Relevant bibliographies by topics / Biocatalyst

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  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers
  6. Reports

Academic literature on the topic 'Biocatalyst'

Author: Grafiati
Published: 4 June 2021
Last updated: 6 September 2023

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Journal articles on the topic "Biocatalyst"

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Cebrián-García, Soledad, Alina Balu, Araceli García, and Rafael Luque. "Sol-Gel Immobilisation of Lipases: Towards Active and Stable Biocatalysts for the Esterification of Valeric Acid." Molecules 23, no. 9 (September 6, 2018): 2283. http://dx.doi.org/10.3390/molecules23092283.

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Alkyl esters are high added value products useful in a wide range of industrial sectors. A methodology based on a simple sol-gel approach (biosilicification) is herein proposed to encapsulate enzymes in order to design highly active and stable biocatalysts. Their performance was assessed through the optimization of valeric acid esterification evaluating the effect of different parameters (biocatalyst load, presence of water, reaction temperature and stirring rate) in different alcoholic media, and comparing two different methodologies: conventional heating and microwave irradiation. Ethyl valerate yields were in the 80–85% range under optimum conditions (15 min, 12% m/v biocatalyst, molar ratio 1:2 of valeric acid to alcohol). Comparatively, the biocatalysts were slightly deactivated under microwave irradiation due to enzyme denaturalisation. Biocatalyst reuse was attempted to prove that good reusability of these sol-gel immobilised enzymes could be achieved under conventional heating.
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Souza, Priscila M. P., Diego Carballares, Luciana R. B. Gonçalves, Roberto Fernandez-Lafuente, and Sueli Rodrigues. "Immobilization of Lipase B from Candida antarctica in Octyl-Vinyl Sulfone Agarose: Effect of the Enzyme-Support Interactions on Enzyme Activity, Specificity, Structure and Inactivation Pathway." International Journal of Molecular Sciences 23, no. 22 (November 17, 2022): 14268. http://dx.doi.org/10.3390/ijms232214268.

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Lipase B from Candida antarctica was immobilized on heterofunctional support octyl agarose activated with vinyl sulfone to prevent enzyme release under drastic conditions. Covalent attachment was established, but the blocking step using hexylamine, ethylenediamine or the amino acids glycine (Gly) and aspartic acid (Asp) altered the results. The activities were lower than those observed using the octyl biocatalyst, except when using ethylenediamine as blocking reagent and p-nitrophenol butyrate (pNPB) as substrate. The enzyme stability increased using these new biocatalysts at pH 7 and 9 using all blocking agents (much more significantly at pH 9), while it decreased at pH 5 except when using Gly as blocking agent. The stress inactivation of the biocatalysts decreased the enzyme activity versus three different substrates (pNPB, S-methyl mandelate and triacetin) in a relatively similar fashion. The tryptophane (Trp) fluorescence spectra were different for the biocatalysts, suggesting different enzyme conformations. However, the fluorescence spectra changes during the inactivation were not too different except for the biocatalyst blocked with Asp, suggesting that, except for this biocatalyst, the inactivation pathways may not be so different.
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Gong, Jixian, Tongtong Kong, Yuqiang Li, Qiujin Li, Zheng Li, and Jianfei Zhang. "Biodegradation of Microplastic Derived from Poly(ethylene terephthalate) with Bacterial Whole-Cell Biocatalysts." Polymers 10, no. 12 (November 30, 2018): 1326. http://dx.doi.org/10.3390/polym10121326.

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At present, the pollution of microplastic directly threatens ecology, food safety and even human health. Polyethylene terephthalate (PET) is one of the most common of microplastics. In this study, the micro-size PET particles were employed as analog of microplastic. The engineered strain, which can growth with PET as sole carbon source, was used as biocatalyst for biodegradation of PET particles. A combinatorial processing based on whole-cell biocatalysts was constructed for biodegradation of PET. Compared with enzymes, the products can be used by strain growth and do not accumulated in culture solution. Thus, feedback inhibition of products can be avoided. When PET was treated with the alkaline strain under high pH conditions, the product concentration was higher and the size of PET particles decreased dramatically than that of the biocatalyst under neutral conditions. This shows that the method of combined processing of alkali and organisms is more efficient for biodegradation of PET. The novel approach of combinatorial processing of PET based on whole-cell biocatalysis provides an attractive avenue for the biodegradation of micplastics.
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Ryan, Jonathon, Hayden Ferral-Smith, and Joshua Wilson. "Wastewater and Mixed Microbial Consortia: a metastudy analysis of Optimal Microbial Fuel Cell configuration." PAM Review Energy Science & Technology 5 (May 31, 2018): 22–36. http://dx.doi.org/10.5130/pamr.v5i0.1496.

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Microbial Fuel Cells (MFCs) are an area of increasing research for use as an alternative energy source, due to their ability to produce electricity while simultaneously treating organic waste. This meta-study determines the optimal MFC configuration for electricity production, through consideration of the biocatalyst and substrate used. This study focuses primarily on comparing the use of mixed microbial consortia to pure strains of biocatalyst, and the use of waste water in contrast to simple substrates such as; acetate, glucose, and lactate. The use of algae as a substrate, and as a biocatalyst, is also investigated. In this study, only single and dual chamber MFCs are compared, and power density standardised to anode surface area (mW/m2) is used as a metric to facilitate the comparison of different experimental setups. This meta-study shows that dual chamber MFCs, using simple substrates, when catalysed by mixed culture biocatalysts, produce greater power densities, than algae, and complex substrates, with average power densities of 280, 70 and 30 (mW/m2) observed respectively. In single chamber MFC configurations, mixed culture biocatalysts have been observed to yield approximately double the power output of pure culture biocatalysts.
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Molnár, Zsófia, Emese Farkas, Ágnes Lakó, Balázs Erdélyi, Wolfgang Kroutil, Beáta G. Vértessy, Csaba Paizs, and László Poppe. "Immobilized Whole-Cell Transaminase Biocatalysts for Continuous-Flow Kinetic Resolution of Amines." Catalysts 9, no. 5 (May 10, 2019): 438. http://dx.doi.org/10.3390/catal9050438.

