English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

Xylanase is the key enzyme responsible for the degradation of hemicellulose and plays an important role in ramie degumming. In this study, an endo-β-1,4-xylanase xyl-1 of GH11 family from  Aspergillus terreus  HG-52 was cloned and identified for the first time. The protein was heterologously expressed in  Escherichia coli  BL21, then purified and analyzed for its biochemical properties. The optimal temperature and pH of xyl-1 are 45°C and pH 5, respectively, with a specific activity as high as 1505.11 U/mg. The immunofluorescence staining combined in-situ catalysis of ramie slices revealed that xyl-1 could degrade ramie xylan fraction. The scanning electron microscopy, X-ray diffraction, and Fourier-transform infrared spectroscopy analysis of ramie fibers treated by xyl-1 showed that the treated fibers were more dispersed, the crystallinity was improved, the absorption peak of hemicellulose functional group was reduced. Residual hemicellulose content reduced from 14.93% to 5.75% and whiteness was reached 45.4, indicating xyl-1 had high-efficiency degumming ability for ramie hemicellulose. This work excavated a promising endo-β-1,4-xylanase for ramie fibers degumming applications and has good potential for commercial application.

A Novel endo-β-1,4-xylanase xyl-1 from Aspergillus terreus HG-52 for High-Efficiency Ramie Degumming