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Lee R Lynd - One of the best experts on this subject based on the ideXlab platform.

  • Inhibition of Pyruvate Kinase From Thermoanaerobacterium saccharolyticum by IMP Is Independent of the Extra-C Domain.
    Frontiers in microbiology, 2021
    Co-Authors: Christopher A. Fenton, Lee R Lynd, Daniel G. Olson, Marybeth Maloney, Qingling Tang, Jeffrey L. Bose, Aron W. Fenton
    Abstract:

    The pyruvate kinase (PYK) isozyme from Thermoanaerobacterium saccharolyticum (TsPYK) has previously been used in metabolic engineering for improved ethanol production. This isozyme belongs to a subclass of PYK isozymes that include an extra C-domain. Like other isozymes that include this extra C-domain, we found that TsPYK is activated by AMP and ribose-5-phosphate (R5P). Our use of sugar-phosphate analogs generated a surprising result in that IMP and GMP are allosteric inhibitors (rather than activators) of TsPYK. We believe this to be the first report of any PYK isozyme being inhibited by IMP and GMP. A truncated protein that lacks the extra C-domain is also inhibited by IMP. A screen of several other bacterial PYK enzymes (include several that have the extra-C domain) indicates that the inhibition by IMP is specific to only a subset of those isozymes.

  • inhibition of pyruvate kinase from Thermoanaerobacterium saccharolyticum by imp is independent of the extra c domain
    Frontiers in Microbiology, 2021
    Co-Authors: Christopher A. Fenton, Lee R Lynd, Daniel G. Olson, Marybeth Maloney, Qingling Tang, Jeffrey L. Bose, Aron W. Fenton
    Abstract:

    The pyruvate kinase (PYK) isozyme from Thermoanaerobacterium saccharolyticum (TsPYK) has previously been used in metabolic engineering for improved ethanol production. This isozyme belongs to a subclass of PYK isozymes that include an extra C-domain. Like other isozymes that include this extra C-domain, we found that TsPYK is activated by AMP and ribose-5-phosphate (R5P). Our use of sugar-phosphate analogues generated a surprising result in that IMP and GMP are allosteric inhibitors (rather than activators) of TsPYK. We believe this to be the first report of any PYK isozyme being inhibited by IMP and GMP. A truncated protein that lacks the extra C-domain is also inhibited by IMP. A screen of several other bacterial PYK enzymes (include several that have the extra-C domain) indicates that the inhibition by IMP is specific to only a subset of those isozymes.

  • Methods for Metabolic Engineering of Thermoanaerobacterium saccharolyticum.
    Methods in molecular biology (Clifton N.J.), 2020
    Co-Authors: Shuen Hon, Lee R Lynd, Tianyong Zheng, Jingxuan Cui, Liang Tian, Daniel G. Olson
    Abstract:

    In this work, we describe genetic tools and techniques for engineering Thermoanaerobacterium saccharolyticum. In particular, the T. saccharolyticum transformation protocol and the methods for selecting for transformants are described. Methods for determining strain phenotypes are also presented.

  • Conversion of phosphoenolpyruvate to pyruvate in Thermoanaerobacterium saccharolyticum.
    Metabolic engineering communications, 2020
    Co-Authors: Jingxuan Cui, Daniel G. Olson, Marybeth Maloney, Lee R Lynd
    Abstract:

    Thermoanaerobacterium saccharolyticum is an anaerobic thermophile that can ferment hemicellulose to produce biofuels, such as ethanol. It has been engineered to produce ethanol at high yield and titer. T. saccharolyticum uses the Embden-Meyerhof-Parnas (EMP) pathway for glycolysis. However, the genes and enzymes used in each step of the EMP pathway in T. saccharolyticum are not completely known. In T. saccharolyticum, both pyruvate kinase (PYK) and pyruvate phosphate dikinase (PPDK) are highly expressed based on transcriptomic and proteomic data. Both enzymes catalyze the formation of pyruvate from phosphoenolpyruvate (PEP). PYK is typically the last step of EMP glycolysis pathway while PPDK is reversible and is found mostly in C4 plants and some microorganisms. It is not clear what role PYK and PPDK play in T. saccharolyticum metabolism and fermentation pathways and whether both are necessary. In this study we deleted the ppdk gene in wild type and homoethanologen strains of T. saccharolyticum and showed that it is not essential for growth or ethanol production.

