Cloning and characterization of a novel mesophilic xylanase gene from Z-1.

UNLABELLED

In order to search for high specific activity and the resistant xylanases to XIP-I and provide more alternative xylanases for industrial production, a strain of from produced xylanases was isolated and identified. Three xylanase genes from Z-1 were cloned and successfully expressed in and , respectively. The specific activities of xyn1 xyn2 and xyn3 for birchwood xylan were 38.79, 0.85 and 243.83 U/mg in , and 40.11, 0 and 910.37 U/mg in , respectively. xyn3 and xyn3 had the similar optimum pH at 6.0 and pH stability at 5.0-9.0. However, they had different optimum temperature and thermal stability, with 30 °C for xyn3 and 40 °C for xyn3, and 4-35 °C for xyn3 and 4-40 °C for xyn3, respectively. The substrate spectrum and the kinetic parameters showed that the two xylanases also exhibited the highest xylanase activity and catalytic efficiency (/) toward birchwood xylan, with 243.83 U/mg and 61.44 mL/mg/s for xyn3 and 910.37 U/mg and 910.37 mL/mg/s for xyn3, respectively. This study provided a novel mesophilic xylanase with high specific activity and catalytic efficiency, thus making it a promising candidate for extensive applications in animal feed and food industry.

SUPPLEMENTARY INFORMATION

The online version contains supplementary material available at 10.1007/s13205-024-03973-0.