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Immobilization of transaminases creates promising biocatalysts for production of chiral amines in batch or continuous-flow mode reactions. E. coli cells containing overexpressed transaminases of various selectivities and hollow silica microspheres as supporting agent were immobilized by an improved sol-gel process to produce immobilized transaminase biocatalysts with suitable stability and mechanical properties for continuous-flow applications. The immobilized cell-based transaminase biocatalyst proved to be durable and easy-to-use in kinetic resolution of four racemic amines 1a–d. The batch and continuous-flow mode kinetic resolutions with transaminase biocatalyst of opposite stereopreference provided access to both enantiomers of the corresponding amines. By using the most suitable immobilized transaminase biocatalysts, this study describes the first transaminase-based approach for the production of both pure enantiomers of 1-(3,4-dimethoxyphenyl)ethan-1-amine 1d.
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Szelwicka, Anna, Anna Wolny, Miroslawa Grymel, Sebastian Jurczyk, Slawomir Boncel, and Anna Chrobok. "Chemo-Enzymatic Baeyer–Villiger Oxidation Facilitated with Lipases Immobilized in the Supported Ionic Liquid Phase." Materials 14, no. 13 (June 22, 2021): 3443. http://dx.doi.org/10.3390/ma14133443.

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A novel method for chemo-enzymatic Baeyer–Villiger oxidation of cyclic ketones in the presence of supported ionic liquid-like phase biocatalyst was designed. In this work, multi-walled carbon nanotubes were applied as a support for ionic liquids which were anchored to nanotubes covalently by amide or imine bonds. Next, lipases B from Candida antarctica, Candida rugosa, or Aspergillus oryzae were immobilized on the prepared materials. The biocatalysts were characterized using various techniques, like thermogravimetry, IR spectroscopy, XPS, elemental analysis, and SEM-EDS microscopy. In the proposed approach, a biocatalyst consisting of a lipase as an active phase allowed the generation of peracid in situ from the corresponding precursor and a green oxidant–hydrogen peroxide. The activity and stability of the obtained biocatalysts in the model oxidation of 2-adamantanone were demonstrated. High conversion of substrate (92%) was achieved under favorable conditions (toluene: n-octanoic acid ratio 1:1 = v:v, 35% aq. H2O2 2 eq., 0.080 g of biocatalyst per 1 mmol of ketone at 20 °C, reaction time 4 h) with four reaction cycles without a drop in its activity. Our ‘properties-by-design’ approach is distinguished by its short reaction time at low temperature and higher thermal stability in comparison with other biocatalysts presented in the literature reports.
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He, Qiyang, Hao Shi, Huaxiang Gu, Gilda Naka, Huaihai Ding, Xun Li, Yu Zhang, Bo Hu, and Fei Wang. "Immobilization of Rhizopus oryzae LY6 onto Loofah Sponge as a Whole-Cell Biocatalyst for Biodiesel Production." BioResources 11, no. 1 (November 30, 2015): 850–60. http://dx.doi.org/10.15376/biores.11.1.850-860.

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Whole cell biocatalysts for biodiesel production have garnered significant attention in recent years, as they can help avoid the complex procedures of isolation, purification, and immobilization of extracellular lipase. Because of its renewability and biodegradability, loofah (Luffa cylindrica) sponge is an advantageous substitute for traditional biomass carriers in whole cell immobilization. Rhizopus oryzae mycelia can spontaneously attach onto loofah sponge particles (LSPs) during cell cultivation. The highest immobilized R. oryzae cells concentration can reach up to 1.40 g/1 g of LSPs. The effects of biocatalyst addition and water content on methanolysis for biodiesel production were investigated in this paper. The operational stability of glutaraldehyde-treated biocatalyst at 35 °C, using a 1:1 oil-to-methanol ratio, was assayed, revealing a 3.4-fold increase in half-life compared with the untreated biocatalyst. Under optimized conditions, the yield of methyl esters in the reaction mixture reached 82.2% to 92.2% in each cycle. These results suggested that loofah sponge is a potential fungi carrier for an immobilized whole-cell biocatalyst.
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Ripoll, Magdalena, Nicolás Soriano, Sofía Ibarburu, Malena Dalies, Ana Paula Mulet, and Lorena Betancor. "Bacteria-Polymer Composite Material for Glycerol Valorization." Polymers 15, no. 11 (May 30, 2023): 2514. http://dx.doi.org/10.3390/polym15112514.

