Rational design of xylose dehydrogenase for improved thermostability and its application in development of efficient enzymatic biofuel cell

Feng, Ruyong; Liang, Bo; Hou, Chaohuan; Han, Dongfei; Han, Lei; Lang, Qiaolin; Liu, Aihua; Han, Lihui

doi:10.1016/j.enzmictec.2015.12.002

Cited by 27 publications

(15 citation statements)

References 35 publications

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“…It is noteworthy that this EFC could retain 85% of its maximal power after 12 h of continuous operation. A rationally designed XDH mutant NA-1 with improved thermostability was anchored on the bacterial surface 493 . After 12 h operation, 88% of its maximal power was retained 493 .…”

Section: Efficient Efcs Based On Microbial Surface Displayed Enzyme Amentioning

confidence: 99%

Tackling the Challenges of Enzymatic (Bio)Fuel Cells

et al. 2019

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The ever-increasing demands for clean and sustainable energy sources combined with rapid advances in bio-integrated portable or implantable electronic devices have stimulated intensive research activities in enzymatic (bio)fuel cells (EFCs). The use of renewable biocatalysts, the utilization of abundant green, safe, and high energy density fuels, together with the capability of working at modest and biocompatible conditions, make EFCs promising as next generation alternative power sources. However, the main challenges (low energy density, relatively low power density, poor operational stability and limited voltage output) hinder future applications of EFCs. This review aims at exploring the underlying mechanism of EFCs and providing possible practical strategies, methodologies and insights to tackle of these issues. Firstly, this review summarizes approaches in achieving high energy densities in EFCs, particularly, employing enzyme cascades for the deep/complete oxidation of fuels. Secondly, strategies for increasing power densities in EFCs, including increasing enzyme activities, facilitating electron transfers, employing nanomaterials, and designing more efficient enzyme-electrode interfaces, are described. The potential of EFCs/(super)capacitor combination is discussed. Thirdly, the review evaluates a range of strategies for improving the stability of EFCs, including the use of different enzyme immobilization approaches, tuning enzyme properties, designing protective matrixes, and using microbial surface displaying enzymes. Fourthly, approaches for the improvement of the cell voltage of EFCs are highlighted. Finally, future developments and a prospective on EFCs are envisioned.

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Section: Efficient Efcs Based On Microbial Surface Displayed Enzyme Amentioning

confidence: 99%

Tackling the Challenges of Enzymatic (Bio)Fuel Cells

et al. 2019

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“…Furthermore, the obtained transaminase variant was highly stable in high organic solvent concentrations and high temperature, required to enhance the solubility of prositagliptin ketone, leading to the commercial production of the antidiabetic Sitagliptin drug (Januvia ® ) (Savile et al, 2010 andKau &Asano, 2012). RD of xylose dehydrogenase for improving enzyme thermostability resulted in obtaining variants with superior thermostability, showing 5-fold higher enzyme half-life (Feng et al, 2016). Recently, Hu et al (2017) reported improvement of several properties of β-Mannanase using RD strategy for enzyme N-glycosylation, where the proper sites for N-glycosylation were selected in the protein loop area and carbohydrate chain was successfully linked to the enzyme.…”

Section: Enzyme Engineering For Enzyme Function Enhancementmentioning

confidence: 99%

Recent Trends for Discovery and Enhancement of Enzyme Function: A Review

Ibrahim

El‐Dewany

2018

Egypt. J. Microbiol.

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R ECENTLY, there is a growing recognition of enzymes utilization as ecofriendly alternative for chemical catalysts in various industrial sectors. Two main approaches are used to expand the enzymes utilization in various industrial applications including (i) Searching nature for discovery of better performing novel biocatalysts and (ii) Improvement of the enzyme function and properties. The recent advances in biocatalyst discovery and engineering have led to an increase of the efficiency and functional diversityof enzymes. Therefore, enzyme application is expanding to broader industrial processes, including those which were previously restricted to the classical chemical catalysts. Furthermore, there is a significant success in developing made-to-order enzymes that meet the industrial process conditions requirements, leading to more efficient and cost-effective processes. Here I highlight state-of-the-art strategies and tools for novel enzyme discovery and function enhancement, including enzyme engineering at the molecular level through different approaches such as directed evolution, rational design, semi rational design and computational de novo enzyme design; in addition to the recently developed field, nanobiocatalysis.

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“…A similar result was found in rehydrated freeze-dried samples at pH 8.0, however, when pH was increased to 8.5, the half-life of the enzyme decreased dramatically. Recently, the thermostability of this enzyme has been improved by rational design mutagenesis for its application in the development of an efficient enzymatic biofuel cell (Feng et al, 2016). Thus, pH 8.0 was chosen for storage and reaction conditions.…”

Section: Stability Studiesmentioning

confidence: 99%