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  • Articles  (44,319)
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  • Articles  (44,319)
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  • 2020-2024
  • 2000-2004  (15,175)
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  • 1
    Electronic Resource
    Electronic Resource
    GTP cyclohydrolase II and 3,4-dihydroxy-2-butanone 4-phosphate synthase are rate-limiting enzymes in riboflavin synthesis of an industrial Bacillus subtilis strain used for riboflavin production (1999)
    Springer
    Journal of industrial microbiology and biotechnology 22 (1999), S. 1-7 
    Details
    ISSN: 1476-5535
    Keywords: Keywords: Bacillus subtilis; riboflavin; 3,4-dihydroxy-2-butanone 4-phosphate synthase; GTP cyclohydrolase II
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: One of the proteins encoded by the riboflavin operon of Bacillus subtilis, RibA, was identified as the rate limiting enzyme in an industrial riboflavin producing strain. An additional single copy of the ribA gene was introduced into the sacB locus of the riboflavin production strain and was expressed constitutively from the medium strength vegI promoter. This led to improved riboflavin titers and yields of riboflavin on glucose of up to 25%. Both enzymatic activities of RibA, the 3,4-dihydroxy-2-butanone 4-phosphate synthase activity located in the N-terminal half of the protein and the GTP cyclohydrolase II activity of the C-terminal domain, are necessary for the improved riboflavin productivity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/sj.jim.2900590
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  • 2
    Electronic Resource
    Electronic Resource
    Thymol-triggered lysis of Escherichia coli expressing Lactobacillus phage LL-H muramidase (1999)
    Springer
    Journal of industrial microbiology and biotechnology 22 (1999), S. 39-43 
    Details
    ISSN: 1476-5535
    Keywords: Keywords: murein; cell wall hydrolase; phage lysin; thymol-triggered lysis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Effective disruption of Escherichia coli cells is achieved by the intracellularly accumulated recombinant murein hydrolase (Lactobacillus bacteriophage LL-H muramidase) after the addition of 5 mM thymol. Thymol destroys the integrity and electric potential of the cytoplasmic membrane, and as a consequence the muramidase can access and hydrolyze the cell wall murein leading to cell lysis. Lysis occurred within 5 min after the addition of thymol and seemed to be efficient at high culture densities. This lysis method does not require cell harvesting or addition of other cell wall weakening substances or exogenous enzymes. As a cell disruption method, thymol-triggered lysis is as efficient as sonication in the presence of 1% Triton. Furthermore, thymol did not interfere with the purification steps of Mur by expanded bed adsorption chromatography (EBA), suggesting that the lysis method presented here is well suited for large-scale production and purification of intracellular proteins of E. coli.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/sj.jim.2900598
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  • 3
    Electronic Resource
    Electronic Resource
    Biotransformation of 1-nitrobenzo[e]pyrene by the fungus Cunninghamella elegans (1999)
    Springer
    Journal of industrial microbiology and biotechnology 22 (1999), S. 52-57 
    Details
    ISSN: 1476-5535
    Keywords: Keywords: nitro-PAHs; metabolism; Cunninghamella elegans; biotransformation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Biotransformation of 1-nitrobenzo[e]pyrene (1-nitro-BeP), an environmental pollutant derived from the nitration of a non-carcinogen, benzo[e]pyrene, was studied using the fungus Cunninghamella elegans ATCC 36112. After 72 h incubation, 89% of 1-nitro-[3H]BeP added had been metabolized to two major metabolites. These metabolites were separated by reversed-phase high performance liquid chromatography and identified by 1H NMR, UV-visible, and mass spectral techniques as 1-nitro-6-benzo[e]pyrenylsulfate and 1-nitrobenzo[e]pyrene 6-O-β-glucopyranoside. Comparison of the fungal metabolism patterns of 1-nitro-BeP and BeP indicates that the nitro group at the C-1 position of BeP altered the regioselectivity of metabolism.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/sj.jim.2900601
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  • 4
    Electronic Resource
    Electronic Resource
    Commercial riboflavin production by recombinant Bacillus subtilis: down-stream processing and comparison of the composition of riboflavin produced by fermentation or chemical synthesis (1999)
    Springer