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Bacterial immobilization is regarded as an enabling technology to improve the stability and reusability of biocatalysts. Natural polymers are often used as immobilization matrices but present certain drawbacks, such as biocatalyst leakage and loss of physical integrity upon utilization in bioprocesses. Herein, we prepared a hybrid polymeric matrix that included silica nanoparticles for the unprecedented immobilization of the industrially relevant Gluconobacter frateurii (Gfr). This biocatalyst can valorize glycerol, an abundant by-product of the biodiesel industry, into glyceric acid (GA) and dihydroxyacetone (DHA). Different concentrations of siliceous nanosized materials, such as biomimetic Si nanoparticles (SiNps) and montmorillonite (MT), were added to alginate. These hybrid materials were significantly more resistant by texture analysis and presented a more compact structure as seen by scanning electron microscopy. The preparation including 4% alginate with 4% SiNps proved to be the most resistant material, with a homogeneous distribution of the biocatalyst in the beads as seen by confocal microscopy using a fluorescent mutant of Gfr. It produced the highest amounts of GA and DHA and could be reused for up to eight consecutive 24 h reactions with no loss of physical integrity and negligible bacterial leakage. Overall, our results indicate a new approach to generating biocatalysts using hybrid biopolymer supports.
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Trawczyńska, Ilona. "Immobilization of permeabilized cells of baker’s yeast for decomposition of H2O2 by catalase." Polish Journal of Chemical Technology 21, no. 2 (June 1, 2019): 59–63. http://dx.doi.org/10.2478/pjct-2019-0021.

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Abstract Permeabilization is one of the effective tools, used to increase the accessibility of intracellular enzymes. Immobilization is one of the best approaches to reuse the enzyme. Present investigation use both techniques to obtain a biocatalyst with high catalase activity. At the beginning the isopropyl alcohol was used to permeabilize cells of baker’s yeast in order to maximize the catalase activity within the treated cells. Afterwards the permeabilized cells were immobilized in calcium alginate beads and this biocatalyst was used for the degradation of hydrogen peroxide to oxygen and water. The optimal sodium alginate concentration and cell mass concentration for immobilization process were determined. The temperature and pH for maximum decomposition of hydrogen peroxide were assigned and are 20°C and 7 respectively. Prepared biocatalyst allowed 3.35-times faster decomposition as compared to alginate beads with non permeabilized cells. The immobilized biocatalyst lost ca. 30% activity after ten cycles of repeated use in batch operations. Each cycles duration was 10 minutes. Permeabilization and subsequent immobilization of the yeast cells allowed them to be transformed into biocatalysts with an enhanced catalase activity, which can be successfully used to decompose hydrogen peroxide.
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Travalia, Beatriz Medeiros, Mercia Galvão, Alvaro Silva Lima, Cleide Mara Faria Soares, Narendra Narain, and Luciana Cristina Lins de Aquino Santana. "Effect of parameters on butyl butyrate synthesis using novel Aspergillus niger lipase as biocatalyst." Acta Scientiarum. Technology 40, no. 1 (July 1, 2018): 35999. http://dx.doi.org/10.4025/actascitechnol.v40i1.35999.

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A novel “green” Aspergillus niger lipase, obtained from the fermentation of pumpkin seeds, was used in a free form and encapsulated in sol-gel matri x in butyl butyrate (pineapple flavor) synthesis. Esterification reactions were performed with varying substrate molar ratio (butanol: butyric acid) ranging between 1:1 and 5:1; temperature between 30 and 60°C and biocatalyst mass between 0 and 1g, respectively, according to experimental design 23 with 6 axial and 3 central points. Maximum butyl butyrate production was obtained when substrate molar ratio (butanol:butyric acid) 3:1, temperature at 60°C and 0.5 g free or encapsulated lipase as biocatalyst, were used. Temperature was the most significant parameter for production with the two biocatalysts, indicating that higher rates mean greater compound synthesis. Response surface plots showed that higher butyl butyrate production may be obtained with higher temperature and molar ratio rates (butanol:butyric acid) and with lower rates of biocatalyst mass in reactions catalyzed by free or encapsulated lipase. Aspergillus niger lipase obtained from agro-industrial waste could be employed as biocatalyst in esterification reactions in the production of natural aroma as butyl butyrate.
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Dissertations / Theses on the topic "Biocatalyst"

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Al, Yaqoub Zakariya. "Biocatalyst development for biodesulfurization." Thesis, University of Manchester, 2013. https://www.research.manchester.ac.uk/portal/en/theses/biocatalyst-development-for-biodesulfurization(77967e83-b529-4f1a-b3f4-2e2607cb4f4f).html.

