Cell surface engineering of industrial microorganisms for biorefining applications

Tanaka, Tsutomu; Kondo, Akihiko

doi:10.1016/j.biotechadv.2015.06.002

Cited by 54 publications

(20 citation statements)

References 134 publications

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“…So, neither substrate nor product needs to be internalized or excreted through the cell membrane; therefore, cytotoxicity of the end product to the cell is alleviated, and biocatalysis is favored [16]. These systems have a wide range of biotechnological applications in many areas such as whole-cell biocatalysis for bioconversion, biosensing, biosorption, and immobilization [17][18][19][20][21][22][23]. The GDSL autotransporter is a distinctive autotransporter that consists of a lipolytic enzyme of the GDSL family of lipases or esterases as a passenger domain at the N-terminus and a β-barrel domain at C-terminus, which is necessary for secretion of the passenger protein to the outer membrane [24].…”

Section: -Vinylguaiacol (4-vg)mentioning

confidence: 99%

Functional Autodisplay of Phenolic Acid Decarboxylase using a GDSL Autotransporter on Escherichia coli for Efficient Catalysis of 4-Hydroxycinnamic Acids to Vinylphenol Derivatives

Long

et al. 2019

Catalysts

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Bioproduction of vinylphenol derivatives, such as 4-vinylguaiacol (4-VG) and 4-vinylphenol (4-VP), from 4-hydroxycinnamic acids, such as ferulic acid (FA) and p-coumaric acid (pCA), employing whole cells expressing phenolic acid decarboxylases (PAD) as a biocatalyst has attracted much attention in recent years. However, the accumulation of 4-VG or 4-VP in the cell may cause high cytotoxicity to Escherichia coli (E. coli) and consequently cell death during the process. In this study, we firstly report the functional display of a phenolic acid decarboxylase (BLPAD) from Bacillus licheniformis using a GDSL autotransporter from Pseudomonas putida on the cell surface of E. coli. Expression and localization of BLPAD on E. coli were verified by SDS-PAGE and protease accessibility. The PelB signal peptide is more effective in guiding the translocation of BLPAD on the cell surface than the native signal peptide of GDSL, and the cell surface displaying BLPAD activity reached 19.72 U/OD600. The cell surface displaying BLPAD showed good reusability and retained 63% of residual activity after 7 cycles of repeated use. In contrast, the residual activity of the intracellular expressing cells was approximately 11% after 3 cycles of reuse. The molar bioconversion yields of 72.6% and 80.4% were achieved at the concentration of 300 mM of FA and pCA in a biphasic toluene/Na2HPO4–citric acid buffer system, respectively. Its good reusability and efficient catalysis suggested that the cell surface displaying BLPAD can be used as a whole-cell biocatalyst for efficient production of 4-VG and 4-VP.

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Section: -Vinylguaiacol (4-vg)mentioning

confidence: 99%

Functional Autodisplay of Phenolic Acid Decarboxylase using a GDSL Autotransporter on Escherichia coli for Efficient Catalysis of 4-Hydroxycinnamic Acids to Vinylphenol Derivatives

Long

et al. 2019

Catalysts

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“…Surface display also promotes synergism and specific activity in different enzymes attached due to very close proximity (Schwarz 2001) and reduces the amount of total enzyme added to the bioreactor (Matano et al 2012a). Moreover, surface display aids in higher yield due to prevention of irreversible desorption of the enzyme from its substrate (Bayer et al 1994;Schwarz 2001;Matano et al 2012b;Tanaka and Kondo 2015). The surface-displayed enzymes work synergistically to hydrolyze cellulose to cello-oligosaccharides and then to glucose, which is very close to the cell surface and is immediately taken up by the fermenting microorganism instead of diffusing out into the medium, thereby increasing the yield (Yamada et al 2013).…”

Section: Alternative-designer Cellulosomesmentioning

confidence: 99%

“…The amount of cellulosomal enzymes to be displayed is dependent on the available surface area (Yamada et al 2013). Also, the unifunctional surface-displayed cellulosomes are not capable of 2-D diffusion (Tanaka and Kondo 2015). Apart from this, the cohesin-dockerin interactions are species specific, which restricts their utilization over a narrow range.…”

Section: Alternative-designer Cellulosomesmentioning

confidence: 99%

Bioprospecting thermostable cellulosomes for efficient biofuel production from lignocellulosic biomass

Arora

Behera

Sharma

et al. 2015

Bioresour. Bioprocess.

