O presente estudo teve como objetivo avaliar a utilização de campo magnético pulsado (CMP) de baixa intensidade na preservação da qualidade microbiológica, cor e estabilidade oxidativa de carne bovina moída durante armazenamento aeróbio refrigerado. Amostras moídas de peixinho bovino (músculo Supraspinatus) foram expostas a CMP por 2 horas às frequências de 1, 30 ou 60 Hz ou, em outra etapa, expostas a CMP de 1 Hz de frequência por 2 horas ou continuamente por 12 dias. Amostras controle não foram expostas ao CMP. As amostras foram armazenadas a 4ºC por até 12 dias, e avaliadas a cada seis dias por meio de análise microbiológica de contagem total de bactérias mesófilas aeróbias, e a cada dois dias por meio de análises físico-químicas e bioquímicas: pH, cor instrumental (escala CIELAB), mioglobina e oxidação lipídica. A exposição ao CMP de 1 Hz por 2 horas reduziu a contagem de mesófilos aeróbios com relação ao controle em 1,3 ciclos logarítmicos no 12º dia de armazenamento refrigerado. Os conteúdos de metamioglobina das amostras expostas por 2 horas ao CMP, independente da frequência de pulso, foram significativamente menores com relação ao controle no 6º dia de armazenamento refrigerado. Os demais parâmetros de qualidade não sofreram alteração significativa com relação ao controle durante o armazenamento e não foi verificado efeito das diferentes frequências de CMP. Conclui-se que campo magnético pulsado de baixa intensidade (ordem de mili Tesla) apresenta potencial para ser utilizado como tecnologia inovadora, em combinação com a refrigeração, na preservação de carnes frescas. Todavia, mais estudos são necessários para melhor entendimento dos mecanismos de ação de campo magnético, principalmente em alimentos. / This study aimed to evaluate the use of low intensity pulsed magnetic field (PMF) in the preservation of microbiological quality, color and oxidative stability of ground beef during aerobic refrigerated storage. Ground beef samples of chuck tender (Supraspinatus muscle) were exposed to PMF for 2 hours at frequencies of 1, 30 and 60 Hz or, in another step, they were exposed to a 1 Hz PMF for 2 hours or continuously for 12 days. Control samples were not exposed to PMF. Samples were stored at 4ºC for up to 12 days, and evaluated every six days through microbiological analysis of total aerobic mesophilic bacteria count, and every two days through physicochemical and biochemical analysis of pH, instrumental color (CIELAB scale), myoglobin and lipid oxidation. Exposure to 1 Hz PMF for 2 hours reduced the growth of aerobic mesophiles in relation to the control by 1.3 logarithmic cycles in the 12th day of refrigerated storage. Metmyoglobin content of samples exposed to the PMF for 2 hours, regardless of the pulse frequency, were significantly lower compared to the control in the 6th day of refrigerated storage. The other quality parameters did not change significantly during storage compared to the control and it was not observed effect of different PMF frequencies. We concluded that low intensity pulsed magnetic field (order of mili Tesla) has the potential to be used as innovative technology, in combination with refrigeration, in fresh meat preservation. However, more studies are needed to better understand the mechanisms of action of magnetic field, mainly in foods.

