Relevant bibliographies by topics / Acidothermus cellulolyticus

Academic literature on the topic 'Acidothermus cellulolyticus'

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Published: 4 June 2021
Last updated: 19 February 2022

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Journal articles on the topic "Acidothermus cellulolyticus"

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Shiang, Ming, James C. Linden, Ali Mohagheghi, Karel Grohmann, and Michael E. Himmel. "Regulation of cellulase synthesis in Acidothermus cellulolyticus." Biotechnology Progress 7, no. 4 (July 1991): 315–22. http://dx.doi.org/10.1021/bp00010a005.

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Baker, John O., William S. Adney, Rafael A. Nleves, Steven R. Thomas, David B. Wilson, and Michael E. Himmel. "A new thermostable endoglucanase,Acidothermus cellulolyticus E1." Applied Biochemistry and Biotechnology 45-46, no. 1 (March 1994): 245–56. http://dx.doi.org/10.1007/bf02941803.

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Barabote, Ravi D., Juanito V. Parales, Ying-Yi Guo, John M. Labavitch, Rebecca E. Parales, and Alison M. Berry. "Xyn10A, a Thermostable Endoxylanase from Acidothermus cellulolyticus 11B." Applied and Environmental Microbiology 76, no. 21 (September 17, 2010): 7363–66. http://dx.doi.org/10.1128/aem.01326-10.

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ABSTRACT We cloned and purified the major family 10 xylanase (Xyn10A) from Acidothermus cellulolyticus 11B. Xyn10A was active on oat spelt and birchwood xylans between 60°C and 100°C and between pH 4 and pH 8. The optimal activity was at 90°C and pH 6; specific activity and Km for oat spelt xylan were 350 μmol xylose produced min−1 mg of protein−1 and 0.53 mg ml−1, respectively. Based on xylan cleavage patterns, Xyn10A is an endoxylanase, and its half-life at 90°C was approximately 1.5 h in the presence of xylan.
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Joh, Lawrence D., Farzaneh Rezaei, Ravi D. Barabote, Juanito V. Parales, Rebecca E. Parales, Alison M. Berry, and Jean S. VanderGheynst. "Effects of phenolic monomers on growth of Acidothermus cellulolyticus." Biotechnology Progress 27, no. 1 (December 22, 2010): 23–31. http://dx.doi.org/10.1002/btpr.525.

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Adney, W. S., M. P. Tucker, R. A. Nieves, S. R. Thomas, and M. E. Himmel. "Low molecular weight thermostable ?-D-glucosidase from Acidothermus cellulolyticus." Biotechnology Letters 17, no. 1 (January 1995): 49–54. http://dx.doi.org/10.1007/bf00134195.

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Baker, John O., James R. McCarley, Rebecca Lovett, Ching-Hsing Yu, William S. Adney, Tauna R. Rignall, Todd B. Vinzant, Stephen R. Decker, Joshua Sakon, and Michael E. Himmel. "Catalytically Enhanced Endocellulase Cel5A from Acidothermus cellulolyticus." Applied Biochemistry and Biotechnology 121, no. 1-3 (2005): 0129–48. http://dx.doi.org/10.1385/abab:121:1-3:0129.

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Lindenmuth, Benjamin E., and Karen A. McDonald. "Production and characterization of Acidothermus cellulolyticus endoglucanase in Pichia pastoris." Protein Expression and Purification 77, no. 2 (June 2011): 153–58. http://dx.doi.org/10.1016/j.pep.2011.01.006.

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Zhang, Qing, Wei Zhang, Chaoyang Lin, Xiaoli Xu, and Zhicheng Shen. "Expression of an Acidothermus cellulolyticus endoglucanase in transgenic rice seeds." Protein Expression and Purification 82, no. 2 (April 2012): 279–83. http://dx.doi.org/10.1016/j.pep.2012.01.011.

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VanderGheynst, Jean S., Farzaneh Rezaei, Todd M. Dooley, and Alison M. Berry. "Switchgrass leaching requirements for solid-state fermentation by Acidothermus cellulolyticus." Biotechnology Progress 26, no. 3 (December 28, 2009): 622–26. http://dx.doi.org/10.1002/btpr.366.

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Brumm, Phillip, Phillip Brumm, Dan Xie, Dan Xie, Larry Allen, Larry Allen, David A. Mead, and David A. Mead. "Hydrolysis of Cellulose by Soluble Clostridium Thermocellum and Acidothermus Cellulolyticus Cellulases." Journal of Enzymes 1, no. 1 (April 26, 2018): 5–19. http://dx.doi.org/10.14302/issn.2690-4829.jen-18-2025.

