007/s00203-024-03982-w

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