Purification and Characterization of Xylanase Produced by Aspergillus fumigatus Isolated from the Northern Border Region of Saudi Arabia

Ameen, Fuad

doi:10.3390/fermentation9070595

Cited by 5 publications

(1 citation statement)

References 46 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Furthermore, these enzymes exhibit remarkable versatility and can be used in diverse sectors such as alternative fuel generation, baking, prebiotic preparation, and the clarification of fruit juices [2][3][4][5][6]. The source of this enzyme has primarily been associated with various fungi (for example, Fusarium [2], Trichoderma [7], Aspergillus [8], Thielavia [9], and Rhizomucor [10]), and bacteria (for example, Bacillus [4], Streptomyces [11], Paenibacillus [12], and Halomonas [13]), showcasing the diverse microbial sources of this enzyme. Among…”

Section: Introductionmentioning

confidence: 99%

Optimization Production of an Endo-β-1,4-Xylanase from Streptomyces thermocarboxydus Using Wheat Bran as Sole Carbon Source

Tran,

Doan,

Dinh

et al. 2024

Recycling

View full text Add to dashboard Cite

Xylanases, key enzymes for hydrolyzing xylan, have diverse industrial applications. The bioprocessing of agricultural byproducts to produce xylanase through fermentation approaches is gaining importance due to its significant potential to reduce enzyme production costs. In this work, the productivity of Streptomyces thermocarboxydus TKU045 xylanase was enhanced through liquid fermentation employing wheat bran as the sole carbon source. The maximum xylanase activity (25.314 ± 1.635 U/mL) was obtained using the following optima factors: 2% (w/v) wheat bran, 1.4% (w/v) KNO3, an initial pH of 9.8, an incubation temperature of 37.3 °C, and an incubation time of 2.2 days. Xylanase (Xyn_TKU045) of 43 kDa molecular weight was isolated from the culture supernatant and was biochemically characterized. Analysis through liquid chromatography with tandem mass spectrometry revealed a maximum amino acid identity of 19% with an endo-1,4-β-xylanase produced by Streptomyces lividans. Xyn_TKU045 exhibited optimal activity at pH 6, with remarkable stability within the pH range of 6.0 to 8.0. The enzyme demonstrated maximum efficiency at 60 °C and considerable stability at ≤70 °C. Mg2+, Mn2+, Ba2+, Ca2+, 2-mercaptoethanol, Tween 20, Tween 40, and Triton X-100 positively influenced Xyn_TKU045, while Zn2+, Fe2+, Fe3+, Cu2+, and sodium dodecyl sulfate exhibited adverse impact. The kinetic properties of Xyn_TKU045 were a Km of 0.628 mg/mL, a kcat of 75.075 s−1 and a kcat/Km of 119.617 mL mg−1s−1. Finally, Xyn_TKU045 could effectively catalyze birchwood xylan into xylotriose and xylobiose as the major products.

show abstract