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The goal of this work was to clone, express, characterize and assemble a set of soluble thermostablecellulases capable of significantly degrading cellulose. We successfully cloned, expressed, and purified eleven Clostridium thermocellum (Cthe) cellulases and eight Acidothermuscellulolyticus(Acel) cellulases. The performance of the nineteen enzymes was evaluated on crystalline (filter paper) and amorphous (PASC) cellulose. Hydrolysis products generated from these two substrates were converted to glucose using beta-glucosidase and the glucose formed was determined enzymatically. Ten of the eleven Cthe enzymes were highly active on amorphous cellulose. The individual enzymes all produced <10% reducing sugar equivalents from filter paper. Combinations of Cthe cellulases gave higher conversions, with the combination of CelE, CelI, CelG, and CelK converting 34% of the crystalline cellulose. All eight Acel cellulases showed endo-cellulase activity and were highly active on PASC. Only Acel_0615 produced more than 10% reducing sugar equivalents from filter paper, and a combination of six Acel cellulases produced 32% conversion. Acel_0617, a GH48 exo-cellulase, and Acel_0619, a GH12 endo-cellulase, synergistically stimulated cellulose degradation by the combination of Cthe cellulases to almost 80%. Addition of both Acel enzymes to the Cthe enzyme mix did not further stimulate hydrolysis. Cthe CelG and CelI stimulated cellulose degradation by the combination of Acel cellulases to 66%.
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Dissertations / Theses on the topic "Acidothermus cellulolyticus"

1

McKenzie, Belinda, and s9907915@student rmit edu au. "Heterologous expression of cellulase enzymes in transplastidic Nicotiana tabacum cv. Petit Havana." RMIT University. Applied Sciences, 2008. http://adt.lib.rmit.edu.au/adt/public/adt-VIT20080805.120923.

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Extensive research into enzyme-induced bio-conversion of lignocellulose to soluble sugars has been conducted and research continues in this area. Several approaches have been taken to attempt to alleviate the economic problems associated with utilisation of lignocellulose in fuel ethanol production. By expressing cellulase genes in planta, it is hoped that the cost of enzyme-mediated hydrolysis of cellulose to its soluble sugar monomers, will be reduced. Some accomplishments have been made in this area using nuclear genetic transformation (Abdeev et al., 2003; Abdeev et al., 2004; Austin-Phillips et al., 1999; Biswas et al., 2006; Dai et al., 2000a,b; Dai et al., 2005; Jin et al., 2003; Kawazu et al., 1999; Sakka et al., 2000; Ziegelhoffer et al., 1999; Ziegelhoffer et al., 2001; Ziegler et al., 2000), but more research is required to bring the levels of cellulase enzyme expression in plants to levels that will make the process economically competitive. Chloroplasts of N. tabacum were selected as a target for transformation for high level expression due to their extremely high rates of transcription and translation. These were transformed with two genes, the e1 gene from A. cellulolyticus, and the cbh1 gene from T. reesei. Further aims included the investigation of the effects of using different promoters, and the novel use of both nuclear and chloroplast-based expression in a single plant, on the level of protein production in the heterologous host. Heterologous expression of the cbh1 gene was not successful. This is thought to be due to toxicity of the protein in a prokaryotic environment. Future studies should focus on trying to avoid this toxicity by targeting of the chloroplast-expressed enzyme to specific tissues, such as the thylakoid membrane, for containment, creating a codon-optimised synthetic gene that better mimics the codon usage of the plant to be used for expression, or placing the expression under a reactive cascade that is only activated upon exposure to an external trigger. Heterologous expression of the full length gene for E1 from A. cellulolyticus was successful. Chloroplast homology vectors under the constitutive promoter Prrn, and the inducible promoter T7, were constructed and these were used to successfully transform N. tabacum cv. Petit Havana chloroplasts. Stable transgenic plants were produced and evaluated by a variety of means, with the heterologously expressed enzyme showing activity against the soluble substrate analogue MUC of up to 3122 ± 466 pmol 4-MU/mg TSP/min and an E1 accumulation level of up to 0.35% ± 0.06 of the total soluble protein. Lastly, chloroplast transformation was combined with nuclear transformation to create novel dual-transgenic plants simultaneously expressing E1 from both the nuclear and chloroplast genomes. The combination of these technologies was very successful, with the heterologously expressed enzyme showing activity against the soluble substrate analogue MUC of up to 35706 ± 955 pmol 4-MU/mg TSP/min and an E1 accumulation level of up to 4.78% ± 0.13 of the total soluble protein, and provides a new approach for increasing the accumulation levels of plant-produced cellulase enzymes.
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Chou, Hong-Li, and 周紘立. "Expression of Acidothermus cellulolyticus endoglucanase E1 in rice for efficient ethanol production." Thesis, 2008. http://ndltd.ncl.edu.tw/handle/12255932370662562120.

