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1.
Prep Biochem Biotechnol ; 54(4): 494-502, 2024 Apr.
Article in English | MEDLINE | ID: mdl-37607210

ABSTRACT

The production of Nisin, an FDA-approved food preservative, was attempted by Lactococcus lactis subsp. lactis ATCC® 11454 using the underutilized milk industry effluent, acid-whey, as a substrate. Nisin production was further improved by studying the effect of supplementation of nutrients and non-nutritional parameters. The addition of yeast extract (6% w/v) as nitrogen source and sucrose (4% w/v) as carbon source were found to be suitable nutrients for the maximum nisin production. The changes in the medium pH due to lactic acid accumulation during batch fermentation and its influence on the production of nisin were analyzed in the optimized whey medium (OWM). The production characteristics in OWM were further compared with the nisin production in MRS media. The influence of nisin as an inducer for its own production was also studied and found that the addition of nisin at 0.22 mg/ml promote the nisin production. The analysis of consumption of various metal ions present in the OWM during the nisin production was also analyzed, and found that the copper ions are the most consumed ion. The highest nisin yield of 2.6 × 105 AU/mL was obtained with OWM.


Subject(s)
Lactococcus lactis , Nisin , Nisin/metabolism , Whey/metabolism , Lactococcus lactis/metabolism , Whey Proteins , Fermentation , Dietary Supplements , Ions , Culture Media
2.
Appetite ; 192: 107097, 2024 01 01.
Article in English | MEDLINE | ID: mdl-37918526

ABSTRACT

Current research in food science has explored the influence of front-of-package (FOP) labeling systems on consumer decision-making, yielding mixed results. We suggest that these inconsistent findings regarding FOP labeling effectiveness stem from a failure to consider a pivotal individual-level variable: consumer susceptibility to FOP labeling (CSFL). In the present research, we define this focal construct and develop and psychometrically validate a seven-item instrument that captures the construct across six studies (N = 1134). The current research may assist in segmenting consumers based on their susceptibility to FOP labeling, thereby facilitating the creation of targeted interventions tailored to this individual difference. Notably, the CSFL scale is positively correlated with consumers' willingness to purchase food items with genuine, third-party FOP labels, but not products lacking labels or products with fictitious FOP labels. This supports the predictive validity of the scale in determining important consumption-related outcomes.


Subject(s)
Food Labeling , Food Preferences , Humans , Food Labeling/methods , Choice Behavior , Food , Consumer Behavior , Nutritive Value
3.
Environ Res ; 235: 116598, 2023 10 15.
Article in English | MEDLINE | ID: mdl-37451577

ABSTRACT

NixMg1-xFe2O4(x = 0, 0.2, 0.4, 0.6) nanoparticles were symphonized via combustion with microwave assistance in the presence of Tamarindus indica seeds extract as fuel. Nanoparticles nature, size, morphology, oxidation state, elemental composition, and optical and luminescence properties were analysed using PXRD, FTIR, SEM, EDX, and HRTEM with SAED, XPS, UV-Visible and photoluminescence spectroscopy. PXRD analysis confirms that synthesized nanoparticles are spinel cubic and have a 17-18 nm average crystalline size. Tetrahedral and octahedral sites regarding stretching vibrations were confirmed by FTIR analysis. SEM and HRTEM data it is disclosed that the morphology of synthesized nanoparticles has nano flakes-like structure with sponge-like agglomeration. Elemental compositions of prepared nanoparticles were confirmed through EDX spectroscopy. XPS Spectroscopy confirmed and revealed transition, oxidation states, and elemental composition. The band gap and absorption phenomenon were disclosed using UV-visible spectroscopy, where the band gap declines (2.1, 2, 1.6, 1.8 eV), with increase in nickel NixMg1-xFe2O4(x = 0, 0.2, 0.4, 0.6) doping. Photoluminescence intensity reduces with an incline in nickel doping, was confirmed and disclosed using photoluminescence spectroscopy. Dyes (Methylene blue and Rhodamine B) degradation activity was performed in the presence of NDMF nanoparticles as a photocatalyst, which disclosed that 98.1% of MB dye and 97.9% of RB dye were degraded in 0-120 min. Regarding initial dye concentration and catalyst load, 5 ppm was initiated as the ideal initial concentration for both RB and MB dyes. 50 mg catalyst dosage was found to be most effective for the degradation of MB and RB dyes. In comparison, pH studies revealed that photodegradation efficiency was higher in neutral (MB-98.1%, RB-97.9%) and basic (MB-99.6%, RB-99.3%) conditions than in acidic (MB-61.8%, RB-60.4%) conditions.


Subject(s)
Nanoparticles , Nickel , Magnesium , Microwaves , Nanoparticles/chemistry , Coloring Agents
4.
J Biol Chem ; 298(12): 102646, 2022 12.
Article in English | MEDLINE | ID: mdl-36309090

