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Protein engineering of GH11 xylanase from Aspergillus fumigatus RT-1 for catalytic efficiency improvement on kenaf biomass hydrolysis

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

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Official URL: http://dx.doi.org/10.1016/j.enzmictec.2019.109383

Abstract

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.

Item Type:Article
Uncontrolled Keywords:Active site, Catalytic efficiency
Subjects:T Technology > TP Chemical technology
Divisions:Chemical and Energy Engineering
ID Code:87593
Deposited By: Widya Wahid
Deposited On:30 Nov 2020 17:04
Last Modified:30 Nov 2020 17:04

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