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  • Molecular Diversity Preservation International  (4)
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  • 1
    Publication Date: 2020-07-05
    Description: Hepcidin, an antimicrobial peptide produced by the liver, also controls the iron balance and regeneration in vertebrates. Two types of hepcidin (Hamp1 and Hamp2) have been found in the bodies of black rockfish (Sebastes schlegelii). The full-length cDNA of hepcidin was cloned to enable a study of the antibacterial roles of these two hepcidins (Hamp) in black rockfish. The antimicrobial function of recombinant hepcidins was tested both in vitro and in vivo by the synthesis in Escherichia coli of recombinant hepcidin (approximately 11 kDa) from black rockfish. The recombinant hepcidins inhibited the growth of two bacterial species, Streptococcus iniae FP5228 and Pseudomonas aeruginosa, at various concentrations, in vitro after 6 h post-incubation, respectively. During infection, the production of ferroportin was reduced, suggesting the preservation of iron to prevent microbial proliferation. In vivo administration of Hamp1, but not Hamp2, synthetic peptides induced a substantial reduction in the expression of ferroportin, suggesting that in black rockfish with two forms of hepcidin, ferroportin production is regulated by the iron-regulator Hamp1, and not by the dedicated antimicrobial Hamp2. The findings of this study suggest the various antimicrobial roles of these two types of hepcidin.
    Electronic ISSN: 2077-1312
    Topics: Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics
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  • 2
    Publication Date: 2020-09-24
    Description: The present study was focused on the investigation of physiochemical changes in tuna subjected to a novel supercooling preservation, which was assisted using a combination of pulsed electric fields (PEF) and oscillating magnetic fields (OMF). Fresh tuna fillets were stored without freezing at −3.2 °C for 8 days. The electrochemical impedance spectroscopy (EIS) parameter Py indicated that there was a significant difference between the frozen-thawed samples (36.3%) and fresh (46.6%) and supercooled (45.9%) samples, indicating that cell damage from ice crystal growth did not occur in the supercooled tuna sample. The microstructure observation and drip loss measurement further confirmed that the ice crystal damage was present in frozen tuna, whereas no cellular damage was found in the supercooled samples. The EIS proved its ability to distinguish between tuna samples that were frozen or chilled (i.e., refrigerated and supercooled) during storage; however, it was less sensitive in detecting the extent of spoilage. Instead, the K-value was used to evaluate tuna freshness, and the measured K-values of the refrigerated, supercooled, and frozen tuna samples after 8 days of storage were 74.3%, 26.4%, and 19.9%, respectively, suggesting that the supercooling treatment significantly preserved the tuna fillets fresh with the improved shelf-life when compared to conventional refrigeration.
    Electronic ISSN: 2304-8158
    Topics: Chemistry and Pharmacology
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  • 3
    Publication Date: 2019-05-17
    Description: The objective of this study was to investigate the influence of pH value on the in vitro digestibility of malic acid-treated corn starch in relation to its structural properties. Varying pH values (1.5–8.5) of 2 M malic acid solution were combined with corn starch in a forced-air oven at 130 °C for 12 h. Using Fourier-transform infrared spectroscopy (FT-IR), carbonyl groups were detected in malic acid-treated corn starch, indicating cross-linking through esterification. As the pH value of malic acid-treated corn starch decreased from 8.5 to 1.5, the resistant starch content increased from 18.2 to 74.8%. This was the result of an increased degree of substitution and was maintained after gelatinization. The granular structure of malic acid-treated corn starches was not destroyed, and the starches maintained birefringence. This malic acid-treated corn starch could be utilized in heat processed foods such as bread and cookies as well as in products with reduced calories.
    Electronic ISSN: 1420-3049
    Topics: Chemistry and Pharmacology
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  • 4
    Publication Date: 2020-08-26
    Description: Bacteria can produce recombinant proteins quickly and cost effectively. However, their physiological properties limit their use for the production of proteins in their native form, especially polypeptides that are subjected to major post-translational modifications. Proteins that rely on disulfide bridges for their stability are difficult to produce in Escherichia coli. The bacterium offers the least costly, simplest, and fastest method for protein production. However, it is difficult to produce proteins with a very large size. Saccharomyces cerevisiae and Pichia pastoris are the most commonly used yeast species for protein production. At a low expense, yeasts can offer high protein yields, generate proteins with a molecular weight greater than 50 kDa, extract signal sequences, and glycosylate proteins. Both eukaryotic and prokaryotic species maintain reducing conditions in the cytoplasm. Hence, the formation of disulfide bonds is inhibited. These bonds are formed in eukaryotic cells during the export cycle, under the oxidizing conditions of the endoplasmic reticulum. Bacteria do not have an advanced subcellular space, but in the oxidizing periplasm, they exhibit both export systems and enzymatic activities directed at the formation and quality of disulfide bonds. Here, we discuss current techniques used to target eukaryotic and prokaryotic species for the generation of correctly folded proteins with disulfide bonds.
    Electronic ISSN: 2079-6382
    Topics: Chemistry and Pharmacology , Medicine
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