    Journal of industrial microbiology and biotechnology 22 (1999), S. 19-26 
    Details
    ISSN: 1476-5535
    Keywords: Keywords: recombinant Bacillus subtilis; riboflavin produced by fermentation; down-stream processing; analytics; registration
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: A novel process for riboflavin production using a recombinant Bacillus subtilis strain has been developed. Here we describe a down-stream processing procedure to obtain riboflavin qualities having a minimal content of 96% (‘feed-grade’) and 98% (‘food/pharma-grade’) riboflavin, respectively. Compared to riboflavin produced by chemical synthesis, products with improved chemical purity were obtained. All compounds representing more than 0.1% of the final products were identified. Feed-grade riboflavin material ex fermentation contained small amounts of amino acids and amino sugars and the biosynthetic riboflavin precursor dimethyl-ribityl-lumazine. All other side products found were derived from riboflavin, resulted from the purification procedure and were also found in riboflavin obtained by chemical synthesis. The Bacillus-produced riboflavin does not contain DNA. The data presented here were used to obtain product approval for the commercial application in the USA, Japan and the UK.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/sj.jim.2900604
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  • 5
    Electronic Resource
    Electronic Resource
    Quantitative sampling of indoor air biomass by signature lipid biomarker analysis (1999)
    Springer
    Journal of industrial microbiology and biotechnology 22 (1999), S. 80-87 
    Details
    ISSN: 1476-5535
    Keywords: Keywords: airborne bacteria; phospholipid fatty acids; human health
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Exposure to airborne biocontaminants may result in a multitude of health effects and is related to a pronounced increase in adult-onset asthma. Established culture-based procedures for quantifying microbial biomass from airborne environments have severe limitations. Assay of the phospholipid fatty acid (PLFA) components of airborne microorganisms provides a quantitative method to define biomass, community composition and nutritional/physiological activity of the microbial community. By collecting airborne particulate matter from a high volume via filtration, we collected sufficient biomass for quantitative PLFA analysis. Comparing high (filtration) and low (impaction) volume air sampling techniques at 26 locations within the Eastern United States, we determined that PLFA analysis provided a viable alternative to the established but flawed culture-based techniques for measuring airborne microbial biomass and community composition. Compared to the PLFA analysis, the culture techniques underestimated the actual viable airborne biomass present by between one to three orders of magnitude. A case study of a manufacturing plant at which there had been complaints regarding the indoor air quality is presented. Phospholipid fatty acid characterization of the biomass enabled contamination point source determination. In comparison with samples taken outdoors, increases in the relative proportion of trans PLFA, reflecting shifts in the physiological status of viable airborne Gram-negative bacteria, were detected in the indoor air samples at a majority of sampling sites.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/sj.jim.2900609
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  • 6
    Electronic Resource
    Electronic Resource
    Thermostability of three α-amylases of Streptomyces sp IMD 2679 (1999)
    Springer
    Journal of industrial microbiology and biotechnology 22 (1999), S. 96-99 
    Details
    ISSN: 1476-5535
    Keywords: Keywords: Streptomyces sp; α-amylase; thermostability; structure-function; dimerisation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The amylolytic system of Streptomyces sp IMD 2679 is composed of three α-amylases, amylase I, II and III, with temperature maxima of 60, 60–65 and 65°C, respectively. Although each α-amylase displayed higher stability in the pH range 6.0–8.5 than at pH 5.0–5.5, differences in their thermostabilities were more evident as the pH increased from pH 6.0 to 8.5. There was a 14-min difference in half-lives between amylase III, the most thermostable enzyme and amylase II at pH 6.0, and a 46-min difference in the half-lives of amylase III and the least thermostable enzyme, amylase I at pH 6.5. In addition, the α-amylases underwent a pH-dependent monomer-dimer transformation. Increased thermostability of the α-amylases was reflected in the variable contents of amino acids (Arg, His, Ser) responsible for electrostatic interactions, and in the levels of aliphatic and bulky hydrophobic amino acids. There was a two-fold reduction in Cys levels in amylase III relative to amylase I and II.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/sj.jim.2900612
