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  • Articles  (3,020)
  • Articles: DFG German National Licenses  (3,020)
  • 2000-2004  (385)
  • 1985-1989  (1,802)
  • 1950-1954  (368)
  • 1930-1934  (247)
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  • Process Engineering, Biotechnology, Nutrition Technology  (3,020)
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  • Articles  (3,020)
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  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food safety 10 (1989), S. 0 
    ISSN: 1745-4565
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Clostridium botulinum may pose a hazard in extended shelf-life refrigerated foods. Nonproteolytic strains ofC. botulinum, which can grow at refrigeration temperatures, may be given sufficient time to grow if the shelf-life is extensive. Proteolytic strains may grow in these products if temperature abuse occurs. Mild heat treatments and vacuum or modified atmosphere packaging may select for C. botulinum and allow toxicity to occur in organoleptically acceptable products. Multiple barriers and multifactorial experiments to generate predictive models are advocated to ensure safety of extended shelf-life refrigerated foods.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Journal of chemical & engineering data 30 (1985), S. 491-492 
    ISSN: 1520-5134
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology , Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The effect of autoclaving on meat enhancement of dietary iron bioavailability was studied. Meat was mixed with FeSO4 or hemoglobin to obtain ratios of iron from meat to iron from FeSO4 or hemoglobin of 100:0, 75:25, 50:50, 25:75, and 0:100. One-half of each mixture (except meat:FeSO4 mixture 0:100) was autoclaved for 90 min at 15 psi. The meat mixtures were lyophilized and formulated into diets to provide approximately 35 mg Fe/kg. Hemoglobin regeneration efficiency (HRE) was determined as the percent iron gained as hemoglobin relative to the iron consumed. Heat increased the HREs of meat/hemoglobin mixtures and of hemoglobin. Heat did not affect the HRE of meat or meat/ferrous sulfate mixtures. Meat did not significantly enhance the bioavailability of total dietary iron.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 52 (1987), S. 0 
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The temporal cholesterolemic patterns to skim milk powder (SMP) and reprocessed SMP (RSMP) diets were compared to diets containing casein or laboratory rat chow over a 24-day period. SMP was hypocholestetemic relative to casein in rats fed a 1% dietary cholesterol. Reprocessing of SMP resulted in an apparent loss of the relative hypocholesterolemic reponse of native SMP. Amino acid analysis of SMP and RSMP, showed only marginally lower lysine levels than casein; however, the Iysine/arginine ratio was higher in SMP than either in casein or RSMP. Available lysine content in SMP was higher than in RSMP, suggesting occurrence of nonenyzmatic browning reactions. Although a similar cholesterolemic response was observed in casein and RSMP, the available lysine content of these two protein sources were markedly different, suggesting that reduced available lysine alone was not totally responsible for the lower cholesterolemic response of SMP, relative to casein.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 50 (1985), S. 0 
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Proximate and micronutrient composition of cantaloupe and honeydew melons purchased from six marketing locations at marketing times near maximum and minimum product availability were determined. Cantaloupe varieties purchased at periods near maximum availability showed significantly higher (α= 0.01) levels of niacin, riboflavin, thiamin, ascorbic acid, folacin and Cr compared to those purchased near minimum availability. Honeydew melon varieties purchased at periods near maximum availability showed significantly lower (α= 0.01) levels of ascorbic acid, folacin, pantothenic acid, K, Zn, and Cr compared to those purchased near minimum availability. Although some differences were observed between values obtained and those reported in Handbook 8–9, proximate composition and mean values for micronutrients approximated those previously reported.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Company
    Nature biotechnology 5 (1987), S. 947-950 
    ISSN: 1546-1696
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: [Auszug] Detection and monitoring of genetically engineered microorganisms released to the environment, as well as pathogens, are primary factors in risk assessment. Culture methods have been proposed for both detection and monitoring. However, microorganisms in natural systems may not always be culturable. ...