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All fossil fuels contain varying levels of sulfur compounds which are undesirable because they cause environmental pollution, corrosion, acid rain and lead to health problems. There is strict international legislation for the permissible levels of sulfur compounds in fossil fuels. The aim of this research therefore was the biocatalyst development for biodesulfurisation using two approaches. In the first approach, Rhodococcus erythropolis IGTS8-5 and IGTS8-5G were immobilised in porous coke particles and tested in repeated cycles successfully. Both bacterial strains grew well in the chemically defined medium with glucose as the main carbon and energy source and the model sulfur compound dibenzothiophene (DBT) as the sole sulfur source. 0.8 g of cells was immobilized on 250 g of coke particles without refreshing the medium over 72 h while 1.8 g of cells were immobilised on 250 g of coke when the media was refreshed every 24 hours for 120 h after the initial immobilisation batch of 72h. The latter, were used repeatedly in twelve consequtive batch desulfurisation cycles during which the biodesulfurisation activity progressively decreased from over 95% removal of 100 ppm DBT to around 45% removal. DBT removal is often expressed in terms of 2-hydroxybiphenyl which is the end product of biodesulfurisation. The biodesulfurisation activityof immobilised bacteria was equivalent to 310 umol 2-HBP h-1g-1 dry cell weight during the first hour. Freely suspended cells on the other hand exhibited biodesulfurisation activity equivalent to 91 umol 2-HBP h-1g-1 dry cell weight. Unfortunately, after the first 24 h, the activity of the immobilised cells decreased to 12 umol 2-HBP h-1g-1 dry cell weight. Use of plant cell cultures for biodesulfurisation is the other novel aspect of this work. Armoracia rusticana (horse radish) cell culture was chosen as the novel biocatalyst since this plant is a well known source of peroxidase enzyme which is involved in the biodesulfurisation metabolism according to the literature on bacterial biodesulfurisation. Arabidospsis thaliana (thale cress) was also used since its genome is completely sequenced and it is a model organism in genomics studies. Our results indicate that cell suspensions of both plants did show biodesulfurisation activity by reducing the level of sulfur compounds, mainly DBT and other three derivatives from both aqueous and oil phase. When compared to the bacteria, in terms of DBT consumption, the activity of A. rusticana was calculated as 55 umol DBT h-1 g-1 DCW and 65 umol DBT h-1 g-1 DCW for A. thaliana while in bacteria it was 91 umol DBT h-1 g-1 DCW for IGTS8-5 and 73 umol DBT h-1 g-1 DCW for IGTS8-5G. Transcriptomics analysis of the plant cell cultures after exposure to the DBT when compared to control cultures showed alterations in gene expression levels several of which were related to sulfur metabolism and transmembrane transporters of sulfate.
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Polyzos, Aris A. "Directed evolution of a sulfoxidation biocatalyst." [Gainesville, Fla.] : University of Florida, 2003. http://purl.fcla.edu/fcla/etd/UFE0000769.

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Chen, Allen Kuan-Liang Biotechnology &amp Biomolecular Sciences Faculty of Science UNSW. "Enhanced biocatalyst production for (R)-phenylacetylcarbinol synthesis." Awarded by:University of New South Wales. School of Biotechnology and Biomolecular Sciences, 2006. http://handle.unsw.edu.au/1959.4/32825.

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The enzymatic production of R-phenylacetylcarbinol (R-PAC), with either whole cells or partially purified pyruvate decarboxylase (PDC) as the biocatalyst, requires high PDC activity and an inexpensive source of pyruvate for an economical feasible biotransformation process. Microbial pyruvate produced by a vitamin auxotrophic strain of Candida glabrata was selected as a potential substrate for biotransformation. With an optimal thiamine concentration of 60 ??g/l, a pyruvic acid concentration of 43 g/l and yield of 0.42 g/g glucose consumed were obtained. Using microbially-produced unpurified pyruvate resulted in similar PAC concentrations to those with commercial pure substrate confirming its potential for enzymatic PAC production. To obtain high activity yeast PDC, Candida utilis was cultivated in a controlled bioreactor. Optimal conditions for PDC production were identified as: fermentative cell growth at initial pH at 6.0 followed by pH downshift to 3.0. Average specific PDC carboligase activity of 392 ?? 20 U/g DCW was achieved representing a 2.7-fold increase when compared to a constant pH process. A mechanism was proposed in which the cells adapted to the pH decrease by increasing PDC activity to convert the accumulated internal pyruvic acid via acetaldehyde to ethanol thereby reducing intracellular acidification. The effect of pH shift on specific PDC activity of Saccharomyces cerevisiae achieved a comparable increase of specific PDC carboligase activity to 335 U/g DCW. The effect of pyruvic acid at pH 3.0 on induction of PDC activity was confirmed by cultivation at pH 3 with added pyruvic acid. Using microarray techniques, genome-wide transcriptional analyses of the effect of pH shift on S. cerevisiae revealed a transient increased expression of PDC1 after pH shift, which corresponded to the increase in specific PDC activity (although the latter was sustained for a longer period). The results showed significant gene responses to the pH shift with approximately 39 % of the yeast genome involved. The induced transcriptional responses to the pH shift were distinctive and showed only limited resemblance to gene responses reported for other environmental stress conditions, namely increased temperature, oxidative conditions, reduced pH (succinic acid), alkaline pH and increased osmolarity.
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Castro, H. F. de. "Biocatalyst and substrate properties for alcohol production." Thesis, University of Manchester, 1985. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.370410.

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Parker, B. M. "Directed evolution of an L-aminoacylase biocatalyst." Thesis, University College London (University of London), 2009. http://discovery.ucl.ac.uk/18724/.

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Enzymes from extreme environments possess highly desirable traits of activity and stability under process conditions. One such example is L-aminoacylase (E.C. Number 3.5.1.14) from the thermophilic archaeon Thermococcus litoralis (TliACY), which catalyzes the hydrolysis of the amide bond between the nitrogen and the carbonyl group of an N-protected L-amino acid. As this reaction is enantiomerspecific, L-aminoacylase is often used to resolve racemic mixtures in the preparation of chiral intermediates. Using protein engineering techniques, the capabilities of such biocatalysts can be extended. This thesis seeks to compare the ability of libraries created by error-prone PCR and structure-guided mutagenesis methods to identify residues governing substrate specificity. Libraries were constructed to screen for variants which showed a shift in substrate specificity towards aliphatic amino acids, whilst maintaining the preferred benzoyl protecting group. An existing fluorescent screen for proteases was adapted for the high-throughput screening of mutant L-aminoacylase libraries, and was demonstrated to be capable of quantitatively detecting millimolar quantities of product. From an error-prone PCR library over the dimerization region of the enzyme, 10000 variants were screened against a variety of N-benzoylated amino acid substrates. Sequence alignment and homology model construction allowed a 3-D model of TliACY to be built from its closest neighbours in the PDB. Phylogenetic comparison methods were used to identify regions and residues of significance, which were then examined using sitedirected saturation mutagenesis. Purification and characterisation of selected variants of TliACY examined two mutants in detail: S4C (S100T / M106K) which exhibited a 300% improvement in catalytic efficiency over wild-type on the Nbenzoyl valine substrate, and S3B (F251K) which showed a shift in substrate preference against aliphatic amino acid substrates.
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Murphy, Tracey L. "Developing a novel biocatalyst : N-acetylamino acid racemase." Thesis, Georgia Institute of Technology, 2002. http://hdl.handle.net/1853/32832.