Red bright color is an important quality attribute that influences beef purchasing and is affected by beef pH. Therefore, the aim of this study was to determine if high ultimate pH affected color stability of longissimus lumborum (LL) steaks from pasture-fed Nellore bulls and if HiOx atmosphere package improved the color stability of high pHu muscles. To achieve these objectives, 18 LL muscles from Nellore bulls were grouped into 3 pHu ranges: normal (n = 6; 5.40 < pHu <5.79), intermediate (n = 6; 5.80 < pHu <6.19) and high (n = 6; pHu > 6.20). All the muscles were cut into 2.5 cm steaks and packaged in 80% O2/ 20% CO2 (v/v) and then stored at 2 ± 1 ºC under dark conditions until day 5 and under fluorescent light until day 14 (the end of display-time). pH, gas composition, instrumental color, surface pigment, metmyoglobin reducing activity (MRA), oxygen consumption rate (OCR), and lipid oxidation were determined throughout display-time. High pHu steaks were darker (L*), redder (a*, a*/b*), with better tone (Hue), less metmyoglobin and higher MRA (p < 0.05) than normal pHu samples. HiOX MAP increased surface OMb during display time in pHu > 6.2 (p < 0.05), showing a bright-red color in high group. Intermediate group was less dark than high group and had longer color stability than normal group (p < 0.05). Therefore, High pHu had great color and lipid oxidation stability and desired color due to HiOx MAP under cold storage for 14 days and intermediate pHu had beneficial aspects presented in both other treatments. / A cor vermelho-brilhante da carne bovina é um atributo de qualidade essencial considerado no momento de compra pelo consumidor, sendo intrinsecamente afetada pelo pH final (pHf) da carne. Assim, esse trabalho objetivou determinar se o pHf alto da carne afetou a estabilidade de carne do músculo Longissimus lumborum (LL) de bovinos da raça Nelore macho inteiro criado a pasto e se a embalagem com atmosfera modificada com alta concentração de oxigênio melhorou a estabilidade de cor da carne com pHf alto. Para isso, 18 músculos LL de Nelore machos inteiros criados a pasto foram classificadas em 3 faixas de pHf: normal (n = 6; 5.40 < pHu <5.79), intermediário (n = 6; 5.80 < pHu <6.19) e alto (n = 6; pHu > 6.20), 48h pós abate. Todos os músculos foram então porcionados em bifes com 2,5 cm de espessura 72h pós abate, os quais foram embalados em atmosfera composta por 80 % O2/ 20% CO2 (v/v), sendo finalmente armazenados a 2 ± 1 ºC no escuro até o 5º dia de tempo de exposição. No 5º dia, as amostras iniciaram a exposição à luz fluorescente até o dia 14 do período. As análises de pH, composição gasosa das embalagens, cor instrumental, pigmentos superficiais, atividade redutora da metamioglobina (ARM), taxa de consume de oxigênio (TCO) e oxidação lipídica foram realizadas ao longo do tempo de exposição. Os bifes com pHf alto apresentaram cor mais escura (L*), vermelha (a*, a*/b*), com melhor tonalidade (hue), menor metamioglobina superficial e maior ARM (p < 0.05). A embalagem com alta concentração de oxigênio aumentou a proporção de oximioglobina (OMB) superficial ao longo do tempo de exposição (p < 0.05), evidenciando uma cor vermelho-brilhante no grupo alto. O grupo Intermediário se mostrou menos escuro o grupo alto e mais prolongada estabilidade de cor que o grupo normal (p < 0.05). Assim, considera-se que a pHf alto afetou a estabilidade de cor e de oxidação lipídica dos músculos e a coloração do grupo alto foi melhorada pela ação da embalagem com oxigênio. O pH Intermediário se mostrou vantajoso por apresentar benefícios presentes nos dois outros tratamentos.