  • The ethanol pathway from Thermoanaerobacterium saccharolyticum improves ethanol production in Clostridium thermocellum.
    Metabolic engineering, 2017
    Co-Authors: Shuen Hon, Tianyong Zheng, Daniel G. Olson, Evert K. Holwerda, Marybeth Maloney, Adam M. Guss, Sean Jean-loup Murphy, Anthony A. Lanahan, Beth Papanek, Lee R Lynd
    Abstract:

    Clostridium thermocellum ferments cellulose, is a promising candidate for ethanol production from cellulosic biomass, and has been the focus of studies aimed at improving ethanol yield. Thermoanaerobacterium saccharolyticum ferments hemicellulose, but not cellulose, and has been engineered to produce ethanol at high yield and titer. Recent research has led to the identification of four genes in T. saccharolyticum involved in ethanol production: adhE, nfnA, nfnB and adhA. We introduced these genes into C. thermocellum and observed significant improvements to ethanol yield, titer, and productivity. The four genes alone, however, were insufficient to achieve in C. thermocellum the ethanol yields and titers observed in engineered T. saccharolyticum strains, even when combined with gene deletions targeting hydrogen production. This suggests that other parts of T. saccharolyticum metabolism may also be necessary to reproduce the high ethanol yield and titer phenotype in C. thermocellum.

Juergen Wiegel - One of the best experts on this subject based on the ideXlab platform.

  • Crystallization and preliminary X-ray diffraction analysis of a novel GH120 β-xylosidase (XylC) from Thermoanaerobacterium saccharolyticum JW/SL-YS485.
    Acta Crystallographica Section F Structural Biology and Crystallization Communications, 2012
    Co-Authors: Wenting Liu, Juergen Wiegel, Wei-lan Shao, Yu Sun, Rey-ting Guo, Chun-hsiang Huang
    Abstract:

    Xylosidases hydrolyze xylopolymers at the nonreducing end to free xylose units. The β-xylosidase (XylC) from Thermoanaerobacterium saccharolyticum JW/SL-­YS485 was expressed in Escherichia coli and the recombinant protein was purified and crystallized. A BLASTP search with the XylC protein sequence showed that no similar structure had previously been solved. XylC was classified as a member of the new glycoside hydrolase family GH120 according to the CAZy website (http://www.cazy.org/). Crystals belonging to the monoclinic space group P21, with unit-cell parameters a = 88.36, b = 202.20, c = 99.87 A, β = 99.04°, were obtained by the sitting-drop vapour-diffusion method and diffracted to 2.2 A resolution. Structure determination using MIR and MAD methods is in progress.

  • Description of Caldanaerobius fijiensis gen. nov., sp. nov., an inulin-degrading, ethanol-producing, thermophilic bacterium from a Fijian hot spring sediment, and reclassification of Thermoanaerobacterium polysaccharolyticum and Thermoanaerobacterium
    INTERNATIONAL JOURNAL OF SYSTEMATIC AND EVOLUTIONARY MICROBIOLOGY, 2008
    Co-Authors: Yongjin Lee, Roderick I. Mackie, Isaac K. O. Cann, Juergen Wiegel
    Abstract:

    An obligately anaerobic, spore-forming, Gram-type-positive but Gram-staining-negative thermophilic bacterium, strain JW/YJL-F3(T), was isolated from a Fijian hot spring sediment sample. Cells of strain JW/YJL-F3(T) were straight to slightly curved rods, 0.5-1.2 microm in diameter and 1.5-19 microm long. The temperature range for growth was between 40 and 67 degrees C, with an optimum at 60-63 degrees C. The pH(25 degrees C) range for growth was 4.5-8.4 with an optimum of 6.8. The salinity range for growth was 0-0.5 %. Strain JW/YJL-F3(T) utilized a range of substrates including arabinose, cellobiose, galactose, glucose, inulin, lactose, maltose, mannose, raffinose, ribose, trehalose, xylose and yeast extract as carbon and energy sources. The major fermentation end products from glucose were ethanol, acetate and formate. Strain JW/YJL-F3(T) converted thiosulfate to elemental sulfur, producing sulfur globules. The DNA G+C content was 37.6 mol% as determined by HPLC. Phylogenetic analysis using the 16S rRNA gene sequence indicated that the isolate is distantly related to the clade of the genus Thermoanaerobacterium. However, Thermoanaerobacterium polysaccharolyticum (96.7 % similarity to the type strain) and Thermoanaerobacterium zeae were the closest relatives, forming a separate, well-supported clade together with the novel isolate. Because Thermoanaerobacterium polysaccharolyticum, Thermoanaerobacterium zeae and strain JW/YJL-F3(T) have different features from other Thermoanaerobacterium species, including a higher G+C content and formate production, and are placed distantly from the remaining species of Thermoanaerobacterium (greater than 10 % distance) in the 16S rRNA gene sequence analysis, we propose to place the new isolate JW/YJL-F3(T) and Thermoanaerobacterium polysaccharolyticum and Thermoanaerobacterium zeae into the novel genus Caldanaerobius gen. nov. as Caldanaerobius fijiensis gen. nov., sp. nov. (the type species), Caldanaerobius polysaccharolyticus comb. nov. and Caldanaerobius zeae comb. nov., respectively. The type strain of Caldanaerobius fijiensis is JW/YJL-F3(T) (=ATCC BAA-1278(T) =DSM 17918(T)).