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Reiche, Alison. "Biocatalyst Selection for a Glycerol-oxidizing Microbial Fuel Cell." Thèse, Université d'Ottawa / University of Ottawa, 2012. http://hdl.handle.net/10393/22764.

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Using glycerol from biodiesel production as a fuel in a microbial fuel cell (MFC) will generate electricity and valuable by-products from what is currently considered waste. This research aims to screen E. coli (W3110, TG1, DH5, BL21), P. freudenreichii (subspecies freudenreichii and shermanii), and mixed cultures enriched from compost (AR1, AR2, AR3) as anodic biocatalysts in a glycerol-oxidizing MFC. Anaerobic fermentation experiments were performed to determine the oxidative capacity of each catalyst towards glycerol. Using an optimized medium for each strain, the highest anaerobic glycerol conversion from each group was achieved by E. coli W3110 (4.1 g/L), P. freudenreichii ssp. shermanii (10 g/L), and AR2 (20 g/L). These cultures were then tested in an MFC system. All three catalysts exhibited exoelectrogenicity. The highest power density was achieved using P. freudenreichii ssp. shermanii (14.9 mW m-2), followed by AR2 (11.7 mW m-2), and finally E. coli W3110 (9.8 mW m-2).
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Snell, David Alfred. "The application of Rhodococcus sp. AJ270 as a biocatalyst." Thesis, University of Sunderland, 1998. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.285282.

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Binti, Suhaili Nurashikin. "Characterisation of biocatalyst production within an integrated biorefinery context." Thesis, University College London (University of London), 2017. http://discovery.ucl.ac.uk/10037553/.

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With the emerging interest in integrated biorefinery concepts, there is a need to identify and develop profitable product streams and ensure the utilisation of as many waste streams as possible. Early stage bioprocess development for these processes can be facilitated by the use of high throughput bioreactor platforms that enables rapid, quantitative and scalable data acquisition. This thesis aims to establish high throughput methodologies for the production and characterisation of industrial biocatalysts within an integrated biorefinery context. Specifically, the work focuses on the production of the CV2025 ω-Transaminase (CV2025 ω-TAm) in Escherichia coli BL21 (DE3) using sugar beet vinasse, a bioethanol waste stream, as a fermentation feedstock. The high throughput platform to be explored is a 24-well, controlled microbioreactor (MBR) that provides individual monitoring and control of process parameters at the well level. Initially, batch E. coli BL21 (DE3) fermentations expressing CV2025 ω-TAm were established in the controlled MBR using a synthetic medium to provide benchmark data on cell growth and enzyme expression. These cultures indicated a good degree of monitoring and control with respect to process parameters as well as culture reproducibility across the wells. Significant enhancements in relation to maximum biomass concentration (Xmax), yield of biomass on substrate (YX/S) and CV2025 ω-TAm specific activity of 3.7, 1.9 and 2.2-fold, respectively, were shown in the MBR compared to conventional shake flask system, also representing a 31-fold volumetric reduction. Optimisation of CV2025 ω-TAm production in the MBR showed that the best cell growth and enzyme titre was achieved with an early induction (6 h), 0.1 mM IPTG and 0.024 mmol IPTG gdcw-1, yielding enhancements in Xmax, YX/S and CV2025 ω-TAm specific activity of 1.04, 1.2 and 1.4-fold, respectively over the non-optimised cultures. Control of dissolved oxygen (DO) levels between 30 - 50% oxygen saturation had no significant impact on cell growth and CV2025 ω-TAm titre. Evaluation of vinasse as a fermentation feedstock for CV2025 ω-TAm production has led to several novel findings. Characterisation of vinasse showed that the feedstock comprised mainly of glycerol along with several reducing sugars, sugar alcohols, acetate, polyphenols and protein. Preliminary results showed E. coli BL21 (DE3) cell growth and CV2025 ω-TAm production were feasible in cultures using 17 to 25% (v/v) vinasse with higher concentrations demonstrating inhibitory effects. The D-galactose in vinasse was shown to facilitate auto-induction of the pQR801 plasmid leading to comparable CV2025 ω-TAm expression as obtained in IPTG-induced cultures. Assessment of different vinasse pre-processing options confirmed the relevance of the dilution step in reducing polyphenol concentrations to below inhibitory levels. Moreover, the use of pasteurised vinasse was found to be promising for large scale applications. Further medium optimisation studies in the MBR showed the benefit of supplementing vinasse with specific media components. Supplementation of diluted vinasse medium with 10 g L-1 yeast extract enabled enhancements of 2.8, 2.5, 5.4 and 3-fold in specific growth rate, Xmax, CV2025 ω-TAm volumetric and specific activity, respectively, over those achieved in non-supplemented cultures. Additionally, the CV2025 ω-TAm titre attained here represented 81% of that obtained using an optimised synthetic medium. Investigation into the metabolic preferences of E. coli BL21 (DE3) when grown on a complex carbon source like vinasse showed the sequential metabolism of D-mannitol before glycerol utilisation, which was followed by the simultaneous metabolism of glycerol, D-xylitol, D-dulcitol and acetate thereafter. Finally, scale-up of the optimal conditions for CV2025 ω-TAm production using both synthetic and vinasse-based media, from the controlled MBR to a 7.5 L stirred tank reactor (STR) was shown based on matched kLa values and specific aeration rates. Results showed a good reproducibility with respect to cell growth, substrate consumption and CV2025 ω-TAm production between the scales, representing a 769-fold volumetric scale translation. The feasibility of further intensification of CV2025 ω-TAm production in STR at higher kLa values using both synthetic and vinasse-based media was also demonstrated leading to enhancements of 1.4 and 1.9-fold in enzyme titre, respectively. Overall, this work has established high throughput methodologies for the characterisation, optimisation and scale-up of industrial biocatalyst production. The approach was demonstrated within the context of an integrated sugar beet biorefinery. However, the utility of the high throughput approach is considered generally applicable across the industrial biotechnology sector.
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Zhang, Jie. "Enantioselective reduction of carbonyl groups : biocatalyst discovery and cofactor recycling /." Zürich : ETH, 2006. http://e-collection.ethbib.ethz.ch/show?type=diss&nr=16810.