Red bright color is an important quality attribute that influences beef purchasing and is affected by beef pH. Therefore, the aim of this study was to determine if high ultimate pH affected color stability of longissimus lumborum (LL) steaks from pasture-fed Nellore bulls and if HiOx atmosphere package improved the color stability of high pHu muscles. To achieve these objectives, 18 LL muscles from Nellore bulls were grouped into 3 pHu ranges: normal (n = 6; 5.40 < pHu <5.79), intermediate (n = 6; 5.80 < pHu <6.19) and high (n = 6; pHu > 6.20). All the muscles were cut into 2.5 cm steaks and packaged in 80% O2/ 20% CO2 (v/v) and then stored at 2 ± 1 ºC under dark conditions until day 5 and under fluorescent light until day 14 (the end of display-time). pH, gas composition, instrumental color, surface pigment, metmyoglobin reducing activity (MRA), oxygen consumption rate (OCR), and lipid oxidation were determined throughout display-time. High pHu steaks were darker (L*), redder (a*, a*/b*), with better tone (Hue), less metmyoglobin and higher MRA (p < 0.05) than normal pHu samples. HiOX MAP increased surface OMb during display time in pHu > 6.2 (p < 0.05), showing a bright-red color in high group. Intermediate group was less dark than high group and had longer color stability than normal group (p < 0.05). Therefore, High pHu had great color and lipid oxidation stability and desired color due to HiOx MAP under cold storage for 14 days and intermediate pHu had beneficial aspects presented in both other treatments. / A cor vermelho-brilhante da carne bovina é um atributo de qualidade essencial considerado no momento de compra pelo consumidor, sendo intrinsecamente afetada pelo pH final (pHf) da carne. Assim, esse trabalho objetivou determinar se o pHf alto da carne afetou a estabilidade de carne do músculo Longissimus lumborum (LL) de bovinos da raça Nelore macho inteiro criado a pasto e se a embalagem com atmosfera modificada com alta concentração de oxigênio melhorou a estabilidade de cor da carne com pHf alto. Para isso, 18 músculos LL de Nelore machos inteiros criados a pasto foram classificadas em 3 faixas de pHf: normal (n = 6; 5.40 < pHu <5.79), intermediário (n = 6; 5.80 < pHu <6.19) e alto (n = 6; pHu > 6.20), 48h pós abate. Todos os músculos foram então porcionados em bifes com 2,5 cm de espessura 72h pós abate, os quais foram embalados em atmosfera composta por 80 % O2/ 20% CO2 (v/v), sendo finalmente armazenados a 2 ± 1 ºC no escuro até o 5º dia de tempo de exposição. No 5º dia, as amostras iniciaram a exposição à luz fluorescente até o dia 14 do período. As análises de pH, composição gasosa das embalagens, cor instrumental, pigmentos superficiais, atividade redutora da metamioglobina (ARM), taxa de consume de oxigênio (TCO) e oxidação lipídica foram realizadas ao longo do tempo de exposição. Os bifes com pHf alto apresentaram cor mais escura (L*), vermelha (a*, a*/b*), com melhor tonalidade (hue), menor metamioglobina superficial e maior ARM (p < 0.05). A embalagem com alta concentração de oxigênio aumentou a proporção de oximioglobina (OMB) superficial ao longo do tempo de exposição (p < 0.05), evidenciando uma cor vermelho-brilhante no grupo alto. O grupo Intermediário se mostrou menos escuro o grupo alto e mais prolongada estabilidade de cor que o grupo normal (p < 0.05). Assim, considera-se que a pHf alto afetou a estabilidade de cor e de oxidação lipídica dos músculos e a coloração do grupo alto foi melhorada pela ação da embalagem com oxigênio. O pH Intermediário se mostrou vantajoso por apresentar benefícios presentes nos dois outros tratamentos.

