Application of xylanase AlXyn10A in degradation of xylan containing complex side chains

By developing the xylanase AlXyn10A of the GH10 family, the problem of inefficient hydrolysis of complex side chains in existing technologies has been solved, thereby improving the efficiency and quality of juice processing, especially in the fields of pear juice and biomass energy.

CN122162884APending Publication Date: 2026-06-09HEBEI UNIV OF SCI & TECH
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Patent Information

Application Number
CN202610239659.5
Authority / Receiving Office
CN · China
Patent Type
Applications(China)
Current Assignee / Owner
Filing Date
2026-02-28
Publication Date
2026-06-09

AI Technical Summary

Technical Problem

Existing xylanases cannot efficiently recognize and hydrolyze complex side chains in plant cell walls, such as ferulic acylated arabinoxylan side chains (FAX3) and methylglucuronic acid xylan side chains (MeGA), leading to problems such as low juice processing efficiency, poor quality of noodle products, and low biomass energy utilization.

Method used

A xylanase, AlXyn10A, derived from rabbit Aspergillus leporis and belonging to the GH10 family, was developed. It can simultaneously recognize and specifically act on FAX3 and MeGA. It achieves efficient hydrolysis by forming hydrogen bonds and specific interactions with the side chain through key residues such as Glu48, Glu72, Asp299, Glu161, and Tyr200.

Benefits of technology

It significantly improved the efficiency of juice processing, enhanced the release rate of nutrients in juice and product stability, improved the quality of noodle products, and increased the utilization rate of biomass energy.

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Abstract

The invention belongs to the technical field of biological engineering, and particularly discloses application of xylanase AlXyn10A in degradation of xylan containing complex side chains. The amino acid sequence of the xylanase AlXyn10A provided by the invention is shown as SEQ ID NO: 1, the xylanase is derived from Aspergillus niger, the specific activity of a pure enzyme reaches 306.4 U / mg, and Co < 2 + > has a remarkable activation effect on the xylanase AlXyn10A, so that the hydrolysis performance is excellent. Structural analysis shows that the xylanase can identify two substrates FAX3 and MeGA at the same time, can effectively degrade xylan containing complex side chains, and has wide application prospects in multiple fields of food, agricultural waste recycling, spinning, papermaking, environmental protection treatment and the like. When the xylanase is applied to a preparation process of pear juice, the juice yield of the pear juice and the reducing sugar content can be remarkably improved, and ascorbic acid is effectively reserved.
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