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Books on the topic "Biocatalyst"

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W, Crull Anna, Ruffio Patricia, and Business Communications Co, eds. Immobilized biocatalyst and bioreactant technology. Stamford, Conn., U.S.A: Business Communications Co., 1986.

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Himmel, Michael E., and George Georgiou, eds. Biocatalyst Design for Stability and Specificity. Washington, DC: American Chemical Society, 1993. http://dx.doi.org/10.1021/bk-1993-0516.

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Chemical Congress of North America (4th 1991 New York, N.Y.). Biocatalyst design for stability and specificity. Edited by Himmel Michael E, Georgiou George, American Chemical Society. Division of Biochemical Technology., and American Chemical Society Meeting. Washington, DC: American Chemical Society, 1993.

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1950-, Krohn Jacqueline, ed. A guide to the identification and treatment of biocatalyst and biochemical intolerances. 2nd ed. Los Alamos, NM: Los Alamos Medical Center, 1994.

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Yong, Yee Peng. Immobilised lipase biocatalyst in solvent-free medium: Immobilisation studies and enzymatic kinetics. Birmingham: University of Birmingham, 1998.

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Biocatalysis based on heme peroxidases: Peroxidases as potential industrial biocatalysts. New York: Springer-Verlag, 2010.

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Hartmeier, Winfried. Immobilized Biocatalysts. Berlin, Heidelberg: Springer Berlin Heidelberg, 1988. http://dx.doi.org/10.1007/978-3-642-73364-2.

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Bommarius, Andreas Sebastian. Biocatalysis. Weinheim: Wiley-VCH, 2004.

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Husain, Qayyum, and Mohammad Fahad Ullah, eds. Biocatalysis. Cham: Springer International Publishing, 2019. http://dx.doi.org/10.1007/978-3-030-25023-2.

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de Gonzalo, Gonzalo, and Pablo Domínguez de María, eds. Biocatalysis. Cambridge: Royal Society of Chemistry, 2017. http://dx.doi.org/10.1039/9781782629993.

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Book chapters on the topic "Biocatalyst"

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Lee, Jin Hyung, Soo Youn Lee, Zhi-Kang Xu, and Jeong Ho Chang. "Nanomaterial-Based Biocatalyst." In Nanocatalysis Synthesis and Applications, 615–41. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2013. http://dx.doi.org/10.1002/9781118609811.ch17.

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Powell, Lawson W. "Immobilized Biocatalyst Technology." In Microbial Enzymes and Biotechnology, 369–94. Dordrecht: Springer Netherlands, 1990. http://dx.doi.org/10.1007/978-94-009-0765-2_11.

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Tholey, Andreas, and Elmar Heinzle. "Methods for Biocatalyst Screening." In Tools and Applications of Biochemical Engineering Science, 1–19. Berlin, Heidelberg: Springer Berlin Heidelberg, 2002. http://dx.doi.org/10.1007/3-540-45736-4_1.

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Satyawali, Yamini, Ehiaze Augustine Ehimen, and Winnie Dejonghe. "Biocatalyst Recycling by Membrane Operations." In Encyclopedia of Membranes, 1–2. Berlin, Heidelberg: Springer Berlin Heidelberg, 2014. http://dx.doi.org/10.1007/978-3-642-40872-4_1981-1.

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Rolland-Fulcrand, Valérie, Robert Jacquier, René Lazaro, and Philippe Viallefont. "New supported biocatalyst for peptide synthesis." In Peptides, 615–16. Dordrecht: Springer Netherlands, 1992. http://dx.doi.org/10.1007/978-94-011-2264-1_244.

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Vargas, Marcos, Xochitl Niehus, Leticia Casas-Godoy, and Georgina Sandoval. "Lipases as Biocatalyst for Biodiesel Production." In Lipases and Phospholipases, 377–90. New York, NY: Springer New York, 2018. http://dx.doi.org/10.1007/978-1-4939-8672-9_21.