  • In situ analysis of sulfur species in sulfur globules produced from thiosulfate by Thermoanaerobacter sulfurigignens and Thermoanaerobacterium thermosulfurigenes.
    Journal of bacteriology, 2007
    Co-Authors: Yongjin Lee, Manfred Rohde, Mona Dashti, Alexander Prange, Henning Lichtenberg, Juergen Wiegel
    Abstract:

    The Firmicutes Thermoanaerobacter sulfurigignens and Thermoanaerobacterium thermosulfurigenes convert thiosulfate, forming sulfur globules inside and outside cells. X-ray absorption near-edge structure analysis revealed that the sulfur consisted mainly of sulfur chains with organic end groups similar to sulfur formed in purple sulfur bacteria, suggesting the possibility that the process of sulfur globule formation by bacteria is an ancient feature.

  • Thermoanaerobacterium aciditolerans sp. nov., a moderate thermoacidophile from a Kamchatka hot spring.
    International Journal of Systematic and Evolutionary Microbiology, 2007
    Co-Authors: Ilya V. Kublanov, Juergen Wiegel, Maria I. Prokofeva, Nadezhda A. Kostrikina, Tatyana V. Kolganova, Tatyana P. Tourova, Elizaveta A. Bonch-osmolovskaya
    Abstract:

    An anaerobic, moderately thermoacidophilic bacterium, strain 761-119T, was isolated from an acidic hot spring in the Orange Field of the Uzon Caldera (Kamchatka, far-eastern Russia). Cells were spore-forming, Gram-positive rods, possessing one polar flagellum. Growth of strain 761-119T was observed between 37 and 68 °C and in the pH20 °C range 3.2–7.1. No growth was observed within 5 days of incubation at or below 35 °C and at or above 70 °C, as well as at or below pH20 °C 2.8 and at or above pH20 °C 7.5. The optimal temperature and pH20 °C for growth were 55 °C and pH20 °C 5.7, respectively. A wide range of carbohydrates and polysaccharides were fermented, as well as peptides and proteinaceous substrates. The main products of glucose fermentation were acetate, ethanol, lactate, H2 and CO2. The DNA G+C content was 34 (±0.5) mol%. 16S rRNA gene sequence analysis indicated that strain 761-119T belonged to the genus Thermoanaerobacterium. The level of 16S rRNA gene sequence similarity with other Thermoanaerobacterium species was 86.5–97.8 %, with the only moderately acidophilic member of this genus, Thermoanaerobacterium aotearoense, being one of its closest relatives. DNA–DNA hybridization with T. aotearoense showed 33 % relatedness. Thus, morphological (one polar flagellum) and physiological characteristics (lower pH limit of growth at pH20 °C 3.2 compared with T. aotearoense) and 16S rRNA gene sequence analyses revealed that strain 761-119T represents a novel species in the genus Thermoanaerobacterium, for which the name Thermoanaerobacterium aciditolerans sp. nov. is proposed, with the type strain 761-119T (=DSM 16487T=VKM B-2363T).

