Metabolic engineering applications to renewable resource utilization

Aristidou, Aristos; Penttilä, Merja

doi:10.1016/s0958-1669(00)00085-9

Cited by 383 publications

(208 citation statements)

References 57 publications

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“…Linear cellulose typically occurs as parallel polymers with extensive hydrogen bonding (Lynd 1996). This structural conformation, as well as the close association with lignin, hemicellulose, starch, protein and minerals makes cellulose highly resistant to hydrolysis (Aristidou and Penttilä 2000;Klinke et al 2004;Perez et al 2002;Zaldivar et al 2001).…”

Section: Lignocellulosic Biomassmentioning

confidence: 99%

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Alcoholic fermentation of carbon sources in biomass hydrolysates by Saccharomyces cerevisiae: current status

Maris

Abbott

Bellissimi

et al. 2006

Antonie van Leeuwenhoek

436

276

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Fuel ethanol production from plant biomass hydrolysates by Saccharomyces cerevisiae is of great economic and environmental significance. This paper reviews the current status with respect to alcoholic fermentation of the main plant biomass-derived monosaccharides by this yeast. Wild-type S. cerevisiae strains readily ferment glucose, mannose and fructose via the Embden-Meyerhof pathway of glycolysis, while galactose is fermented via the Leloir pathway. Construction of yeast strains that efficiently convert other potentially fermentable substrates in plant biomass hydrolysates into ethanol is a major challenge in metabolic engineering. The most abundant of these compounds is xylose. Recent metabolic and evolutionary engineering studies on S. cerevisiae strains that express a fungal xylose isomerase have enabled the rapid and efficient anaerobic fermentation of this pentose.L-Arabinose fermentation, based on the expression of a prokaryotic pathway in S. cerevisiae, has also been established, but needs further optimization before it can be considered for industrial implementation. In addition to these already investigated strategies, possible approaches for metabolic engineering of galacturonic acid and rhamnose fermentation by S. cerevisiae are discussed. An emerging and major challenge is to achieve the rapid transition from proof-of-principle experiments under 'academic' conditions (synthetic media, single substrates or simple substrate mixtures, absence of toxic inhibitors) towards efficient conversion of complex industrial substrate mixtures that contain synergistically acting inhibitors.

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Section: Lignocellulosic Biomassmentioning

confidence: 99%

“…Hemicellulose composition is strongly dependent on the plant source. However, in contrast to cellulose, hemicellulose is easily hydrolyzed to its constituent monosaccharides (Aristidou and Penttilä 2000;Klinke et al 2004;Perez et al 2002;Zaldivar et al 2001).…”

Section: Lignocellulosic Biomassmentioning

confidence: 99%

Alcoholic fermentation of carbon sources in biomass hydrolysates by Saccharomyces cerevisiae: current status

Maris

Abbott

Bellissimi

et al. 2006

Antonie van Leeuwenhoek

436

276

View full text Add to dashboard Cite

show abstract

“…So far, key contributions enable the utilization of the pentose sugars which C. glutamicum naturally cannot metabolize. These sugars, namely xylose and arabinose, display significant fractions in agricultural residues and other lignocellulosic biomass recently receiving increasing interest as a cheap and most abundant raw material for biobased production [161]. Through heterologous expression of the E. coli genes xylA and xylB C. glutamicum was able to consume xylose as sole source of carbon [162].…”

Section: Utilization Of Alternative Substratesmentioning

confidence: 99%

Analysis and Engineering of Metabolic Pathway Fluxes in Corynebacterium glutamicum

Wittmann

2010

Biosystems Engineering I

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The Gram-positive soil bacterium Corynebacterium glutamicum was discovered as a natural overproducer of glutamate about 50 years ago. Linked to the steadily increasing economical importance of this microorganism for production of glutamate and other amino acids, the quest for efficient production strains has been an intense area of research during the past few decades. Efficient production strains were created by applying classical mutagenesis and selection and especially metabolic engineering strategies with the advent of recombinant DNA technology. Hereby experimental and computational approaches have provided fascinating insights into the metabolism of this microorganism and directed strain engineering. Today, C. glutamicum is applied to the industrial production of more than 2 million tons of amino acids per year. The huge achievements in recent years, including the sequencing of the complete genome and efficient post genomic approaches, now provide the basis for a new, fascinating era of research -analysis of metabolic and regulatory properties of C. glutamicum on a global scale towards novel and superior bioprocesses.

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“…1) Among them, xylan is composed of -1,4-linked xylopyranosyl units which carry side groups such as acetyl-, arabinofuranosyl-, and glucuronylgroups. 2) The complete breakdown of a branched xylan requires the action of several hydrolytic enzymes, i.e., endo-1,4--xylanase (xylanase), which attacks the polysaccharide backbone, -xylosidase, which hydrolyzes xylooligosaccahrides to D-xylose, and a series of enzymes which cleave side-chain groups.…”

mentioning

confidence: 99%

“…7) Nowadays, the use ofxylosidase in fermentation of xylose or xylose-containing hydrolyzate for ethanol production or bioconversion into xylitol has been focused on. 8,9) Clostridium stercorarium is a thermophilic anaerobic bacterium 10) capable of fermenting various kinds of polysaccharides such as xylan and recognized as a good source of thermophilic glycoside hydrolases and their genes. Indeed, so far, several genes encoding xylanase and -xylosidase have been cloned and characterized along with their gene products, i.e., xylanase genes xynA, 11) xynB 12) and xynC, 13) and -xylosidase genes xylA, 14) bxlA and bxlB.…”

mentioning

confidence: 99%

Sequencing and Expression of the Gene Encoding theClostridium stercorariumβ-Xylosidase Xyl43B inEscherichia coli

Suryani

Kimura

Sakka

et al. 2004

Bioscience, Biotechnology, and Biochemistry

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The Clostridium stercorarium F-9 xyl43B gene encoding the -xylosidase Xyl43B consists of an open reading frame of 1,491 nucleotides that encodes a putative protein, classified in family 43, of 497 amino acids with a predicted molecular weight of 56,355. The deduced amino acid sequence of Xyl43B has sequence similarity with -xylosidases from Bacteriodes thetaiotaomicron (57% sequence identity), Prevotella ruminicola (45%), Streptomyces coelicolor (40%), and Clostridium acetobutylicum (36%), all of which have been classified in family 43 of the glycoside hydrolases. Xyl43B was purified from a recombinant Escherichia coli and characterized. The optimum pH of the purified enzyme was 3.5 and it was stable over pH from 3.0 to 8.0. Its optimum temperature was 80 C and it showed thermostability in the temperature range from 50 to 70 C. Xyl43B had a K m of 6.2 mM and a V max of 15 mol min À1 mg À1 for p-nitrophenyl--D-xylopyranoside.

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Metabolic engineering applications to renewable resource utilization

Cited by 383 publications

References 57 publications

Alcoholic fermentation of carbon sources in biomass hydrolysates by Saccharomyces cerevisiae: current status

Alcoholic fermentation of carbon sources in biomass hydrolysates by Saccharomyces cerevisiae: current status

Analysis and Engineering of Metabolic Pathway Fluxes in Corynebacterium glutamicum

Sequencing and Expression of the Gene Encoding theClostridium stercorariumβ-Xylosidase Xyl43B inEscherichia coli

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