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  • 11
    Electronic Resource
    Electronic Resource
    Highly Concentrated Branched Oligosaccharides as Cryoprotectant for Surimi (1999)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 64 (1999), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Freeze-thawing studies at different concentrations, using an actomyosin solution (extracted from Alaska pollock), revealed that an 8% (w/v) solution of oligosaccharides mixture (HBOS) was most effective in cryoprotection. During frozen storage (-18°C), HBOS showed cryoprotective effects similar to sucrose and a sucrose+sorbitol mixture (1:1). Surimi gel prepared with HBOS showed higher hardness and more dense microstructure than others, although water holding capacity was slightly lower than the gel with sucrose+sorbitol. HBOS containing gel showed lower whiteness than sucrose but no difference with sucrose+sorbitol. HBOS appeared to have good potential as a non-sweet cryoprotectant of fish protein.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1999.tb15055.x
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  • 12
    Electronic Resource
    Electronic Resource
    Strengthening of Alumina by Formation of a Mullite/Glass Layer on the Surface (1997)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of the American Ceramic Society 80 (1997), S. 0 
    Details
    ISSN: 1551-2916
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics , Physics
    Notes: A layer composed of mullite and silicate glass was caused to form on the surface of a high-purity alumina ceramic in order to enhance the strength of the material. The layer was formed by exposing the specimens above a bed of SiC platelets at 1400°3C to a flowing H2 atmosphere containing ∼0.1% H2O. A reaction between the SiC platelets and the H2O in the environment resulted in the generation of SiO gas. Some of the SiO gas subsequently reacted with ambient H2O in the atmosphere, forming SiO2“smoke” which was deposited on, and reacted with, the alumina substrate. The strength of the ceramic was significantly improved by the reaction layer, which was found to be comprised of mullite and silicate glass. The increases in strength (about 60% above that of the material in the “as-polished” condition) was attributed to the blunting of surface cracks. A similar strengthening effect was observed in samples of the material which had been ground with a 220-grit diamond abrasive wheel (as had all of the samples) but not polished.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1151-2916.1997.tb03064.x
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  • 13
    Electronic Resource
    Electronic Resource
    Human anti-Pseudomonas aeruginosa outer membrane proteins IgG cross-protective against infection with heterologous immunotype strains of P. aeruginosa (1999)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS immunology and medical microbiology 25 (1999), S. 0 
    Details
    ISSN: 1574-695X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: In order to develop an effective means to treat and prevent Pseudomonas aeruginosa infections, we have purified P. aeruginosa outer membrane protein (Oprs)-specific human IgG antibody using a large-scale affinity column. In this study, we investigated the cross-protective activity of the purified anti-Oprs IgG against various immunotype strains of P. aeruginosa. The anti-Oprs IgG reacted with Oprs isolated from seven Fisher-Devlin immunotype strains of P. aeruginosa and was able to promote opsonophagocytic killing of all seven immunotype strains by human phagocytic cells. Administration of 500 μg anti-Oprs IgG to mice raised the LD50 of the P. aeruginosa strains by 8–250-fold, indicating the protective capacity against heterologous P. aeruginosa strains as well as homologous strains. In contrast, despite high titers against P. aeruginosa Oprs, total serum IgG isolated from burn patient sera was no better than normal serum IgG in protecting mice from infection with P. aeruginosa. These data demonstrate that the affinity-purified human anti-Oprs IgG could afford protection against heterologous immunotype P. aeruginosa strains and provide a rationale to use anti-Oprs IgG as an adjunct for treatment of P. aeruginosa infections in humans.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-695X.1999.tb01358.x
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  • 14
    Electronic Resource
    Electronic Resource
    Erratum to ‘Identification of the genes encoding enzymes involved in the early biosynthetic pathway of pteridines in Synechocystis sp. PCC 6803’ (1999)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 179 (1999), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1999.tb08725.x
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  • 15
    Electronic Resource
    Electronic Resource
    Identification of the genes encoding enzymes involved in the early biosynthetic pathway of pteridines in Synechocystis sp. PCC 6803 (1999)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 176 (1999), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The biosynthetic pathway for the pteridine moiety of cyanopterine, as well as tetrahydrobiopterine, has been investigated in Synechocystis sp. PCC 6803. Open reading frames slr0426, slr1626, slr0078 and sll0330 of the organism putatively encoding GTP cyclohydrolase I, dihydroneopterine aldolase, 6-pyruvoyltetrahydropterine synthase and sepiapterine reductase, respectively, have been cloned into T7-based vectors for expression in Escherichia coli. The recombinant proteins have been purified to homogeneity and demonstrated to possess expected genuine activities except that of sll0330. Our result is the first direct evidence for the functional assignment of the open reading frames in Synechocystis sp. PCC 6803. Furthermore, the 6-pyruvoyltetrahydropterine synthase gene is demonstrated for the first time in prokaryotes. Based on the result, biosynthesis of cyanopterine is discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1999.tb13658.x
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  • 16
    Electronic Resource
    Electronic Resource