<p>In the present thesis the density functional B3LYP has been used to study reactions of NO and O₂ in redox active enzymes.</p><p>Reduction of nitric oxide (NO) to nitrous oxide (N₂O) is an important part in the bacterial energy conservation (denitrification). The reduction of NO in three different bimetallic active sites leads to the formation of hyponitrous acid anhydride (N₂O₂^2-). The stability of this intermediate is crucial for the reaction rate. In the two diiron systems, respiratory and scavenging types of NOR, it is possible to cleave the N-O bond, forming N₂O, without any extra protons or electrons. In a heme-copper oxidase, on the other hand, both a proton and an electron are needed to form N₂O.</p><p>In addition to being an intermediate in the denitrification, NO is a toxic agent. Myoglobin in the oxy-form reacts with NO forming nitrate (NO₃ ^-) at a high rate, which should make this enzyme an efficient NO scavenger. Peroxynitrite (ONOO^-) is formed as a short-lived intermediate and isomerizes to nitrate through a radical reaction.</p><p>In the mechanism for pumping protons in cytochrome oxidase, thermodynamics, rather than structural changes, might guide protons to the heme propionate for further translocation.</p><p>The dioxygenation of arachidonic acid in prostaglandin endoperoxide H synthase forms the bicyclic prostaglandin G₂, through a cascade of radical reactions. The mechanism proposed by Hamberg and Samuelsson is energetically feasible.</p>

<p>In this thesis, the structure and stability of globular proteins adsorbed onto nanometer-sized hydrophilic silica particles were investigated using differential scanning calorimetry (DSC), hydrogen/deuterium exchange (HDX), and mass spectrometry (MS). The adsorption process itself was characterized with fluorescence and absorption spectroscopy and surface plasmon resonance (SPR). The combination of these methods offered a unique insight into adsorption-induced changes within proteins related to their adsorption characteristics. DSC contributed with thermodynamic information on the overall structural stability within the protein population. HDX in combination with MS contributed information on the structure and stability of adsorbed proteins with focus on changes within the secondary structure elements. In order to increase the structural resolution in this part of the investigation, proteolysis was performed prior to the MS analyzing step. Knowledge on the protein adsorption process was utilized in a practical approach called ligand fishing. In this approach, SPR was used to monitor the chip-based affinity purification of a protein with MS used for protein identification.</p><p>Adsorption isotherms revealed that electrostatic interactions play an important role in the adsorption of proteins to hydrophilic surfaces. DSC investigation revealed that the thermal stability of proteins reduces with increasing electrostatic attraction between the protein and the surface and that this effect diminishes at higher surface coverage. The mass-increase due to exchange between protein hydrogen atoms and deuterium atoms in solution was investigated as a function of time. This gave insight into adsorption-induced changes in the structural stability of proteins. By combining DSC and HDX-MS, it was possible to differentiate between adsorption-induced changes in the secondary and tertiary structure. Additionally, if limited proteolysis was performed, the investigations gave insight into the orientation and protein segment specific changes in the stability of proteins adsorbed to silica surfaces. The adsorption of proteins to silica particles also provided the basis for a new experimental design that allows handling of minute amounts of proteins in a ligand fishing application, as used in the field of functional proteomics.</p>

In this thesis, the structure and stability of globular proteins adsorbed onto nanometer-sized hydrophilic silica particles were investigated using differential scanning calorimetry (DSC), hydrogen/deuterium exchange (HDX), and mass spectrometry (MS). The adsorption process itself was characterized with fluorescence and absorption spectroscopy and surface plasmon resonance (SPR). The combination of these methods offered a unique insight into adsorption-induced changes within proteins related to their adsorption characteristics. DSC contributed with thermodynamic information on the overall structural stability within the protein population. HDX in combination with MS contributed information on the structure and stability of adsorbed proteins with focus on changes within the secondary structure elements. In order to increase the structural resolution in this part of the investigation, proteolysis was performed prior to the MS analyzing step. Knowledge on the protein adsorption process was utilized in a practical approach called ligand fishing. In this approach, SPR was used to monitor the chip-based affinity purification of a protein with MS used for protein identification. Adsorption isotherms revealed that electrostatic interactions play an important role in the adsorption of proteins to hydrophilic surfaces. DSC investigation revealed that the thermal stability of proteins reduces with increasing electrostatic attraction between the protein and the surface and that this effect diminishes at higher surface coverage. The mass-increase due to exchange between protein hydrogen atoms and deuterium atoms in solution was investigated as a function of time. This gave insight into adsorption-induced changes in the structural stability of proteins. By combining DSC and HDX-MS, it was possible to differentiate between adsorption-induced changes in the secondary and tertiary structure. Additionally, if limited proteolysis was performed, the investigations gave insight into the orientation and protein segment specific changes in the stability of proteins adsorbed to silica surfaces. The adsorption of proteins to silica particles also provided the basis for a new experimental design that allows handling of minute amounts of proteins in a ligand fishing application, as used in the field of functional proteomics.

