288 research outputs found

    Protein oxidation in meat during chill storage

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    Proteolysis of camel milk by lactic acid bacteria

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    Acid stress response and protein induction in Campylobacter jejuni isolates with different acid tolerance.

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    <p>Abstract</p> <p>Background</p> <p>During the transmission route from poultry to the human host, the major foodborne pathogen <it>C. jejuni</it> may experience many types of stresses, including low pH caused by different acids. However, not all strains are equally sensitive to the stresses. The aim of this study was to investigate the response to acid stress of three sequenced <it>C. jejuni</it> strains with different acid tolerances using HCl and acetic acid.</p> <p>Results</p> <p>Two-dimensional gel electrophoresis was used for proteomic analysis and proteins were radioactively labelled with methionine to identify proteins only related to acid exposure. To allow added radioactive methionine to be incorporated into induced proteins, a modified chemically defined broth was developed with the minimal amount of methionine necessary for satisfactory growth of all strains. Protein spots were analyzed using image software and identification was done with MALDI-TOF-TOF. The most acid-sensitive isolate was <it>C. jejuni</it> 327, followed by NCTC 11168 and isolate 305 as the most tolerant. Overall, induction of five proteins was observed within the pI range investigated: 19 kDa periplasmic protein (p19), thioredoxin-disulfide (TrxB), a hypothetical protein Cj0706 (Cj0706), molybdenum cofactor biosynthesis protein (MogA), and bacterioferritin (Dps). Strain and acid type dependent differences in the level of response were observed. For strain NCTC 11168, the induced proteins and the regulator <it>fur</it> were analysed at the transcriptomic level using qRT-PCR. In this transcriptomic analysis, only up-regulation of <it>trxB</it> and <it>p19</it> was observed.</p> <p>Conclusions</p> <p>A defined medium that supports the growth of a range of <it>Campylobacter</it> strains and suitable for proteomic analysis was developed. Mainly proteins normally involved in iron control and oxidative stress defence were induced during acid stress of <it>C. jejuni</it>. Both strain and acid type affected sensitivity and response.</p

    Antioxidant capacity of hydrolyzed porcine tissues

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    The antioxidative capacity of seven different porcine tissue hydrolysates (colon, appendix, rectum, pancreas, heart, liver, and lung) were tested by four different assays, including iron chelation, 2,2′-azino-bis (3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) radical scavenging, 2,2-Diphenyl-1-(2,4,6-trinitrophenyl) hydrazyl (DPPH) radical scavenging, and inhibition of lipid oxidation. All hydrolyzed tissues displayed antioxidant capacity in all four assays, with colon, liver, and appendix as the three most potent inhibitors of lipid oxidation (47, 29, and 27 mmol/L trolox equivalent antioxidant capacity [TEAC], respectively) and liver, colon, pancreas, and appendix as the four most potent iron chelators (92% ± 1.1, 79.3% ± 3.2, 77.1% ± 1.8, and 77% ± 2.3, respectively). Furthermore, colon and appendix showed good radical scavenging capacities with ABTS scavenging of 86.4% ± 2.1 and 84.4% ± 2.9 and DPPH scavenging of 17.6% ± 0.3 and 17.1% ± 0.2, respectively. Our results provide new knowledge about the antioxidant capacity of a variety of animal by-products, which can be transformed into antioxidant hydrolysates, thereby creating added value
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