  • Transformation of Thermoanaerobacterium sp. strain JW/SL‐YS485 with plasmid pIKM1 conferring kanamycin resistance
    FEMS Microbiology Letters, 2006
    Co-Authors: Volker Mai, W. Walter Lorenz, Juergen Wiegel
    Abstract:

    The industrial application of thermophilic (eu)bacteria is hampered by the lack of genetic systems for these bacteria. We report here the first unequivocal transformation of a Gram-positive, thermophilic, anaerobic microorganism, Thermoanaerobacterium, with the kanamycin resistance-mediating plasmid pIKM1. The construct pIKM1 is based on the Escherichia coli–Clostridium acetobutylicum shuttle vector pIMP1 and contains the thermostable kanamycin cassette from S. faecalis plasmid pKD102. Using electrotransformation, plasmid pIKM1 mediated kanamycin resistance in Thermoanaerobacterium sp. strain JW/SL-YS485 up to 400 μg ml−1 at 48°C and 200 μg ml−1 at 60°C.

J. G. Zeikus - One of the best experts on this subject based on the ideXlab platform.

  • Crystallization and preliminary X-ray crystallographic analysis of β-xylosidase from Thermoanaerobacterium saccharolyticum, a thermophilic anaerobe
    Acta Crystallographica Section D Biological Crystallography, 2002
    Co-Authors: Jin Kuk Yang, Hye-jin Yoon, Hyung Jun Ahn, Byung Il Lee, Maris Laivenieks, Claire Vieille, Hyung-wook Kim, J. G. Zeikus, Won Suh
    Abstract:

    β-Xylosidases are involved in the breakdown of xylans into xylose and belong to either family 39 or 43 of the glycosyl hydrolases. At present, no structural information is available for any member of these families. β-Xylosidase from the thermophilic anaerobe Thermoanaerobacterium saccharolyticum, a member of glycosyl hydrolase family 39, has been crystallized at 296 K using the hanging-drop vapour-diffusion method. The crystal diffracts to 2.4 A resolution with synchrotron X-rays and belongs to space group P41212 (or P43212), with unit-cell parameters a = b = 92.75, c = 241.37 A. The asymmetric unit contains two monomers of the recombinant enzyme, giving a corresponding VM of 2.21 A3 Da−1 and a solvent content of 44.3%.

  • Cloning and sequencing of the Thermoanaerobacterium saccharolyticum B6A-RI apu gene and purification and characterization of the amylopullulanase from Escherichia coli.
    Applied and environmental microbiology, 1994
    Co-Authors: M V Ramesh, S. E. Lowe, S M Podkovyrov, J. G. Zeikus
    Abstract:

    The amylopullulanase gene (apu) of the thermophilic anaerobic bacterium Thermoanaerobacterium saccharolyticum B6A-RI was cloned into Escherichia coli. The complete nucleotide sequence of the gene was determined. It encoded a protein consisting of 1,288 amino acids with a signal peptide of 35 amino acids. The enzyme purified from E. coli was a monomer with an M(r) of 142,000 +/- 2,000 and had same the catalytic and thermal characteristics as the native glycoprotein from T. saccharolyticum B6A. Linear alignment and the hydrophobic cluster analysis were used to compare this amylopullulanase with other amylolytic enzymes. Both methods revealed strictly conserved amino acid residues among these enzymes, and it is proposed that Asp-594, Asp-700, and Glu-623 are a putative catalytic triad of the T. saccharolyticum B6A-RI amylopullulanase.

  • Thermal stabilization of xylose isomerase from Thermoanaerobacterium thermosulfurigenes
    Nature Biotechnology, 1993
    Co-Authors: Menghsiao Meng, M. Bagdasarian, J. G. Zeikus
    Abstract:

    The thermostability of D-xylose isomerase from Thermoanaerobacterium thermosulfurigenes was enhanced by site-directed substitutions of aromatic amino acids in the active site. This enhancement may be explained as the consequence of the reduction of the area of water-accessible hydrophobic surface. The kinetics of thermoinactivation of the enzyme in aqueous solution was also investigated, and we report that in addition to the well known divalent cations, the monovalent cation, K+, also protects the enzyme against thermoinactivation. The kinetic data suggest that the formation of incorrect conformations of the enzyme (“scrambled structure”) is the dominant factor governing the process of thermoinactivation at elevated temperature (80–90°C).