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Fan, Xiaohu, Xochitl Niehus, and Georgina Sandoval. "Lipases as Biocatalyst for Biodiesel Production." In Lipases and Phospholipases, 471–83. Totowa, NJ: Humana Press, 2012. http://dx.doi.org/10.1007/978-1-61779-600-5_27.

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Grewal, Jasneet, and Sunil K. Khare. "Lipases as Biocatalyst for Production of Biolubricants." In Environmentally Friendly and Biobased Lubricants, 187–203. Taylor & Francis Group, 6000 Broken Sound Parkway NW, Suite 300, Boca Raton, FL 33487-2742: CRC Press, 2016. http://dx.doi.org/10.1201/9781315373256-12.

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Thakur, Shilpi, Hardik Patel, Shilpa Gupte, and Akshaya Gupte. "Laccases: The Biocatalyst with Industrial and Biotechnological Applications." In Microorganisms in Sustainable Agriculture and Biotechnology, 309–42. Dordrecht: Springer Netherlands, 2011. http://dx.doi.org/10.1007/978-94-007-2214-9_16.

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Bosco, Francesca, Bernardo Ruggeri, and Guido Sassi. "Phanerochaete chrysosporium AS a Biocatalyst in Bioremediation Option." In Contaminated Soil ’95, 1159–60. Dordrecht: Springer Netherlands, 1995. http://dx.doi.org/10.1007/978-94-011-0421-0_53.

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Conference papers on the topic "Biocatalyst"

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Matveeva, Valentina, Ekaterina Golikova, Natalia Lakina, Alexandrina Sulman, Alexander Sidorov, Valentin Doluda, Alexey Yu Karpenkov, and Esther Sulman. "Magnetically separable biocatalyst of D-glucose oxidation." In RECENT ADVANCES ON ENVIRONMENT, CHEMICAL ENGINEERING AND MATERIALS. Author(s), 2018. http://dx.doi.org/10.1063/1.5060688.

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Zhang, Yong, Zhengzhong Mao, Shaoan Cheng, Miao Yu, Wei Wei, and Xinke Wu. "Model Construction of the Electric Methane Generation Based on Biocatalyst." In 2019 IEEE 3rd Conference on Energy Internet and Energy System Integration (EI2). IEEE, 2019. http://dx.doi.org/10.1109/ei247390.2019.9062096.

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Riadi, Lieke, Ruth Chrisnasari, Joshua Kristanto, Cahaya Caesar Bigravida, and Meyta Sanoe. "Immobilization of xylanase on acid pretreatment bentonite as green biocatalyst." In INTERNATIONAL CONFERENCE ON INFORMATICS, TECHNOLOGY, AND ENGINEERING 2021 (InCITE 2021): Leveraging Smart Engineering. AIP Publishing, 2022. http://dx.doi.org/10.1063/5.0080318.

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Dubrovskis, Vilis, and Dagnis Dubrovskis. "Methane production from briquettes of birch sawdust." In 22nd International Scientific Conference Engineering for Rural Development. Latvia University of Life Sciences and Technologies, Faculty of Engineering, 2023. http://dx.doi.org/10.22616/erdev.2023.22.tf124.

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Renewable energy sources have the potential to reduce emissions of GHG when compared to the combustion of fossil fuels and thereby to mitigate climate change. Bioenergy systems can contribute to climate change mitigation if they replace traditional fossil fuel use (IPCC, 2012). Latvia is also striving to achieve neutral emissions by 2030. Therefore, the use of renewable energy is supported. Wood waste maybe an important resource for biogas production. The biodegradability is however limited because of the recalcitrant nature of the biofibers (lignocellulosic biomass) it contains. More and more biogas plants used the pellets or briquettes from various residues as a raw material. Their advantage is not only cheaper transport over longer distances, but also they absorb moisture well and do not form a floating layer. Hydraulic retention time working with such raw materials as birch sawdust and briquettes is relatively long and requires large volumes of bioreactors. Variety of additives can be used to improve the anaerobic digestion process. This article shows the results, where the enzymes alpha amylase, xylanase and biocatalyst Metaferm are used for the digestion process of birch briquette improvement. Birch briquettes were digested in 0.75 l bioreactors at temperature 38 °C in a batch mode process. Two biorectors were for control purposes and contained inoculums only. Other 14 biorectors contained biomass substrates without or with added enzymes or biocatalyst. Average specific biogas or methane yield from anaerobic fermentation of birch briquettes was 0.427 L·g-1DOM or 0.178 L·g-1DOM respectively. Addition of enzymes and biocatalyst (1ml) in bioreactors with birch briquettes increases the average methane yield.
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Parra, Erika A., Adrienne Higa, Cullen R. Buie, John D. Coates, and Liwei Lin. "Real-time biocatalyst loading and electron transfer via microfabricated transparent electrode." In 2010 IEEE 23rd International Conference on Micro Electro Mechanical Systems (MEMS). IEEE, 2010. http://dx.doi.org/10.1109/memsys.2010.5442423.

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Sulman, Aleksandrina. "THE DESIGN OF MAGNETICALLY SEPARABLE BIOCATALYST ON THE BASIS OF GLUCOSE OXIDASE." In 19th SGEM International Multidisciplinary Scientific GeoConference EXPO Proceedings. STEF92 Technology, 2019. http://dx.doi.org/10.5593/sgem2019/4.1/s17.066.

