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1.
J Environ Manage ; 290: 112487, 2021 Jul 15.
Article in English | MEDLINE | ID: mdl-33873020

ABSTRACT

This paper presents the possibility of valorization of animal manure (camel and cow) by mixing it with agro-industrial biomass (cotton stalk and rapeseed oil cake) to produce pellets for use in power generation processes. Feedstocks were mixed in specific proportions based on certain assumptions concerning the energy and mechanical parameters of pellets. The assessment concerned both the combustion behavior as well as mechanical properties of four types of pellets derived from blends of animal manure and agro-industrial biomass. Thermogravimetry (TGA) and Differential Scanning Calorimetry (DSC) techniques are applied to analyze the reaction areas, characteristic temperatures as well as heat flow rates of raw materials and their blends. Results showed that addition of agro-industrial biomass (even 10%) to animal manure changed the specific combustion parameters: initiation and burn-out temperature and combustion time. For blends of cow manure (COM) and rapeseed oil cake (ROC), a reduction in the initiation temperature was achieved compared to the combustion of raw cow manure, and the combustion time increased by 1/3. In the case of camel manure (CAM) with the addition of cotton stalk (CS) the burn-out temperature and combustion time decreased. The addition of agro-biomass also causes a change in the heat release profiles, for the blends no pronounced DSC peaks are obtained in the area of devolatilization as it happens animal manure alone and in the area of fixed carbon combustion as for cotton stalk and rapeseed oil cake. The heat released from camel manure blends was 9.2-9.3 kJ/kg and from cow manure blends 10.2-10.4 kJ/kg. An evaluation of the physical and mechanical properties showed that all types of pellets at a moisture content of 10-15% have a similar drop strength in the range of 80-85%, while this strength decreases to 40-60% after the pellets have absorbed water.


Subject(s)
Lignin , Manure , Animals , Biomass , Thermogravimetry
2.
Exp Biol Med (Maywood) ; 231(8): 1439-47, 2006 Sep.
Article in English | MEDLINE | ID: mdl-16946413

ABSTRACT

The main objective of this investigation was to determine the influence of acute deficits of protein and energy on the blood levels of interleukin-10 (IL-10) and transforming growth factor-beta (TGF-beta), physiologically the main anti-inflammatory and tolerogenic cytokines. In four 14-day experiments, male and female C57BL/6J mice, initially 19 days old, consumed a complete purified diet either ad libitum or in restricted daily quantities, or had free access to an isocaloric purified low-protein diet. A zero-time control group (19 days old) was included. In the first two experiments, serum IL-10 levels were assessed by sandwich enzyme-linked immunosorbent assay (ELISA) and bioassay. The mean serum IL-10 bioactivities were higher (P < or = 0.05) in both malnourished groups (low-protein and restricted intake: 15.8 and 12.2 ng/ml, respectively) than in the zero-time and age-matched control groups (6.3 and 7.3 ng/ml, respectively), whereas serum IL-10 immunoactivity was high only in the restricted intake group (e.g., second experiment: 17.0 pg/ml vs. 5.4, 3.7, and 3.1 pg/ml in the zero-time control, age-matched control and low-protein group, respectively). The third and fourth experiments centered on plasma TGF-beta immunoactivity (sandwich ELISA) and bioactivity, respectively. The ELISA revealed a high mean plasma TGF-beta1 level (P < or = 0.05) in the low-protein group only, but TGF-beta bioactivity (beta1 isoform, although 15% beta2 in the restricted intake group) was high in both malnourished groups (8.7 and 9.3 ng/ml in the low-protein and restricted groups, respectively) relative to the age-matched control group (0.5 ng/ml). Thus, metabolically distinct weanling systems mimicking marasmus and incipient kwashiorkor both exhibit a blood cytokine profile that points to a tolerogenic microenvironment within immune response compartments. A model emerges in which malnutrition-associated immune competence, at least in advanced weight loss, centers on cytokine-mediated peripheral tolerance that reduces the risk of catabolically induced autoimmune disease, but this is at the cost of attenuated responsiveness to infectious agents.


Subject(s)
Deficiency Diseases/blood , Deficiency Diseases/immunology , Enzyme-Linked Immunosorbent Assay , Interleukin-10/blood , Transforming Growth Factor beta/blood , Animals , Enzyme-Linked Immunosorbent Assay/methods , Female , Food Deprivation/physiology , Humans , Male , Mice , Mice, Inbred C57BL , Protein Deficiency/blood , Protein Deficiency/immunology , Protein Isoforms/blood , Sensitivity and Specificity , Transforming Growth Factor beta1
3.
Protein Expr Purif ; 46(2): 390-400, 2006 Apr.
Article in English | MEDLINE | ID: mdl-16236525

ABSTRACT

Chicken major histocompatibility complex (MHC) B21 and B19 haplotypes are associated with resistance and susceptibility to Marek's disease (MD), respectively. T-cell-mediated immune response is crucial in coordinating protection against Marek's disease virus (MDV) infection, but it has been difficult to identify and characterize antigen-specific T-cells. MHC class II tetramers and oligomers have been widely used for characterization of antigen-specific T-cells in the context of infectious and autoimmune diseases. Thus, the objective of this study was to synthesize chicken MHC class II oligomers of B21 and B19 haplotypes for the future identification of antigen-specific T-cells. To achieve this objective, full-length coding sequences of chicken MHC class II B21 and B19 molecules were amplified and the molecules were expressed as fusion proteins, carrying Fos and Jun leucine zipper (LZ), histidine-tag and biotin ligase recognition site sequences, using a baculovirus expression system. Recombinant MHC-II were loaded with self-peptides, which stabilized the heterodimer in SDS-PAGE and allowed the detection of these molecules in Western blots with a conformation-specific anti-chicken MHC class II antibody. Biotinylated MHC molecules were conjugated to streptavidin to form oligomers, which were resolved under the transmission electron microscope through immuno-gold labelling, thus confirming success of oligomerization. In conclusion, chicken MHC class II oligomers may be used in the future to study the antigen-specific CD4+ T-cell compartment.


Subject(s)
Baculoviridae , Histocompatibility Antigens Class II/biosynthesis , Recombinant Fusion Proteins/biosynthesis , Animals , CD4-Positive T-Lymphocytes/immunology , Cell Line , Chickens/genetics , Genetic Predisposition to Disease/genetics , Haplotypes , Histocompatibility Antigens Class II/genetics , Histocompatibility Antigens Class II/immunology , Leucine Zippers/genetics , Marek Disease/genetics , Marek Disease/immunology , Proto-Oncogene Proteins c-fos/genetics , Proto-Oncogene Proteins c-jun/genetics , Recombinant Fusion Proteins/genetics , Recombinant Fusion Proteins/immunology , Spodoptera
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