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      Potential use of sugar binding proteins in reactors for regeneration of CO 2 fixation acceptor D-Ribulose-1,5-bisphosphate

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          Abstract

          Sugar binding proteins and binders of intermediate sugar metabolites derived from microbes are increasingly being used as reagents in new and expanding areas of biotechnology. The fixation of carbon dioxide at emission source has recently emerged as a technology with potentially significant implications for environmental biotechnology. Carbon dioxide is fixed onto a five carbon sugar D-ribulose-1,5-bisphosphate. We present a review of enzymatic and non-enzymatic binding proteins, for 3-phosphoglycerate (3PGA), 3-phosphoglyceraldehyde (3PGAL), dihydroxyacetone phosphate (DHAP), xylulose-5-phosphate (X5P) and ribulose-1,5-bisphosphate (RuBP) which could be potentially used in reactors regenerating RuBP from 3PGA. A series of reactors combined in a linear fashion has been previously shown to convert 3-PGA, (the product of fixed CO 2 on RuBP as starting material) into RuBP (Bhattacharya et al., 2004; Bhattacharya, 2001). This was the basis for designing reactors harboring enzyme complexes/mixtures instead of linear combination of single-enzyme reactors for conversion of 3PGA into RuBP. Specific sugars in such enzyme-complex harboring reactors requires removal at key steps and fed to different reactors necessitating reversible sugar binders. In this review we present an account of existing microbial sugar binding proteins and their potential utility in these operations.

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          Most cited references136

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          Complete genome sequence of a multiple drug resistant Salmonella enterica serovar Typhi CT18.

          Salmonella enterica serovar Typhi (S. typhi) is the aetiological agent of typhoid fever, a serious invasive bacterial disease of humans with an annual global burden of approximately 16 million cases, leading to 600,000 fatalities. Many S. enterica serovars actively invade the mucosal surface of the intestine but are normally contained in healthy individuals by the local immune defence mechanisms. However, S. typhi has evolved the ability to spread to the deeper tissues of humans, including liver, spleen and bone marrow. Here we have sequenced the 4,809,037-base pair (bp) genome of a S. typhi (CT18) that is resistant to multiple drugs, revealing the presence of hundreds of insertions and deletions compared with the Escherichia coli genome, ranging in size from single genes to large islands. Notably, the genome sequence identifies over two hundred pseudogenes, several corresponding to genes that are known to contribute to virulence in Salmonella typhimurium. This genetic degradation may contribute to the human-restricted host range for S. typhi. CT18 harbours a 218,150-bp multiple-drug-resistance incH1 plasmid (pHCM1), and a 106,516-bp cryptic plasmid (pHCM2), which shows recent common ancestry with a virulence plasmid of Yersinia pestis.
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            Hydrogen from catalytic reforming of biomass-derived hydrocarbons in liquid water.

            Concerns about the depletion of fossil fuel reserves and the pollution caused by continuously increasing energy demands make hydrogen an attractive alternative energy source. Hydrogen is currently derived from nonrenewable natural gas and petroleum, but could in principle be generated from renewable resources such as biomass or water. However, efficient hydrogen production from water remains difficult and technologies for generating hydrogen from biomass, such as enzymatic decomposition of sugars, steam-reforming of bio-oils and gasification, suffer from low hydrogen production rates and/or complex processing requirements. Here we demonstrate that hydrogen can be produced from sugars and alcohols at temperatures near 500 K in a single-reactor aqueous-phase reforming process using a platinum-based catalyst. We are able to convert glucose -- which makes up the major energy reserves in plants and animals -- to hydrogen and gaseous alkanes, with hydrogen constituting 50% of the products. We find that the selectivity for hydrogen production increases when we use molecules that are more reduced than sugars, with ethylene glycol and methanol being almost completely converted into hydrogen and carbon dioxide. These findings suggest that catalytic aqueous-phase reforming might prove useful for the generation of hydrogen-rich fuel gas from carbohydrates extracted from renewable biomass and biomass waste streams.
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              BRENDA, the enzyme database: updates and major new developments.

              BRENDA (BRaunschweig ENzyme DAtabase) represents a comprehensive collection of enzyme and metabolic information, based on primary literature. The database contains data from at least 83,000 different enzymes from 9800 different organisms, classified in approximately 4200 EC numbers. BRENDA includes biochemical and molecular information on classification and nomenclature, reaction and specificity, functional parameters, occurrence, enzyme structure, application, engineering, stability, disease, isolation and preparation, links and literature references. The data are extracted and evaluated from approximately 46,000 references, which are linked to PubMed as long as the reference is cited in PubMed. In the past year BRENDA has undergone major changes including a large increase in updating speed with >50% of all data updated in 2002 or in the first half of 2003, the development of a new EC-tree browser, a taxonomy-tree browser, a chemical substructure search engine for ligand structure, the development of controlled vocabulary, an ontology for some information fields and a thesaurus for ligand names. The database is accessible free of charge to the academic community at http://www.brenda. uni-koeln.de.
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                Author and article information

                Journal
                Microb Cell Fact
                Microbial Cell Factories
                BioMed Central (London )
                1475-2859
                2004
                2 June 2004
                : 3
                : 7
                Affiliations
                [1 ]Department of Biotechnology, Haldia Institute of Technology, Haldia, West Bengal, India
                [2 ]Environmental Biotechnology Division, ABRD Company LLC, 1555 Wood Road, Cleveland, Ohio, 44121, USA
                [3 ]Department of Ophthalmic Research, Cleveland Clinic Foundation, Area I31, 9500 Euclid Avenue, Cleveland, Ohio, 44195, USA
                Article
                1475-2859-3-7
                10.1186/1475-2859-3-7
                421735
                15175111
                753a184a-8fa2-442a-bcee-e54bf0b75925
                Copyright © 2004 Mahato et al; licensee BioMed Central Ltd. This is an Open Access article: verbatim copying and redistribution of this article are permitted in all media for any purpose, provided this notice is preserved along with the article's original URL.
                History
                : 8 May 2004
                : 2 June 2004
                Categories
                Review

                Biotechnology
                Biotechnology

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