A Novel endo-β-1,4-xylanase xyl-1 from Aspergillus terreus HG-52 for High-Efficiency Ramie Degumming
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...
| Main Authors: | , , , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Taylor & Francis Group
2022-11-01
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| Series: | Journal of Natural Fibers |
| Subjects: | |
| Online Access: | http://dx.doi.org/10.1080/15440478.2022.2111390 |
| _version_ | 1797679882797318144 |
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| author | Ya Wu Tong Shu Pandeng Li Zhikuan Wang Huihui Wang Fei Pan Yingnan Li Tianyi Yu Longjiang Yu |
| author_facet | Ya Wu Tong Shu Pandeng Li Zhikuan Wang Huihui Wang Fei Pan Yingnan Li Tianyi Yu Longjiang Yu |
| author_sort | Ya Wu |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-03-11T23:21:22Z |
| format | Article |
| id | doaj.art-4f047698bb054cecb93ecf4fab26f73a |
| institution | Directory Open Access Journal |
| issn | 1544-0478 1544-046X |
| language | English |
| last_indexed | 2024-03-11T23:21:22Z |
| publishDate | 2022-11-01 |
| publisher | Taylor & Francis Group |
| record_format | Article |
| series | Journal of Natural Fibers |
| spelling | doaj.art-4f047698bb054cecb93ecf4fab26f73a2023-09-20T13:26:02ZengTaylor & Francis GroupJournal of Natural Fibers1544-04781544-046X2022-11-011916138901390010.1080/15440478.2022.21113902111390A Novel endo-β-1,4-xylanase xyl-1 from Aspergillus terreus HG-52 for High-Efficiency Ramie DegummingYa Wu0Tong Shu1Pandeng Li2Zhikuan Wang3Huihui Wang4Fei Pan5Yingnan Li6Tianyi Yu7Longjiang Yu8Huazhong University of Science and TechnologyHuazhong University of Science and TechnologyHuazhong University of Science and TechnologyHuazhong University of Science and TechnologyHuazhong University of Science and TechnologyBeijing Technology and Business UniversityJiangnan UniversityHuazhong University of Science and TechnologyHuazhong University of Science and TechnologyXylanase 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.http://dx.doi.org/10.1080/15440478.2022.2111390aspergillus terreusendo-β-1,4-xylanaseimmunofluorescenceramie degumminghemicellulosehigh-efficiency |
| spellingShingle | Ya Wu Tong Shu Pandeng Li Zhikuan Wang Huihui Wang Fei Pan Yingnan Li Tianyi Yu Longjiang Yu A Novel endo-β-1,4-xylanase xyl-1 from Aspergillus terreus HG-52 for High-Efficiency Ramie Degumming Journal of Natural Fibers aspergillus terreus endo-β-1,4-xylanase immunofluorescence ramie degumming hemicellulose high-efficiency |
| title | A Novel endo-β-1,4-xylanase xyl-1 from Aspergillus terreus HG-52 for High-Efficiency Ramie Degumming |
| title_full | A Novel endo-β-1,4-xylanase xyl-1 from Aspergillus terreus HG-52 for High-Efficiency Ramie Degumming |
| title_fullStr | A Novel endo-β-1,4-xylanase xyl-1 from Aspergillus terreus HG-52 for High-Efficiency Ramie Degumming |
| title_full_unstemmed | A Novel endo-β-1,4-xylanase xyl-1 from Aspergillus terreus HG-52 for High-Efficiency Ramie Degumming |
| title_short | A Novel endo-β-1,4-xylanase xyl-1 from Aspergillus terreus HG-52 for High-Efficiency Ramie Degumming |
| title_sort | novel endo β 1 4 xylanase xyl 1 from aspergillus terreus hg 52 for high efficiency ramie degumming |
| topic | aspergillus terreus endo-β-1,4-xylanase immunofluorescence ramie degumming hemicellulose high-efficiency |
| url | http://dx.doi.org/10.1080/15440478.2022.2111390 |
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