  • Cloning, sequencing and biochemical characterization of xylose isomerase from Thermoanaerobacterium saccharolyticum strain B6A-RI.
    Journal of General Microbiology, 1993
    Co-Authors: Yong-eok Lee, Matur. V. Ramesh, J. G. Zeikus
    Abstract:

    Summary: The xylose isomerase gene from Thermoanaerobacterium saccharolyticum strain B6A-RI was cloned by complementation using Escherichia coli xyl-5 mutant strain HB101. One positive clone was detected and the recombinant plasmid, pZXI6, was isolated. The clone contained the vector pUC18 and an insert fragment of 4.5 kb. The cloned xylose isomerase gene (xylA) was expressed constitutively in E. coli. The gene contained one open reading frame (ORF) of 1317 bp, which corresponds to 439 amino acid residues. The molecular mass of the gene product was calculated to be 50474 Da from the deduced amino acid sequence. A putative promoter region (Pribnow box), TATAATATATAAT, which repeated twice at the −10 region in E. coli, was found 25 bp upstream of the ribosomal binding site. The deduced amino acid sequence of T. saccharolyticum strain B6A-RI xylose isomerase exhibited very high homology to those from Thermoanaerobacterium thermosulfurigenes 4B (formerly Clostridium thermosulfurogenes 4B) and Thermoanaerobacter ethanolicus 39E (formerly Clostridium thermohydrosulfuricum 39E). Codon usage in xynA, xynB and xylA showed a clear propensity for AT-containing isocodons. The native molecular mass of the purified recombinant thermostable xylose isomerase was 200 kDa, and the enzyme was a tetramer comprised of identical subunits. The apparent temperature and pH optima for activity of the cloned xylose isomerase were 80 °C and 7.0 to 7.5, respectively.

  • Cloning, sequencing and biochemical characterization of xylose isomerase from Thermoanaerobacterium saccharolyticum strain B6A-RI.
    Journal of general microbiology, 1993
    Co-Authors: Y E Lee, Matur. V. Ramesh, J. G. Zeikus
    Abstract:

    The xylose isomerase gene from Thermoanaerobacterium saccharolyticum strain B6A-RI was cloned by complementation using Escherichia coli xyl-5 mutant strain HB101. One positive clone was detected and the recombinant plasmid, pZX16, was isolated. The clone contained the vector pUC18 and an insert fragment of 4.5 kb. The cloned xylose isomerase gene (xylA) was expressed constitutively in E. coli. The gene contained one open reading frame (ORF) of 1317 bp, which corresponds to 439 amino acid residues. The molecular mass of the gene product was calculated to be 50474 Da from the deduced amino acid sequence. A putative promoter region (Pribnow box), TATAATATATAAT, which repeated twice at the -10 region in E. coli, was found 25 bp upstream of the ribosomal binding site. The deduced amino acid sequence of T. saccharolyticum strain B6A-RI xylose isomerase exhibited very high homology to those from Thermoanaerobacterium thermosulfurigenes 4B (formerly Clostridium thermosulfurogenes 4B) and Thermoanaerobacter ethanolicus 39E (formerly Clostridium thermohydrosulfuricum 39E). Codon usage in xynA, xynB and xylA showed a clear propensity for AT-containing isocodons. The native molecular mass of the purified recombinant thermostable xylose isomerase was 200 kDa, and the enzyme was a tetramer comprised of identical subunits. The apparent temperature and pH optima for activity of the cloned xylose isomerase were 80 degrees C and 7.0 to 7.5, respectively.

Sompong O-thong - One of the best experts on this subject based on the ideXlab platform.

  • Draft genome sequence of Thermoanaerobacterium sp. strain PSU-2 isolated from thermophilic hydrogen producing reactor
    Genomics data, 2017
    Co-Authors: Sompong O-thong, Chonticha Mamimin, Poonsuk Prasertsan, Peerawat Khongkliang, Apinya Singkhala, Nilskare Birkeland
    Abstract:

    Thermoanaerobacterium sp. strain PSU-2 was isolated from thermophilic hydrogen producing reactor and subjected to draft genome sequencing on 454 pyrosequencing and annotated on RAST. The draft genome sequence of strain PSU-2 contains 2,552,497 bases with an estimated G + C content of 35.2%, 2555 CDS, 8 rRNAs and 57 tRNAs. The strain had a number of genes responsible for carbohydrates metabolic, amino acids and derivatives, and protein metabolism of 17.7%, 14.39% and 9.81%, respectively. Strain PSU-2 also had gene responsible for hydrogen biosynthesis as well as the genes related to Ni-Fe hydrogenase. Comparative genomic analysis indicates strain PSU-2 shares about 94% genome sequence similarity with Thermoanaerobacterium xylanolyticum LX-11. The nucleotide sequence of this draft genome was deposited into DDBJ/ENA/GenBank under the accession MSQD00000000.

