Biochemical characterization of an organic solvent- and salt-tolerant xylanase and its application of arabinoxylan-oligosaccharides production from corn fiber gum

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Academy of National Food and Strategic Reserves Administration, No 11 Baiwanzhuang Avenue, Xicheng District, Beijing [1 ]
100037, China
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Int. J. Biol. Macromol. | 2024年
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A endo-xylanase; of the glycoside hydrolase family 10 from Schizophyllum commune DB01; was expressed in P. pastoris. Recombinant xylanase (Scxyn5) retained above 80 % maximum activity in 10 % dimethyl sulfoxide and retained 90 % maximum activity in 5 M NaCl on the substrate of birchwood xylan. The effect of NaCl on the catalytic activity of Scxyn5 was significantly different toward various substrates; which was caused by the difference of monosaccharide composition and sturcture of the substrates. Furthermore; when corn fiber gum (CFG) was used as a substrate; the catalytic activity of Scxyn5 increased by 1.3–2.03 times in 1–5 M NaCl. Based on response surface methodology; the highest catalytic activity of Scxyn5 in hydrolyzing CFG were achieved with enzymatic temperature of 50 °C; pH value of 6.0; and 4 M NaCl. These properties of Scxyn5 suit the arabinoxylan-oligosaccharides (AXOs) preparation from CFG and some other potential applications in food industry. © 2024 Elsevier B.V;
D O I：
10.1016/j.ijbiomac.2024.136146
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