    Cloning of the thermostable phytase gene (phy) from Bacillus sp. DS11 and its overexpression in Escherichia coli (1998)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 162 (1998), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Phytase hydrolyzes phytate to release inorganic phosphate, which would decrease the addition of phosphorus to feedstuffs for monogastric animals and thus reduce environmental pollution. The gene encoding phytase from Bacillus sp. DS11 was cloned in Escherichia coli and its sequence determined. A 560-bp DNA fragment was used as a probe to screen the genomic library. It was obtained through PCR of Bacillus sp. DS11 chromosomal DNA and two oligonucleotide primers based on N-terminal amino acid sequences of the purified protein and the cyanogen bromide-cleaved 21-kDa fragment. The phy cloned was encoded by a 2.2-kb fragment. This gene comprises 1152 nucleotides and encodes a polypeptide of 383 amino acids with a deduced molecular mass of 41 808 Da. Phytase was produced to 20% content of total soluble proteins in E. coli BL21 (DE3) using the pET22b(+) vector with the inducible T7 promoter. This is the first nucleic sequence report on phytase from a bacterial strain.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1998.tb12997.x
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  • 17
    Electronic Resource
    Electronic Resource
    Purification of an antifungal PR-5 protein from flower buds of Brassica campestris and cloning of its gene (1997)
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 101 (1997), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: An antifungal pathogenesis-related (PR) group 5 protein with a molecular mass of 27 kDa (BFTP) was purified from flower buds of Brassica campestris. BFTP exhibits antifungal activity against Neurospora crassa, causing rapid release of cytoplasmic material at the hyphal tips of the fungus. BFTP immuno-cross-reacts with antiserum raised against the tobacco osmotin-like PR-5 protein. Using a PCR product generated with the help of two degenerate PCR primers for (1) the N-terminal amino acid sequence of the protein and (2) the conserved peptide domain that appears in all PR-5 proteins, we were able to isolate from a flower-bud cDNA library a cDNA (933 bp) that encodes this protein (pBFTP). The deduced amino acid sequence shows high similarity to PWIR2 from wheat (43%) and thaumatin II from Thaumatococcus daniellii Benth (40%). It contains the 16 cysteine residues that are conserved in all PR-5 proteins at their invariant positions. The cDNA predicts the synthesis of a preprotein which is subsequently processed into the mature protein by removal of an N-terminal signal peptide. The mRNA is predominantly expressed in flower buds, with a moderate level of transcripts detected in stems. Very low levels of the mRNA are present in root and leaf tissue. The gene is a member of a small multigene family in the genome of B. campestris.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1399-3054.1997.tb01041.x
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  • 18
    Electronic Resource
    Electronic Resource
    Riboflavin-Sensitized Photodynamic UV Spectrophotometry for Ascorbic Acid Assay in Beverages (1995)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 60 (1995), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Riboflavin-sensitized photodynamic ultraviolet spectrophotometric assay of various commercial beverages was carried out. The maximum concentration of ascorbic acid for obtaining a background correction (15 min illumination and pH 7.5) was 21 μg/mL ascorbic acid in the testing solution. The upper limit of the measurement range for a straight line in the calibration graph of standard ascorbic acid was 10 μg/mL, (working range 0–10 μg/mL). The results in repeatability of the method for ascorbic acid contents in commercial fruit juices and soft-drinks showed a maximum of 4% relative standard deviation. Recovery tests with known amounts of added ascorbic acid in different fruit juices and sports drink showed the recovery of added ascorbic acid was 97.5–102.3%. Indophenol, iodine and/or HPLC methods were used in parallel to ascertain the reliability of the proposed method. This type assay could be successfully applied to many commercial beverages for determination of ascorbic acid with good accuracy, precision and reliability.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1995.tb05673.x
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  • 19
    Electronic Resource
    Electronic Resource
    Characterization of an alkaline lipase from Proteus vulgaris K80 and the DNA sequence of the encoding gene (1996)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 135 (1996), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract A facultatively anaerobic bacterium producing an extracellular alkaline lipase was isolated from the soil collected near a sewage disposal plant in Korea and identified to be a strain of Proteus vulgaris. The molecular mass of the purified lipase K80 was estimated to be 31 kDa by SDS-PAGE. It was found to be an alkaline enzyme having maximum hydrolytid activity at pH 10, while fairly stable in a wide pH range from 5 to 11. The gene for lipase K80 was cloned in Escherichia coli. Sequence analysis showed an open reading frame of 861 bp coding for a polypeptide of 287 amino acid residues. The deduced amino acid sequence of the lipase gene had 46.3% identity to the lipase from Pseudomonas fragi.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1996.tb07975.x
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  • 20
    Electronic Resource
    Electronic Resource
    Investigating the Comparative Biology of the Heterokonts with Nucleic Acids (1996)
    Oxford, UK : Blackwell Publishing Ltd
    The @journal of eukaryotic microbiology 43 (1996), S. 0 
    Details
    ISSN: 1550-7408
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: During the last decade investigations of heterokont protists utilizing molecular methods have challenged established biosystematic concepts. Most investigations emphasized the chloroplast genome or sequences from nuclear-encoded, ribosomal genes. Refinement of DNA isolation protocols, advent of “universal primers” and the polymerase chain reaction, automated sequencing and increased accessibility of DNA sequence databases have expanded data-gathering efficiency and increased dataset sizes. Because independent datasets have been easier to obtain, the testing of specific phylogenetic hypotheses has been facilitated, altering relationship concepts, primarily at phylum/class levels, and perceptions of cellular evolution. New approaches have emphasized ecological studies and extended studies to genus/species levels and poorly investigated genomes. This paper reviews studies documenting these impacts and identifies some current limitations. Additionally, new DNA sequence data from our laboratory on nuclear-encoded rDNA internal transcribed spacers and the chloroplast-encoded psb A gene suggest that these regions will provide taxonomic resolution for the Synu-rophyceae, at the class/order level and subspecies level, respectively.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1550-7408.1996.tb04489.x
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