  • Thermophilic hydrogen production from co-fermentation of palm oil mill effluent and decanter cake by Thermoanaerobacterium thermosaccharolyticum PSU-2
    International Journal of Hydrogen Energy, 2016
    Co-Authors: Chonticha Mamimin, Aminee Jehlee, Sittikorn Saelor, Poonsuk Prasertsan, Sompong O-thong
    Abstract:

    Co-fermentation of palm oil mill effluent (POME) for hydrogen production by Thermoanaerobacterium thermosaccharolyticum PSU-2 under thermophilic condition was investigated. Hydrogen production from co-fermentation POME with 5 g/L decanter cake and without was 2.6 and 1.7 L-H2/L-POME. Co-fermentation of POME with decanter cake enhanced hydrogen production. Tbm. thermosaccharolyticum PSU-2 augmentation at 20% v/v was found to be an efficient start-up strategy in continuous hydrogen production from co-fermentation of POME with decanter cake. Tbm. thermosaccharolyticum PSU-2 augmentation could suppress normal flora bacteria in POME and decanter cake. Hydrogen production of 7.2 L-H2/L-POME and hydrogen production rate of 18.1 mmol-H2/L/h was achieved from continuous hydrogen in long term operation. The soluble metabolites were dominated by acetic acid and butyric acid. Tbm. thermosaccharolyticum PSU-2 augmentation could use for control undesired bacteria in the hydrogen production system with flavored Thermoanaerobacterium sp. as dominant species.

  • Biohydrogen Production from Palm Oil Mill Effluent Pretreated by Chemical Methods Using Thermoanaerobacterium-Rich Sludge
    Iranica Journal of Energy and Environment, 2013
    Co-Authors: Poonsuk Prasertsan, Sompong O-thong
    Abstract:

    The effect of alkaline and acid pretreatment on solubilization of solid organic matter in palm oil mill effluent (POME) and hydrogen production by Thermoanaerobacterium-rich sludge was studied. Organic matter solubilization of alkaline and acid pretreatments were increased up to 28 and 15.7% of initial soluble COD in POME, respectively. That corresponds to carbohydrate solubilization of 41 and 32% of initial soluble carbohydrate in POME, respectively. A maximum hydrogen production yield of 4.6 l H /l-POME was achieved 2 from POME pretreated with 1.5% w/v NaOH, which was 3-fold greater than raw POME and 1-fold greater than POME pretreated with 1.5% w/v HCl. Optimum conditions for biohydrogen production from alkaline pretreated POME using Thermoanaerobacterium-rich sludge was found at initial pH 5.5 and temperature of 60°C, which gives a maximum hydrogen production yield of 5.2 l H /l-POME and increased 51% as compared to raw POME. 2 The biogas was mainly composed of hydrogen and carbon dioxide with the percentage of hydrogen ranging from 55-60% of biogas and free of methane. During the conversion of alkaline pretreated POME into hydrogen, the acetic and butyric acids were main by-products in the metabolism. The results showed that alkaline pretreatment is an effective pretreatment methods for enhancing the hydrogen production yield from POME. The use of Thermoanaerobacterium-rich sludge is promising for future engineering practice of biohydrogen production from alkaline pretreated POME.

  • Biohydrogen Production from Palm Oil Mill Effluent Pretreated by Chemical Methods Using Thermoanaerobacterium-Rich Sludge
    2013
    Co-Authors: Jiravut Seengenyoung, Poonsuk Prasertsan, Sompong O-thong
    Abstract:

    Abstract: The effect of alkaline and acid pretreatment on solubilization of solid organic matter in palm oil mill effluent (POME) and hydrogen production by Thermoanaerobacterium-rich sludge was studied. Organic matter solubilization of alkaline and acid pretreatments were increased up to 28 and 15.7 % of initial soluble COD in POME, respectively. That corresponds to carbohydrate solubilization of 41 and 32 % of initial soluble carbohydrate in POME, respectively. A maximum hydrogen production yield of 4.6 l H /l-POME was achieved2 from POME pretreated with 1.5 % w/v NaOH, which was 3-fold greater than raw POME and 1-fold greater than POME pretreated with 1.5 % w/v HCl. Optimum conditions for biohydrogen production from alkaline pretreated POME using Thermoanaerobacterium-rich sludge was found at initial pH 5.5 and temperature of 60°C, which gives a maximum hydrogen production yield of 5.2 l H /l-POME and increased 51 % as compared to raw POME.2 The biogas was mainly composed of hydrogen and carbon dioxide with the percentage of hydrogen ranging from 55-60 % of biogas and free of methane. During the conversion of alkaline pretreated POME into hydrogen, the acetic and butyric acids were main by-products in the metabolism. The results showed that alkaline pretreatment is an effective pretreatment methods for enhancing the hydrogen production yield from POME. The use of Thermoanaerobacterium-rich sludge is promising for future engineering practice of biohydroge