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Abstract:
碩士
國立嘉義大學
農業生物技術研究所
96
Use of lignocellulosic crops or agricultural residues, such as rice straw or corn stover, for ethanol production is not only economical (high energy output/input ratio) but also environment friendly (e.g. without extra CO2 emission or carbon neutral) to curtail our reliance on fossil oil and prevent global warming. The overall goal of this study is to develop rice as a bioreactor for large-scale production of cellulose hydrolytic enzymes and to improve rice straw as an efficient biomass feedstock. For enhanced hydrolysis of cellulose to glucose, the cellulose hydrolytic enzyme β-1,4-endoglucanase (E1) from the thermophilic bacteria Acidothermus cellulolyticus has been introduced into rice via Agrobacterium-mediated transformation method with the protein targeted to the apoplastic compartment. A total of 52 transgenic rice plants from 5 independent lines overexpressing the bacterial enzyme were obtained and the plants exhibited a normal phenotype and expressed the gene at varying levels. The enzyme activities in the highest expressing transgenic rice lines were about 20 fold higher than those of various transgenic plants obtained in previous studies and the protein amounts accounted for up to 6.1% of the total leaf soluble protein. SDS-PAGE, zymogram and HPLC analyses showed that the bacterial enzyme exhibits thermostability and substrate specificity. Thus, transgenic rice plants can effectively serve as a bioreactor for large scale production of the hydrolytic enzyme. In addition, expression of this important cellulose hydrolytic enzyme in rice can also serve the autohydrolytic function for efficient conversion of its cellulose to glucose.
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Book chapters on the topic "Acidothermus cellulolyticus"

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Hubbard, D. W., T. B. Co, P. P. N. Murthy, and R. Mandalam. "Modelling the Growth of Acidothermus cellulolyticus." In Advances in Bioprocess Engineering, 241–45. Dordrecht: Springer Netherlands, 1994. http://dx.doi.org/10.1007/978-94-017-0641-4_34.

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Baker, John O., James R. McCarley, Rebecca Lovett, Ching-Hsing Yu, William S. Adney, Tauna R. Rignall, Todd B. Vinzant, Stephen R. Decker, Joshua Sakon, and Michael E. Himmel. "Catalytically Enhanced Endocellulase CeI5A from Acidothermus cellulolyticus." In Twenty-Sixth Symposium on Biotechnology for Fuels and Chemicals, 129–48. Totowa, NJ: Humana Press, 2005. http://dx.doi.org/10.1007/978-1-59259-991-2_12.

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McCarter, Suzanne L., William S. Adney, Todd B. Vinzant, Edward Jennings, Fannie Posey Eddy, Stephen R. Decker, John O. Baker, Joshua Sakon, and Michael E. Himmel. "Exploration of Cellulose Surface-Binding Properties of Acidothermus cellulolyticus Cel5A by Site-Specific Mutagenesis." In Biotechnology for Fuels and Chemicals, 273–87. Totowa, NJ: Humana Press, 2002. http://dx.doi.org/10.1007/978-1-4612-0119-9_22.

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Teymouri, Farzaneh, Hasan Alizadeh, Lizbeth Laureano-Pérez, Bruce Dale, and Mariam Sticklen. "Effects of Ammonia Fiber Explosion Treatment on Activity of Endoglucanase from Acidothermus cellulolyticus in Transgenic Plant." In Proceedings of the Twenty-Fifth Symposium on Biotechnology for Fuels and Chemicals Held May 4–7, 2003, in Breckenridge, CO, 1183–91. Totowa, NJ: Humana Press, 2004. http://dx.doi.org/10.1007/978-1-59259-837-3_95.

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Ransom, Callista, Venkatesh Balan, Gadab Biswas, Bruce Dale, Elaine Crockett, and Mariam Sticklen. "Heterologous Acidothermus cellulolyticus 1,4-β-Endoglucanase E1 Produced Within the Corn Biomass Converts Corn Stover Into Glucose." In Applied Biochemistry and Biotecnology, 207–19. Totowa, NJ: Humana Press, 2007. http://dx.doi.org/10.1007/978-1-60327-181-3_20.

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