Relevant bibliographies by topics / E1 endoglucanase

Academic literature on the topic 'E1 endoglucanase'

Author: Grafiati
Published: 4 June 2021
Last updated: 18 February 2022

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Journal articles on the topic "E1 endoglucanase"

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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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Sun, Ye, Jay J. Cheng, Michael E. Himmel, Christopher D. Skory, William S. Adney, Steven R. Thomas, Brent Tisserat, Yufuko Nishimura, and Yuri T. Yamamoto. "Expression and characterization of Acidothermus cellulolyticus E1 endoglucanase in transgenic duckweed Lemna minor 8627." Bioresource Technology 98, no. 15 (November 2007): 2866–72. http://dx.doi.org/10.1016/j.biortech.2006.09.055.

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Kingsbury, Nathaniel J., and Karen A. McDonald. "Quantitative Evaluation of E1 Endoglucanase Recovery from Tobacco Leaves Using the Vacuum Infiltration-Centrifugation Method." BioMed Research International 2014 (2014): 1–10. http://dx.doi.org/10.1155/2014/483596.

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As a production platform for recombinant proteins, plant leaf tissue has many advantages, but commercialization of this technology has been hindered by high recovery and purification costs. Vacuum infiltration-centrifugation (VI-C) is a technique to obtain extracellularly-targeted products from the apoplast wash fluid (AWF). Because of its selective recovery of secreted proteins without homogenizing the whole tissue, VI-C can potentially reduce downstream production costs. Lab scale experiments were conducted to quantitatively evaluate the VI-C method and compared to homogenization techniques in terms of product purity, concentration, and other desirable characteristics. From agroinfiltratedNicotiana benthamianaleaves, up to 81% of a truncated version of E1 endoglucanase fromAcidothermus cellulolyticuswas recovered with VI-C versus homogenate extraction, and average purity and concentration increases of 4.2-fold and 3.1-fold, respectively, were observed. Formulas were developed to predict recovery yields of secreted protein obtained by performing multiple rounds of VI-C on the same leaf tissue. From this, it was determined that three rounds of VI-C recovered 97% of the total active recombinant protein accessible to the VI-C procedure. The results suggest that AWF recovery is an efficient process that could reduce downstream processing steps and costs for plant-made recombinant proteins.
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Nieves, Rafael A., Yat-Chen Chou, Michael E. Himmel, and Steven R. Thomas. "Quantitation ofAcidothermus cellulolyticus E1 endoglucanase andThermomonospora fusca E3 exoglucanase using enzyme-linked immunosorbent assay (ELISA)." Applied Biochemistry and Biotechnology 51-52, no. 1 (September 1995): 211–23. http://dx.doi.org/10.1007/bf02933425.

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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." Applied Biochemistry and Biotechnology 137-140, no. 1-12 (April 2007): 207–19. http://dx.doi.org/10.1007/s12010-007-9053-3.

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Makenova, Aiganym T., Herman B. Scholthof, Erlan M. Ramankulov, and Shuga A. Manabayeva. "Transient expression of Acidothermus cellulolyticus endoglucanase E1 by a Tomato bushy stunt virus-based plant expression vector." Journal of Biotechnology 208 (August 2015): S29—S30. http://dx.doi.org/10.1016/j.jbiotec.2015.06.080.

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Dai, Ziyu, Brian S. Hooker, Ryan D. Quesenberry, and Steven R. Thomas. "Optimization of Acidothermus cellulolyticus Endoglucanase (E1) Production in Transgenic Tobacco Plants by Transcriptional, Post-transcription and Post-translational Modification." Transgenic Research 14, no. 5 (October 2005): 627–43. http://dx.doi.org/10.1007/s11248-005-5695-5.

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You-Ji, Hu, and David B. Wilson. "Cloning of Thermomonospora fusca genes coding for beta 1-4 endoglucanases E1, E2 and E5." Gene 71, no. 2 (November 1988): 331–37. http://dx.doi.org/10.1016/0378-1119(88)90050-9.

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Chung, Daehwan, Jenna Young, Minseok Cha, Roman Brunecky, Yannick J. Bomble, Michael E. Himmel, and Janet Westpheling. "Expression of the Acidothermus cellulolyticus E1 endoglucanase in Caldicellulosiruptor bescii enhances its ability to deconstruct crystalline cellulose." Biotechnology for Biofuels 8, no. 1 (August 13, 2015). http://dx.doi.org/10.1186/s13068-015-0296-x.

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Dissertations / Theses on the topic "E1 endoglucanase"

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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 "E1 endoglucanase"

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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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