# Purification, and characterization of xylanase by Aspergillus krugeri AUMC 15912 utilizing sugarcane bagasse under solid-state fermentation conditions

## TL;DR

Researchers optimized and purified a xylanase enzyme from a fungus using sugarcane waste, finding it effective for industrial uses like biofuel production.

## Contribution

A 508-fold purified xylanase with detailed characterization from Aspergillus krugeri using sugarcane bagasse under SSF.

## Key findings

- Xylanase activity maximized at pH 7.0 and 30°C with ammonium chloride, yielding 183 ± 16 U/g dry substrate.
- Purified enzyme showed peak activity of 1697.5 U/mg at pH 6.0 and 45°C with a molecular weight of 33.11 kDa.
- Activity varied with salts and inhibitors, with residual activity ranging from 30.12% (NiCl₂) to 86.65% (CuSO₄).

## Abstract

This study focuses on optimizing, purifying, and characterizing xylanase produced by Aspergillus krugeri AUMC 15912 utilizing sugarcane bagasse under solid-state fermentation (SSF). The strain, isolated from sugarcane bagasse, exhibited significant xylanase activity, which was maximized after six days of incubation at pH 7.0 and 30 °C using ammonium chloride as the nitrogen source, yielding 183 ± 16 U/g dry substrate (gds). The enzyme was purified 508-fold through sequential chromatography on Trilite MC 08 and Sephacryl S-200 columns, resulting in a single band of 33.11 kDa on SDS-PAGE. The purified xylanase displayed peak activity of 1697.5 U/mg at pH 6.0 and 45 °C, with kinetic parameters Km and Vmax of 1.75 mM and 17.98 µmol/min, respectively. Activity was influenced by various salts and inhibitors, with residual activity ranging from 30.12% (NiCl₂) to 86.65% (CuSO₄). These findings highlight the potential of A. krugeri AUMC 15912-derived xylanase for industrial applications in bioconversion, food processing, and biofuel production.