  • Simultaneous thermophilic hydrogen production and phenol removal from palm oil mill effluent by Thermoanaerobacterium-rich sludge
    International Journal of Hydrogen Energy, 2012
    Co-Authors: Chonticha Mamimin, Poonsuk Prasertsan, Piyapong Thongdumyu, Adilan Hniman, Tsuyoshi Imai, Sompong O-thong
    Abstract:

    Abstract Thermoanaerobacterium-rich sludge was used for hydrogen production and phenol removal from palm oil mill effluent (POME) in the presence of phenol concentration of 100–1000 mg/L. Thermoanaerobacterium-rich sludge yielded the most hydrogen of 4.2 L H2/L-POME with 65% phenol removal efficiency at 400 mg/L phenol. Butyric acid and acetic acid were the main metabolites. The effects of oil palm ash, NH4NO3 and iron concentration (Fe2+) on hydrogen production and phenol removal efficiency from POME by Thermoanaerobacterium-rich sludge was investigated using response surface methodology (RSM). The RSM results indicated that the presence of 0.2 g Fe2+/L, 0.3 g/L NH4NO3 and 20 g/L oil palm ash in POME could improved phenol removal efficiency, with predicted hydrogen production and phenol removal efficiency of 3.45 L H2/L-POME and 93%, respectively. In a confirmation experiment under optimized conditions highly reproducible results were obtained, with hydrogen production and phenol removal efficiency of 3.43 ± 0.12 L H2/L-POME and 92 ± 1.5%, respectively. Simultaneous hydrogen production and phenol removal efficiency in continuous stirred tank reactor at hydraulic retention time (HRT) of 1 and 2 days were 4.0 L H2/L-POME with 85% and 4.2 L H2/L-POME with 92%, respectively. Phenol degrading Thermoanaerobacterium-rich sludge comprised of Thermoanaerobacterium thermosaccharolyticum, Thermoanaerobacterium aciditolerans, Desulfotomaculum sp., Bacillus coagulans and Clostridium uzonii. Phenol degrading Thermoanaerobacterium-rich sludge has great potential to harvest hydrogen from phenol-containing wastewater.

Nanqi Ren - One of the best experts on this subject based on the ideXlab platform.

  • Bioaugmentation with Thermoanaerobacterium thermosaccharolyticum W16 to enhance thermophilic hydrogen production using corn stover hydrolysate
    International Journal of Hydrogen Energy, 2019
    Co-Authors: Kun Zhang, Guang-li Cao, Nanqi Ren
    Abstract:

    Abstract In the present work, with corn stover hydrolysate as the substrate, an efficient hydrogen-producing thermophile, Thermoanaerobacterium thermosaccharolyticum W16, was added to three kinds of seed sludge (rotten corn stover (RCS), cow dung compost (CDC), and sludge from anaerobic digestion (SAD)) to investigate the effect of bioaugmentation on thermophilic hydrogen production. Batch test results indicate that the bioaugmentation with a small amount of the strain T. thermosaccharolyticum W16 (5% of total microbes) increased the hydrogen yield to varying degrees (RCS: from 8.78 to 9.90 mmol H2/g utilized sugar; CDC: from 8.18 to 8.42 mmol H2/g utilized sugar; SAD: from 8.55 to 9.17 mmol H2/g utilized sugar). The bioaugmentation process also influenced the soluble metabolites composition towards more acetate and less butyrate production for RCS, and more acetate and less ethanol accumulation for SAD. Microbial community analysis indicates that Thermoanaerobacterium spp. and Clostridium spp. dominated microbial community in all situations and might be mainly responsible for thermophilic hydrogen generation. For RCS and SAD, the bioaugmentation obviously increased the relative abundance of the strain T. thermosaccharolyticum W16 in microbial community, which might be the main reason for the improvement of hydrogen production in these cases.