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Springer
    Journal of industrial microbiology and biotechnology 3 (1988), S. 263-272 
    ISSN: 1476-5535
    Keywords: Adaptation to cyanide ; Cyanide degradation ; Formate ; Pseudomonad ; Industrial wastewater
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary A cyanide-degrading pseudomonad was isolated by selective enrichment in a chemostat inoculated with coke-plant activated sludge and maintained at a dilution rate of 0.042/h for 60 days with a feed of 10 mg/l cyanide. The isolate, a facultative methylotroph capable of growth on methanol and methylamine, degraded cyanide to formate and ammonia; it could utilize the released ammonia as a nitrogen source but did not further metabolize formate under the experimental conditions employed. Both cyanide-degrading enzyme activity and respiratory resistance to cyanide were inducible and were enhanced by repeated exposure to the compound. Cell-free extracts stoichiometrically converted cyanide to formate and ammonia in a reaction that did not require oxygen. Enzyme activity, lost upon dialysis, was restored by less than equimolar ratios of NAD(P)H or ascorbate to cyanide, indicating that the reductants did not function directly as co-enzymes.
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature America Inc.
    Nature biotechnology 18 (2000), S. 339-342 
    ISSN: 1546-1696
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: [Auszug] Several important crops have been engineered to express toxins of Bacillus thuringiensis (Bt) for insect control. In 1999, US farmers planted nearly 8 million hectares (nearly 20 million acres) of transgenic Bt crops approved by the EPA. Bt-transgenic plants can greatly reduce the use of ...
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  • 9
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract A 3.0-kb genomic fragment has been isolated from Rhodospirillum rubrum (ATCC 25903) that contains an open reading frame (ORF) with strong homology to other known polyhydroxyalkanoate (PHA) synthase genes. This ORF has lower homology to the R. rubrum strain Ha PHA synthase than would be expected within the same species. We have conducted a series of heterologous expression studies evaluating the in vivo substrate specificity of PHA synthase genes from Rhodobacter sphaeroides, Ralstonia eutropha (formerly Alcaligenes eutrophus), Thiocystis violacea, and Nocardia corrallina, within the PHA-synthase-negative hosts, Ralstonia eutropha DSM541 and Pseudomonas putida GpP104. The N. corrallina PHA synthase incorporated the highest percentage of C5 monomers in the polymer when fermented in medium supplemented with 0.1% heptanoate as the sole carbon source. When the T. violacea and R. sphaeroides were expressed in the PHA-negative host DSM541, a greater percentage of C5 monomer was observed in the polymer as compared to the expression of the PHA synthase of R. eutropha, when the transconjugants were fermented in medium supplemented with 0.4% propionate. Evaluation for preference of medium-chain-length monomers demonstrated the flexibility of the N. corrallina, T. violacea, and R. eutropha synthase genes to polymerize a copolyester composed of short- and medium-chain-length monomers when the respective transconjugants were fermented in medium supplemented with 0.5% octanoate. These studies demonstrate that the PHA synthase from N. corrallina, T. violacea, and R. eutropha are able to polymerize a copolyester composed of short- and medium-chain-length monomers, while the PHA synthase from R. sphaeroides lacks this ability and only produces a short-chain-length polymer. These observations suggest that the composition of the PHA from the PHA-producing organisms does not necessarily reflect the inherent specificity of the PHA synthase.
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  • 10
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract A chitinase gene (chiA) from Pseudomonas sp. YHS-A2 was cloned into Escherichia coli using pUC19. The nucleotide sequence determination revealed a single open reading frame of chiA comprised of 1902 nucleotide base pairs and 633 deduced amino acids with a molecular weight of 67,452 Da. Amino acid sequence alignment showed that ChiA contains two putative chitin-binding domains and a single catalytic domain. Two proline-threonine repeat regions, which are linkers between catalytic and substrate-binding domains in some cellulases and xylanases, were also found. From E. coli, ChiA was purified 12.8-fold relative to the periplasmic fraction. The Michaelis constant and maximum initial velocity for p-nitrophenyl-N,N′-diacetylchitobiose were 1.06 mM and 44.4 μmol/h per mg protein, respectively. The purified ChiA binds not only to colloidal chitin but also to other substrates (avicel, chitosan, and xylan), but the binding affinity of avicel, chitosan, and xylan is around 10 times lower than that of colloidal chitin. The reaction of ChiA with colloidal chitin and chitooligosaccharides (trimer-hexamer) produced an end product of N,N′-diacetylchitobiose, indicating that ChiA is a chitobiosidase.
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