ABSTRACT

Iron (Fe) sequestration is one of the most important strategies of the host to control the growth and survival of invading pathogens. Ferritin (Ft) plays a pivotal role in the sequestration mechanism of mammalian hosts by storing Fe. Recent evidence suggests that poly(rC)-binding proteins (PCBPs) act as chaperones for loading Fe into Ft. Incidentally, modulation of host PCBPs in respect to storing Fe in Ft during any infection remains unexplored. Among PCBPs, PCBP1 and PCBP2 are present in every cell type and involved in interacting with Ft for Fe loading. Leishmania donovani (LD) resides within macrophages during the mammalian stage of infection, causing life-threatening visceral leishmaniasis. Here, we reveal the ability of LD to cleave PCBP1 and PCBP2 in host monocytes/macrophages. LD cleaves PCBP1-FLAG into two fragments and PCBP2-FLAG into multiple fragments, thus affecting their interactions with Ft and resulting in decreased Fe loading into Ft. LD-derived culture supernatant or exosome-enriched fractions are also able to cleave PCBPs, suggesting involvement of a secreted protease of the parasite. Using an immune-depletion experiment and transgenic mutants, we confirmed the involvement of zinc-metalloprotease GP63 in cleaving PCBPs. We further revealed that by cleaving host PCBPs, Leishmania could inhibit Fe loading into Ft to accumulate available Fe for higher intracellular growth. This is the first report of a novel strategy adopted by a mammalian pathogen to interfere with Fe sequestration into Ft by cleaving chaperones for its survival advantage within the host.


Subject(s)
Ferritins , Iron , Leishmania donovani , Leishmaniasis, Visceral , Molecular Chaperones , Animals , Ferritins/metabolism , Iron/metabolism , Leishmania donovani/metabolism , Macrophages/metabolism , Molecular Chaperones/metabolism , DNA-Binding Proteins/metabolism , Mice
5.
Cell Microbiol ; 20(7): e12834, 2018 07.
Article in English | MEDLINE | ID: mdl-29470856

ABSTRACT

Hepcidin mediated ferroportin (Fpn) degradation in macrophages is a well adopted strategy to limit iron availability towards invading pathogens. Leishmania donovani (LD), a protozoan parasite, resides within macrophage and competes with host for availing iron. Using in vitro and in vivo model of infection, we reveal that LD decreases Fpn abundance in host macrophages by hepcidin independent mechanism. Unaffected level of Fpn-FLAG in LD infected J774 macrophage confirms that Fpn down-regulation is not due its degradation. While increased Fpn mRNA but decreased protein expression in macrophages suggests blocking of Fpn translation by LD infection that is confirmed by 35 S-methionine labelling assay. We further reveal that LD blocks Fpn translation by induced binding of iron regulatory proteins (IRPs) to the iron responsive element present in its 5'UTR. Supershift analysis provides evidence of involvement of IRP2 particularly during in vivo infection. Accordingly, a significant increase in IRP2 protein expression with simultaneous decrease in its stability regulator F-box and leucine-rich repeat Protein 5 (FBXL5) is detected in splenocytes of LD-infected mice. Increased intracellular growth due to compromised expressions of Fpn and FBXL5 by specific siRNAs reveals that LD uses a novel strategy of manipulating IRP2-FBXL5 axis to inhibit host Fpn expression.


Subject(s)
Cation Transport Proteins/antagonists & inhibitors , F-Box Proteins/metabolism , Host-Pathogen Interactions , Iron Regulatory Protein 2/metabolism , Leishmania donovani/growth & development , Leishmaniasis, Visceral/pathology , Macrophages/parasitology , Animals , Cation Transport Proteins/biosynthesis , Cell Line , Disease Models, Animal , Female , Gene Expression Regulation , Immune Evasion , Leishmania donovani/pathogenicity , Leishmaniasis, Visceral/immunology , Leishmaniasis, Visceral/parasitology , Macrophages/immunology , Mice, Inbred BALB C , Models, Biological , Protein Biosynthesis
6.
J Biol Chem ; 290(12): 7634-46, 2015 Mar 20.
Article in English | MEDLINE | ID: mdl-25572399

ABSTRACT

Adequate availability of iron is important for cellular energy metabolism. Catecholamines such as epinephrine and norepinephrine promote energy expenditure to adapt to conditions that arose due to stress. To restore the energy balance, epinephrine/norepinephrine-exposed cells may face higher iron demand. So far, no direct role of epinephrine/norepinephrine in cellular iron homeostasis has been reported. Here we show that epinephrine/norepinephrine regulates iron homeostasis components such as transferrin receptor-1 and ferritin-H in hepatic and skeletal muscle cells by promoting the binding of iron regulatory proteins to iron-responsive elements present in the UTRs of transferrin receptor-1 and ferritin-H transcripts. Increased transferrin receptor-1, decreased ferritin-H, and increased iron-responsive element-iron regulatory protein interaction are also observed in liver and muscle tissues of epinephrine/norepinephrine-injected mice. We demonstrate the role of epinephrine/norepinephrine-induced generation of reactive oxygen species in converting cytosolic aconitase (ACO1) into iron regulatory protein-1 to bind iron-responsive elements present in UTRs of transferrin receptor-1 and ferritin-H. Our study further reveals that mitochondrial iron content and mitochondrial aconitase (ACO2) activity are elevated by epinephrine/norepinephrine that are blocked by the antioxidant N-acetyl cysteine and iron regulatory protein-1 siRNA, suggesting involvement of reactive oxygen species and iron regulatory protein-1 in this mechanism. This study reveals epinephrine and norepinephrine as novel regulators of cellular iron homeostasis.


Subject(s)
Catecholamines/physiology , Energy Metabolism , Homeostasis , Iron-Regulatory Proteins/physiology , Iron/metabolism , RNA Processing, Post-Transcriptional , Animals , Cell Line, Tumor , DNA Primers , Humans , Liver/cytology , Liver/metabolism , Mice , Muscle, Skeletal/cytology , Muscle, Skeletal/metabolism
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