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  • 7
    Electronic Resource
    Electronic Resource
    Aerobic batch degradation of phenol using immobilized Pseudomonas putida (1999)
    Springer
    Journal of industrial microbiology and biotechnology 22 (1999), S. 121-126 
    Details
    ISSN: 1476-5535
    Keywords: Keywords: biodegradation; phenol; Pseudomonas putida; immobilized
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Alginate concentrations between 2 and 4% had little effect on the degradation rate of phenol by alginate-immobilized Pseudomonas putida. Ten-degree shifts from 25°C resulted in approximately 30% slower degradation. Maximal degradation rates were favored at pH 5.5–6.0. The response of degradation rate to increased air flow in the bubble column used was almost linear and an optimal higher than 16 vol vol−1 was indicated, although free cells appeared in the reaction medium above 12 vol vol−1. When the initial phenol concentration was raised, degradation rate was not significantly affected until levels higher than 1200 mg ml−1 where performance was markedly reduced. Increasing the ratio of total bead volume to medium volume gave progressively smaller increases in degradation rate. At a medium volume to total bead volume ratio of 5:1, the maximum degradation rate was 250 mg L−1 h−1.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/sj.jim.2900617
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  • 8
    Electronic Resource
    Electronic Resource
    Purification and characterization of the intracellular β-glucosidase from Aureobasidium sp ATCC 20524 (1999)
    Springer
    Journal of industrial microbiology and biotechnology 22 (1999), S. 160-163 
    Details
    ISSN: 1476-5535
    Keywords: Keywords: β-glucosidase; cellobiase; cellobiose-hydrolysis; Aureobasidium
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: β-Glucosidase hydrolyzing cellobiose was extracted from Aureobasidium sp ATCC 20524 and purified to homogeneity. The molecular mass was estimated to be about 331 kDa. The enzyme contained 26.5% (w/w) carbohydrate. The optimum pH and temperature for the enzyme reaction were pH 4 and 80°C, respectively. The enzyme was stable at a wide range of pH, 2.2–9.8, after 3 h and at 75°C for 15 min. The kinetic parameters were determined. The enzyme was relatively stable against typical organic enzyme inhibitors. The enzyme also hydrolyzed gentiobiose, p-nitrophenyl-β-glucoside and salicin.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/sj.jim.2900618
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  • 9
    Electronic Resource
    Electronic Resource
    Cryptococcus nodaensis sp nov, a yeast isolated from soil in Japan that produces a salt-tolerant and thermostable glutaminase (1999)
    Springer
    Journal of industrial microbiology and biotechnology 22 (1999), S. 127-132 
    Details
    ISSN: 1476-5535
    Keywords: Keywords: umami; L-glutamic acid, glutaminase; Cryptococcus
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: An anamorphic basidiomycetous yeast, which produced a salt-tolerant and thermostable glutaminase, was isolated from soil in Japan and classified in the genus Cryptococcus. Its substrate specificity suggests that this enzyme is an L-glutaminase asparaginase (EC 3.5.1.38). The strain, G60, resembles Cryptococcus laurentii in the taxonomic criteria traditionally employed for yeasts, however it can be distinguished as a separate species based on DNA–DNA reassociation experiments and sequence analysis of the large sub-unit rDNA. Phenotypically, the isolate can be differentiated from C. laurentii by the inability to utilize arbutin as a sole source of carbon. Based on sequence analysis, the strain is related to a group of hymenomycetous yeasts including Bulleromyces albus, Bullera unica, C. laurentii and C. skinneri. The strain, which is formally described as Cryptococcus nodaensis, is industrially important for the formation of the umami taste during production of proteolytic seasonings.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/sj.jim.2900623
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  • 10
    Electronic Resource
    Electronic Resource
    Closed ecological systems for space travel and extraterrestrial habitation, (Volume 3) (1999)
    Springer
    Journal of industrial microbiology and biotechnology 22 (1999), S. 216-224 
    Details
    ISSN: 1476-5535
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/sj.jim.2900634
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