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  • General Chemistry  (254)
  • Biochemistry and Biotechnology  (33)
  • Computational Chemistry and Molecular Modeling  (12)
  • 1
    Electronic Resource
    Electronic Resource
    Weinheim : Wiley-Blackwell
    Zeitschrift für die chemische Industrie 54 (1941), S. 213-215 
    ISSN: 0044-8249
    Keywords: Chemistry ; General Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 0887-3585
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: A mixed phage library containing random peptides from four to eight residues in length flanked by cysteine residues was screened using a recombinant soluble, form of human ICAM-1, which included residues 1-453, (ICAM-11-453). Phage bound to immobilized ICAM-11-453 were eluted by three methods: (1) soluble ICAM-11-453, (2) neutralizing murine monoclonal antibody, (anti-ICAM-1, M174F5B7), (3) acidic conditions. After three rounds of binding and elution, a single, unique ICAM-1 binding phage bearing the peptide EWCEYLGGYLRYCA was isolated; the identical phage was selected with each method of elution. Attempts to isolate phage from non-constrained (i.e., not containing cysteines) libraries did not yield a phage that bound to ICAM-1. Phage displaying EWCEYLGGYLRCYA bound to immobilized ICAM-11-453 and to ICAM-11-185, a recombinant ICAM-1, which contains only the two amino-terminal immunoglobulin domains residing within residues 1-185. This is the region of the ICAM-1 that is bound by LFA-1. The phage did not bind to proteins other than ICAM-1. The phage bound to two ICAM-1 mutants, which contained amino acid substitutions that dramatically decreased or eliminated the binding to LFA-1. Studies were also performed with the corresponding synthetic peptide. The linear form of the synthetic EWCEYLGGYLRCYA peptide was found to inhibit LFA-1 binding to immobilized ICAM-11-453 in a protein-protein binding assay. By contrast, the disulfide, cyclized, form of the peptide was inactive. The EWCEYL portion of the sequence is homologous to the EWPEYL sequence found within rhinovirus coat protein 14, a nonintegrin protein that binds to ICAM-1. Taken together, the results suggests that the EWCEYLGGYLRCYA sequence is capable to binding to immobilized ICAM-1. Phage display appears to represent a new approach for the identification of peptides that interfere with ICAM-1 binding to β2 integrins. © 1996 Wiley-Liss, Inc.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 58 (1998), S. 554-559 
    ISSN: 0006-3592
    Keywords: directed evolution ; esterase ; epothilon ; Pseudomonas fluorescens ; stereoselectivity ; mutator strain ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The directed evolution of an esterase from Pseudomonas fluorescens using the mutator strain Epicurian coli XL1-Red was investigated. Mutants were assayed for their ability to hydrolyze a sterically hindered 3-hydroxy ester, which can serve as a building block in the synthesis of epothilones. Screening was performed by plating esterase producing colonies derived from mutation cycles onto minimal media agar plates containing indicator substances (neutral red and crystal violet). Esterase-catalyzed hydrolysis of the 3-hydroxy ester (ethyl or glycerol ester) was detected by the formation of a red color due to a pH decrease caused by the released acid. Esterases isolated from positive clones were used in preparative biotransformations of the ethyl ester. One variant containing two mutations (A209D and L181V) stereoselectively hydrolyzed the ethyl ester resulting in 25% ee for the remaining ester. © 1998 John Wiley & Sons, Inc. Biotechnol Bioeng 58: 554-559, 1998.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 45 (1995), S. 219-228 
    ISSN: 0006-3592
    Keywords: formate conversion ; mass spectrometer ; anaerobic conversion ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The dynamics of the anaerobic conversion of formate in a microbial mixed culture taken from an anaerobic fluidized bed reactor was studied using a new stirred micro reactor equipped with a membrane mass spectrometer. The microreactor with a toroidally shaped bottom and pitched blade turbine and a cylindrical flow guide was thermostated and additionally equipped with a pH electrode and pH control. During fed-batch experiments using formate, the dissolved gases (methane, hydrogen, and carbon dioxide), as well as the acid consumption rates for pH control were monitored continuously. Initially and at the end of each experiment, organic acids were analyzed using ion chromatography (IC). It was found that about 50% of the formate was converted to methane via hydrogen and carbon dioxide, 40% gave methane either directly or via acetate. This was calculated from experiments using H13CO3- pulses and measurement of 12CH4 and 13CH4 production rates. About 10% of the formate was converted to lactate, acetate, and propionate, thereby increasing the measured CO2/CH4 production ratio. The nondissociated formic acid was shown to be rate determining. From the relatively high Ks value of 2.5 mmol m-3, it was concluded that formate cannot play an important role in electron transfer. During dynamic feeding of formate, hydrogen concentration always increased to a maximum before decreasing again. This peak was found to be very discriminative during modeling. From the various models set up, only those with two-stage degradation and double Monod kinetics, both for CO2 and hydrogen, were able to describe the experimental data adequately. Additional discrimination was possible with the IC measurement of organic acids. © 1995 John Wiley & Sons, Inc.