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The adverse climatic conditions due to continuous use of fossil-derived fuels are the driving factors for the development of renewable sources of energy. Current biofuel research focuses mainly on lignocellulosic biomass (LCB) such as agricultural, industrial and municipal solid wastes due to their abundance and renewability. Although many mesophilic cellulolytic microorganisms have been reported, efficient and economical bioconversion to simple sugars is still a challenge. Thermostable cellulolytic enzymes play an indispensible role in degradation of the complex polymeric structure of LCB into fermentable sugar stream due to their higher flexibility with respect to process configurations and better specific activity than the mesophilic enzymes. In some anaerobic thermophilic/thermotolerant microorganisms, few cellulases are organized as unique multifunctional enzyme complex, called the cellulosome. The use of cellulosomal multienzyme complexes for saccharification seems to be a promising and cost-effective alternative for complete breakdown of cellulosic biomass. This paper aims to explore and review the important findings in cellulosomics and forward the path for new cutting-edge opportunities in the success of biorefineries. Herein, we summarize the protein structure, regulatory mechanisms and their expression in the host cells. Furthermore, we discuss the recent advances in specific strategies used to design new multifunctional cellulosomal enzymes, which can function as lignocellulosic biocatalysts and evaluate the roadblocks in the yield and stability of such designer thermozymes with overall progress in lignocellulose-based biorefinery.

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“…In order to generate fermentable sugars such as glucose and xylose from lignocellulosic biomass, the addition of costly commercial enzymes is usually needed; however, this enzymatic treatment also generates oligomers of glucose such as cellobiose and xylose, which are not directly utilizable by a micro‐organism such as S. cerevisiae . In the last decade, the cell surface engineering approach has emerged as a promising option to obviate the addition of commercial enzymes . This approach consists of anchoring enzymes (e.g., those capable of degrading biomass) to the yeast cell wall (Figure ).…”

Section: Introductionmentioning

confidence: 99%

Combined Cell Surface Display of β‐d‐Glucosidase (BGL), Maltose Transporter (MAL11), and Overexpression of Cytosolic Xylose Reductase (XR) in Saccharomyces cerevisiae Enhance Cellobiose/Xylose Coutilization for Xylitol Bioproduction from Lignocellulosic Biomass

Guirimand

Bamba

Matsuda

et al. 2019

Biotechnology Journal

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Xylitol is a highly valuable commodity chemical used extensively in the food and pharmaceutical industries. The production of xylitol from d‐xylose involves a costly and polluting catalytic hydrogenation process. Biotechnological production from lignocellulosic biomass by micro‐organisms like yeasts is a promising option. In this study, xylitol is produced from lignocellulosic biomass by a recombinant strain of Saccharomyces cerevisiae (S. cerevisiae) (YPH499‐SsXR‐AaBGL) expressing cytosolic xylose reductase (Scheffersomyces stipitis xylose reductase [SsXR]), along with a β‐d‐glucosidase (Aspergillus aculeatus β‐glucosidase 1 [AaBGL]) displayed on the cell surface. The simultaneous cofermentation of cellobiose/xylose by this strain leads to an ≈2.5‐fold increase in Yxylitol/xylose (=0.54) compared to the use of a glucose/xylose mixture as a substrate. Further improvement in the xylose uptake by the cell is achieved by a broad evaluation of several homologous and heterologous transporters. Homologous maltose transporter (ScMAL11) shows the best performance in xylose transport and is used to generate the strain YPH499‐XR‐ScMAL11‐BGL with a significantly improved xylitol production capacity from cellobiose/xylose coutilization. This report constitutes a promising proof of concept to further scale up the biorefinery industrial production of xylitol from lignocellulose by combining cell surface and metabolic engineering in S. cerevisiae.

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Cell surface engineering of industrial microorganisms for biorefining applications

Cited by 54 publications

References 134 publications

Functional Autodisplay of Phenolic Acid Decarboxylase using a GDSL Autotransporter on Escherichia coli for Efficient Catalysis of 4-Hydroxycinnamic Acids to Vinylphenol Derivatives

Functional Autodisplay of Phenolic Acid Decarboxylase using a GDSL Autotransporter on Escherichia coli for Efficient Catalysis of 4-Hydroxycinnamic Acids to Vinylphenol Derivatives

Bioprospecting thermostable cellulosomes for efficient biofuel production from lignocellulosic biomass

Combined Cell Surface Display of β‐d‐Glucosidase (BGL), Maltose Transporter (MAL11), and Overexpression of Cytosolic Xylose Reductase (XR) in Saccharomyces cerevisiae Enhance Cellobiose/Xylose Coutilization for Xylitol Bioproduction from Lignocellulosic Biomass

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