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Yang, Jie, Sasan Ghobadian, Reza Montazami, and Nastaran Hashemi. "Using Shewanella Oneidensis MR1 as a Biocatalyst in a Microscale Microbial Fuel Cell." In ASME 2013 11th International Conference on Fuel Cell Science, Engineering and Technology collocated with the ASME 2013 Heat Transfer Summer Conference and the ASME 2013 7th International Conference on Energy Sustainability. American Society of Mechanical Engineers, 2013. http://dx.doi.org/10.1115/fuelcell2013-18373.

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Microbial fuel cell (MFC) technology is a promising area in the field of renewable energy because of their capability to use the energy contained in wastewater, which has been previously an untapped source of power. Microscale MFCs are desirable for their small footprints, relatively high power density, fast start-up, and environmentally-friendly process. Microbial fuel cells employ microorganisms as the biocatalysts instead of metal catalysts, which are widely applied in conventional fuel cells. MFCs are capable of generating electricity as long as nutrition is provided. Miniature MFCs have faster power generation recovery than macroscale MFCs. Additionally, since power generation density is affected by the surface-to-volume ratio, miniature MFCs can facilitate higher power density. We have designed and fabricated a microscale microbial fuel cell with a volume of 4 μL in a polydimethylsiloxane (PDMS) chamber. The anode and cathode chambers were separated by a proton exchange membrane. Carbon cloth was used for both the anode and the cathode. Shewanella Oneidensis MR-1 was chosen to be the electrogenic bacteria and was inoculated into the anode chamber. We employed Ferricyanide as the catholyte and introduced it into the cathode chamber with a constant flow rate of approximately 50 μL/hr. We used trypticase soy broth as the bacterial nutrition and added it into the anode chamber approximately every 15 hours once current dropped to base current. Using our miniature MFC, we were able to generate a maximum current of 4.62 μA.
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Yetti, Elvi, Amalia A’la, Nailul Luthfiyah, Hans Wijaya, Ahmad Thontowi, and Yopi. "Formulation of bacterial consortium as whole cell biocatalyst for degradation of oil compounds." In PROCEEDINGS OF THE 3RD INTERNATIONAL SYMPOSIUM ON APPLIED CHEMISTRY 2017. Author(s), 2017. http://dx.doi.org/10.1063/1.5011909.

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Hartanto, Tan Jeremy, Wideawati Nurjuwita, Mochammad Purwanto, Ashadi Sasongko, and Umi Sholikah. "Biogas production from tofu liquid waste with effective microorganisms biocatalyst in anaerobic digester." In THE 9TH INTERNATIONAL CONFERENCE OF THE INDONESIAN CHEMICAL SOCIETY ICICS 2021: Toward a Meaningful Society. AIP Publishing, 2022. http://dx.doi.org/10.1063/5.0104571.

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Yasuhara, H., K. Hayashi, and M. Okamura. "Evolution in Mechanical and Hydraulic Properties of Calcite-Cemented Sand Mediated by Biocatalyst." In Geo-Frontiers Congress 2011. Reston, VA: American Society of Civil Engineers, 2011. http://dx.doi.org/10.1061/41165(397)407.

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Reports on the topic "Biocatalyst"

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Suominen, Pirkko, David Glassner, and Robert Kean. Development of Biocatalyst for the Fermentation of Agricultural Feedstocks to Chemicals. Office of Scientific and Technical Information (OSTI), January 2005. http://dx.doi.org/10.2172/859231.

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Lalonde, James. Low-Cost Biocatalyst for Acceleration of Energy Efficient CO2 Capture Solvents. Office of Scientific and Technical Information (OSTI), August 2012. http://dx.doi.org/10.2172/1052141.

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Hwee, N. Methane Consuming Biocatalysts in Gas-Solid Reactor System. Office of Scientific and Technical Information (OSTI), June 2022. http://dx.doi.org/10.2172/1871393.

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Shanmugam, K. T., L. O. Ingram, J. A. Maupin-Furlow, J. F. Preston, and H. C. Aldrich. Thermophilic Gram-Positive Biocatalysts for Biomass Conversion to Ethanol. Office of Scientific and Technical Information (OSTI), December 2003. http://dx.doi.org/10.2172/882538.

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Baker, Sarah E., J. M. Knipe, J. Oakdale, and J. Stolaroff. Enzyme-Embedded, Microstructural Reactors for Industrial Biocatalysis. Office of Scientific and Technical Information (OSTI), October 2016. http://dx.doi.org/10.2172/1331441.

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Mercer-Smith, Janet. Smart Microbial Cell Technology: A high-throughput platform to optimize biocatalysts. Office of Scientific and Technical Information (OSTI), August 2020. http://dx.doi.org/10.2172/1648063.

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Karplus, Martin. Final progress report for DOE grant [Protein dynamics and biocatalysis]. Office of Scientific and Technical Information (OSTI), September 2001. http://dx.doi.org/10.2172/805789.

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DYER, RICHARD B. HYPERTHERMOPHILE BIOCATALYSIS: THE MOLECULAR BASIS OF ENZYME STABILITY AND ACTIVITY. Office of Scientific and Technical Information (OSTI), August 2002. http://dx.doi.org/10.2172/801271.

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Nghiem, NP. Continuous Ethanol Production Using Immobilized-Cell/Enzyme Biocatalysts in Fluidized-Bed Bioreactor (FBR). Office of Scientific and Technical Information (OSTI), November 2003. http://dx.doi.org/10.2172/885574.

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Hwee, N. Methane Remediation Using Biocatalysts in Batch Gas-Solid Mass Transfer System Challenges and Prospects. Office of Scientific and Technical Information (OSTI), February 2022. http://dx.doi.org/10.2172/1860693.

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