  • Simultaneous saccharification and fermentation of fungal pretreated cornstalk for hydrogen production using Thermoanaerobacterium thermosaccharolyticum W16.
    Bioresource technology, 2013
    Co-Authors: Lei Zhao, Wan-qian Guo, Guang-li Cao, Hong-yu Ren, Aijie Wang, Nanqi Ren
    Abstract:

    Abstract In this research, environmentally friendly fungal pretreatment was first adopted for deconstruction of cornstalk. Then the fungal-pretreated cornstalk was employed to produce hydrogen in simultaneous saccharification and fermentation (SSF) using crude enzyme from Trichoderma viride and Thermoanaerobacterium thermosaccharolyticum W16. The influence of various factors including substrate concentration, initial pH, and enzyme loading on hydrogen production were evaluated. The highest hydrogen yield of 89.3 ml/g-cornstalk was obtained with an initial pH 6.5, 0.75% substrate concentration, and 34 FPU/g cellulose. Compared the result with SSF of physical or chemical pretreated lignocellulosic materials, this research suggested an economic and efficient way for hydrogen production from lignocellulosic biomass.

  • Optimization of immobilization parameters of Thermoanaerobacterium thermosaccharolyticum W16 on a new carrier for enhanced hydrogen production
    RSC Advances, 2012
    Co-Authors: Lei Zhao, Guang-li Cao, Jing Yao, Hong-yu Ren, Nanqi Ren, Aijie Wang
    Abstract:

    A new biological carrier mycelia pellet was adopted for enhanced hydrogen production by Thermoanaerobacterium thermosaccharolyticum W16. Immobilization parameters were optimized by response surface methodology for achieving maximum hydrogen yield. To our best knowledge, this is the first report detailing the interaction of immobilization parameters of this bacterium on a mycelia pellet.

  • Statistical optimization of culture condition for enhanced hydrogen production by Thermoanaerobacterium thermosaccharolyticum W16.
    Bioresource technology, 2009
    Co-Authors: Guang-li Cao, Wan-qian Guo, Jing Yao, Nanqi Ren, Aijie Wang, Yujie Feng, Qingliang Zhao
    Abstract:

    The optimization of culture condition for enhanced hydrogen production by Thermoanaerobacterium thermosaccharolyticum W16 was conducted using statistical experimental design and analysis. Plackett-Burman design was first used to screen the most important variables influencing hydrogen production, and subsequently central composite design was adopted to investigate the optimum value of the selected factors for achieving maximum hydrogen yield. Experimental results showed that xylose, phosphate buffer, and yeast extract had significant influence on hydrogen production and the maximum hydrogen yield of 2.39 mol/mol xylose was predicted when the concentrations of xylose, phosphate buffer, and yeast extract were 12.24 g/L, 0.170 M, and 4.11 g/L, respectively. The results were further verified by repeated experiments under optimal conditions. The excellent correlation between predicted and measured values further confirmed the validity and practicability of this statistical optimum strategy.

  • Acid hydrolysis of corn stover for biohydrogen production using Thermoanaerobacterium thermosaccharolyticum W16
    International Journal of Hydrogen Energy, 2009
    Co-Authors: Guang-li Cao, Wan-qian Guo, Nanqi Ren, Aijie Wang, Yujie Feng, Duu-jong Lee, Bing-feng Liu, Qingliang Zhao
    Abstract:

    Abstract Lignocellulosic biomass, if properly hydrolyzed, can be an ideal feedstock for fermentative hydrogen production. This work considered the pretreatment of corn stover (CS) using a dilute acid hydrolysis process and studied its fermentability for hydrogen production by the strain Thermoanaerobacterium thermosaccharolyticum W16. The effects of sulfuric acid concentration and reaction time in the hydrolysis stage of the process were determined based on a 22 central composite experimental design with respect to maximum hydrogen productivity. The optimal hydrolysis conditions to yield the maximum quantity of hydrogen by W16 were 1.69% sulfuric acid and 117 min reaction time. At these conditions, the hydrogen yield was shown to be 3305 ml H2 L−1 medium, which corresponds to 2.24 mol H2 mol−1 sugar. The present results indicate the potential of using T. thermosaccharolyticum W16 for high-yield conversion of CS hemicellulose into bio-H2 integrated with acid hydrolysis.

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