Protein engineering of GH11 xylanase from Aspergillus fumigatus RT-1 for catalytic efficiency improvement on kenaf biomass hydrolysis
Enzyme hydrolysis faces a bottleneck due to the recalcitrance of the lignocellulose biomass. The protein engineering of GH11 xylanase from Aspergillus fumigatus RT-1 was performed near the active site and at the N-terminal region to improve its catalytic efficiency towards pretreated kenaf (Hibiscus...
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| Format: | Article |
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Elsevier Inc.
2019
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| _version_ | 1796864472644583424 |
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| author | Damis, Siti Intan Rosdianah Abdul Murad, Abdul Munir Abu Bakar, Farah Diba Rashid, Siti Aishah Jaafar, Nardiah Rizwana Md. Illias, Rosli |
| author_facet | Damis, Siti Intan Rosdianah Abdul Murad, Abdul Munir Abu Bakar, Farah Diba Rashid, Siti Aishah Jaafar, Nardiah Rizwana Md. Illias, Rosli |
| author_sort | Damis, Siti Intan Rosdianah |
| collection | ePrints |
| description | Enzyme hydrolysis faces a bottleneck due to the recalcitrance of the lignocellulose biomass. The protein engineering of GH11 xylanase from Aspergillus fumigatus RT-1 was performed near the active site and at the N-terminal region to improve its catalytic efficiency towards pretreated kenaf (Hibiscus cannabinus) hydrolysis. Five mutants were constructed by combined approaches of error-prone PCR, site-saturation and site-directed mutagenesis. The double mutant c168 t/Q192H showed the most effective hydrolysis reaction with a 13.9-fold increase in catalytic efficiency, followed by mutants Y7L and c168 t/Q192 H/Y7L with a 1.6-fold increase, respectively. The enhanced catalytic efficiency evoked an increase in sugar yield of up to 28% from pretreated kenaf. In addition, mutant c168 t/Q192 H/Y7L improved the thermostability at higher temperature and acid stability. This finding shows that mutations at distances less than 15 Å from the active site and at putative secondary binding sites affect xylanase catalytic efficiency towards insoluble substrates hydrolysis. |
| first_indexed | 2024-03-05T20:42:23Z |
| format | Article |
| id | utm.eprints-87593 |
| institution | Universiti Teknologi Malaysia - ePrints |
| last_indexed | 2024-03-05T20:42:23Z |
| publishDate | 2019 |
| publisher | Elsevier Inc. |
| record_format | dspace |
| spelling | utm.eprints-875932020-11-30T09:04:12Z http://eprints.utm.my/87593/ Protein engineering of GH11 xylanase from Aspergillus fumigatus RT-1 for catalytic efficiency improvement on kenaf biomass hydrolysis Damis, Siti Intan Rosdianah Abdul Murad, Abdul Munir Abu Bakar, Farah Diba Rashid, Siti Aishah Jaafar, Nardiah Rizwana Md. Illias, Rosli TP Chemical technology Enzyme hydrolysis faces a bottleneck due to the recalcitrance of the lignocellulose biomass. The protein engineering of GH11 xylanase from Aspergillus fumigatus RT-1 was performed near the active site and at the N-terminal region to improve its catalytic efficiency towards pretreated kenaf (Hibiscus cannabinus) hydrolysis. Five mutants were constructed by combined approaches of error-prone PCR, site-saturation and site-directed mutagenesis. The double mutant c168 t/Q192H showed the most effective hydrolysis reaction with a 13.9-fold increase in catalytic efficiency, followed by mutants Y7L and c168 t/Q192 H/Y7L with a 1.6-fold increase, respectively. The enhanced catalytic efficiency evoked an increase in sugar yield of up to 28% from pretreated kenaf. In addition, mutant c168 t/Q192 H/Y7L improved the thermostability at higher temperature and acid stability. This finding shows that mutations at distances less than 15 Å from the active site and at putative secondary binding sites affect xylanase catalytic efficiency towards insoluble substrates hydrolysis. Elsevier Inc. 2019-12 Article PeerReviewed Damis, Siti Intan Rosdianah and Abdul Murad, Abdul Munir and Abu Bakar, Farah Diba and Rashid, Siti Aishah and Jaafar, Nardiah Rizwana and Md. Illias, Rosli (2019) Protein engineering of GH11 xylanase from Aspergillus fumigatus RT-1 for catalytic efficiency improvement on kenaf biomass hydrolysis. Enzyme and Microbial Technology, 131 . p. 109383. ISSN 0141-0229 http://dx.doi.org/10.1016/j.enzmictec.2019.109383 |
| spellingShingle | TP Chemical technology Damis, Siti Intan Rosdianah Abdul Murad, Abdul Munir Abu Bakar, Farah Diba Rashid, Siti Aishah Jaafar, Nardiah Rizwana Md. Illias, Rosli Protein engineering of GH11 xylanase from Aspergillus fumigatus RT-1 for catalytic efficiency improvement on kenaf biomass hydrolysis |
| title | Protein engineering of GH11 xylanase from Aspergillus fumigatus RT-1 for catalytic efficiency improvement on kenaf biomass hydrolysis |
| title_full | Protein engineering of GH11 xylanase from Aspergillus fumigatus RT-1 for catalytic efficiency improvement on kenaf biomass hydrolysis |
| title_fullStr | Protein engineering of GH11 xylanase from Aspergillus fumigatus RT-1 for catalytic efficiency improvement on kenaf biomass hydrolysis |
| title_full_unstemmed | Protein engineering of GH11 xylanase from Aspergillus fumigatus RT-1 for catalytic efficiency improvement on kenaf biomass hydrolysis |
| title_short | Protein engineering of GH11 xylanase from Aspergillus fumigatus RT-1 for catalytic efficiency improvement on kenaf biomass hydrolysis |
| title_sort | protein engineering of gh11 xylanase from aspergillus fumigatus rt 1 for catalytic efficiency improvement on kenaf biomass hydrolysis |
| topic | TP Chemical technology |
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