    Additional Material: 11 Ill.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 24 (1982), S. 1905-1909 
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 24 (1982), S. 1901-1904 
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 27 (1985), S. 67-80 
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Fermentation (stoichiometric) equations are derived for anaerobic fermentations of propionic-acid bacteria (of both the Propionibacterium and acrylate pathways) and for production of various oxychemicals (butanol, acetone, isopropanol, butanediol, butyrate, acetate, propionate, succinate, lactate, and acrylate) from pentoses, hexoses, and cellobiose. The derivations of the equations are based on the fermentation biochemistries of the various bacterial classes. The validity of the equations is tested using fermentation data from the literature. The equations are shown to be valuable, among other uses, for calculating maximal yields and selectivities of the various fermentation products, as “gateway sensors” for monitoring of the fermentations, and for calculating the extents of the various intracellular reactions of the fermentation biochemistry.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 27 (1985), S. 1246-1257 
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: A fermentation system has been designed to demonstrate the use of gas chromatography (GC) for on-line monitoring of the butanol-acetone and other complex saccharolytic fermentations. Tangential flow ultrafiltration was used to sterilely and continuously obtain a cell-free filtrate from the fermentation broth for on-line GC analysis of butanol, butyrate, acetate, acetone, ethanol, and acetoin. The liquid injection system consists of a phosphoric acid contactor, a slider-type injection valve, and a heater to address the difficulties (ghosting) encountered in the analysis of carboxylic acids. The fermentation headspace gas was also analyzed by on-line GC for nitrogen and carbon dioxide, while hydrogen was measured by difference. Raw chromatographic data were analyzed by a chromatography data system. Both raw and processed data were transmitted to a VAX 11/750 computer for further processing (using the fermentation equation) and archiving. The fermentation equation, which has recently been derived and tested on completed fermentation data, was also found to be valid during transient fermentations and thus useful as a gateway sensor for calculating various fermentation parameters on-line. Such parameters include glucose concentration and gas composition, as well as a number of unobservable parameters (such as YATP, excess ATP, and NAD reduced by FdH2), which characterize the state of the fermentation.
    Additional Material: 13 Ill.
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 29 (1987), S. 962-968 
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: An artisanal static process for protein enrichment of cassava by solid-state fermentation, developed in laboratory and tested on pilot units in Burundi (Central Africa), provides enriched cassava containing 10.7% of dry matter protein versus 1% before fermentation. Cassava chips, processed into granules of 2-4-mm diameter, are moistened (40% water content) and steamed. After cooling to 40°C, cassava is mixed with a nutritive solution containing the inoculum (Rhizopus oryzae, strain MUCL 28627) and providing the following per 100 g dry matter: 3.4 g urea, 1.5 g KH2PO4, 0.8 g MgSO4·7H2O, and 22.7 g citric acid. For the fermentation, cassava, with ca. 60% moisture content, is spread in a thin layer (2-3 cm thick) on perforated trays and slid into an aerated humidified enclosure. The incubation lasts ± 65 h. The production of protein enriched cassava is 3.26 kg dry matter/m2 tray. The effects of the variation of the nutritive solution composition and the inoculum conservation period on the protein production are equally discussed.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 40 (1992), S. 183-186 
    ISSN: 0006-3592
    Keywords: Gluconobacter oxydans ; 5-ketogluconic acid ; tartatic acid ; vanadate ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The dependence of tartaric acid production by Gluconobacter oxydans ssp. oxydans ATCC 19357 and G. oxydans ssp. suboxydans ATCC 621 on vanadate was investigated. It was found with both organisms that trataric acid could only be produced in a medium containing vanadate (NH4VO3). A proposed intermediate of the tartaric acid metabolism in G. oxydans, 5-ketogluconic acid, was tested on its reactivity in the presence of the oxidizing catalyst vanadate. It could be shown that 5-ketogluconic acid and the catalyst vanadate, but not the activity of G. oxydans, were responsible for the formation of tartaric acid. G. oxydans was not able to produce tartaric acid by itself. The stereochemical identity of the formed tartaric acid could be identified as the L-(+)-type. Oxalic acid was formed from 5-ketogluconic acid with vanadate in the absence and in the presence of G. oxydans. The ratio of oxalic acid to tartaric acid was 1:1.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
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