Biochemical characterization of xylanase GH11 isolated from Aspergillus niger BCC14405 (XylB) and its application in xylooligosaccharide production

• Published in: Biotechnology letters Vol. 43; no. 12; pp. 2299 - 2310
• Main Authors: Aiewviriyasakul, Katesuda, Bunterngsook, Benjarat, Lekakarn, Hataikarn, Sritusnee, Wipawee, Kanokratana, Pattanop, Champreda, Verawat
• Format: Journal Article
• Language: English
• Published: Dordrecht Springer Netherlands 01.12.2021; Springer Nature B.V
• Subjects: Applied Microbiology; arabinoxylan; Aspergillus niger; Aspergillus niger - chemistry; Aspergillus niger - enzymology; Biochemistry; biomass; Biomedical and Life Sciences; Biotechnology; Carboxymethylcellulose; Cellulose; Crystalline cellulose; Endo-1,4-beta Xylanases - genetics; Endo-1,4-beta Xylanases - isolation & purification; Energy costs; Enzyme Stability - genetics; Enzymes; family; genes; Glucuronates - biosynthesis; Glucuronates - chemistry; Glycosidases; Glycosyl hydrolase; heat tolerance; Hydrogen-Ion Concentration; Hydrolase; Hydrolysis; Life Sciences; Lignocellulose; Microbiology; Oligosaccharides - biosynthesis; Oligosaccharides - chemistry; Original Research Paper; Phosphoric acid; prebiotics; Saccharification; Substrate Specificity; Substrates; Temperature; Xylan; Xylanase; xylanases; Xylans - genetics; Xylans - metabolism; XylB gene; xylooligosaccharides; Yeast; yeasts; Glycosyl hydrolase; Xylanase; Lignocellulose; Xylooligosaccharides; Aspergillus niger
• ISSN: 0141-5492; 1573-6776; 1573-6776
• DOI: 10.1007/s10529-021-03202-1

Objective To develop an endo-β-1,4-xylanase with high specificity for production of prebiotic xylooligosaccharides that optimally works at moderate temperature desirable to reduce the energy cost in the production process. Results The xylB gene, encoding for a glycosyl hydrolase family 11 xylanase from a thermoresistant fungus, Aspergillus niger BCC14405 was expressed in a methylotrophic yeast P . pastoris KM71 in a secreted form. The recombinant XylB showed a high specific activity of 3852 and 169 U mg −1 protein on beechwood xylan and arabinoxylan, respectively with no detectable side activities against different forms of cellulose (Avicel Ò PH101 microcrystalline cellulose, phosphoric acid swollen cellulose and carboxymethylcellulose). The enzyme worked optimally at 45 °C, pH 6.0. It showed a specific cleavage pattern by releasing xylobiose (X2) as the major product from xylooligosaccharides (X3 to X6) substrates. The highest XOS yield of 708 mg g −1 substrate comprising X2, X3 and X6 was obtained from beechwood xylan hydrolysis. Conclusion The enzyme is potent for XOS production and for saccharification of lignocellulosic biomass.