In the present thesis the density functional B3LYP has been used to study reactions of NO and O2 in redox active enzymes. Reduction of nitric oxide (NO) to nitrous oxide (N2O) is an important part in the bacterial energy conservation (denitrification). The reduction of NO in three different bimetallic active sites leads to the formation of hyponitrous acid anhydride (N2O22-). The stability of this intermediate is crucial for the reaction rate. In the two diiron systems, respiratory and scavenging types of NOR, it is possible to cleave the N-O bond, forming N2O, without any extra protons or electrons. In a heme-copper oxidase, on the other hand, both a proton and an electron are needed to form N2O. In addition to being an intermediate in the denitrification, NO is a toxic agent. Myoglobin in the oxy-form reacts with NO forming nitrate (NO3 -) at a high rate, which should make this enzyme an efficient NO scavenger. Peroxynitrite (ONOO-) is formed as a short-lived intermediate and isomerizes to nitrate through a radical reaction. In the mechanism for pumping protons in cytochrome oxidase, thermodynamics, rather than structural changes, might guide protons to the heme propionate for further translocation. The dioxygenation of arachidonic acid in prostaglandin endoperoxide H synthase forms the bicyclic prostaglandin G2, through a cascade of radical reactions. The mechanism proposed by Hamberg and Samuelsson is energetically feasible.

Submitted by JULIANA APARECIDA CERQUEIRA null (julianacerqueira.vet@gmail.com) on 2017-08-16T14:34:40Z No. of bitstreams: 1 Dissertação PDF.pdf: 1523644 bytes, checksum: 34b73cfc23737b94845062cc56505e49 (MD5) / Approved for entry into archive by Monique Sasaki (sayumi_sasaki@hotmail.com) on 2017-08-22T20:39:49Z (GMT) No. of bitstreams: 1 cerqueira_ja_me_jabo.pdf: 1523644 bytes, checksum: 34b73cfc23737b94845062cc56505e49 (MD5) / Made available in DSpace on 2017-08-22T20:39:49Z (GMT). No. of bitstreams: 1 cerqueira_ja_me_jabo.pdf: 1523644 bytes, checksum: 34b73cfc23737b94845062cc56505e49 (MD5) Previous issue date: 2017-07-28 / Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq) / As principais alterações fisiológicas ou patológicas induzidas pelo exercício que ocorrem na musculatura esquelética ou cardíaca podem ser identificadas por meio de biomarcadores séricos. Consolidados em atletas da espécie humana e equina, são praticamente inexistentes em cães estudos sobre a dinâmica destes biomarcadores relacionados com a prática de exercício máximo e treinamento. Objetivou-se determinar a cinética dos biomarcadores séricos musculares creatina quinase (CK), aspartato aminotransferase (AST), mioglobina; e cardíacos, troponina cardíaca I (cTnI) e creatina quinase isoenzima MB (CK-MB) de cães submetidos a esforço intenso e condicionamento aeróbio. A ação da venopunção sobre os biomarcadores também foi avaliada. Foram utilizados 18 cães hígidos da raça Beagle distribuídos em três grupos: sedentário (S), não treinado (NT) e treinado (T). Os cães foram submetidos a dois testes de esforço incremental (TEI-1 e TEI-2) para obtenção da curva lactato-velocidade (CLV). Verificou-se se a CLV teve modelo exponencial. O programa de treinamento foi realizado em esteira por 8 semanas na velocidade relacionada a 70-80 % do limiar de lactato (VLL). Determinou-se a velocidade correspondente a frequência cardíaca no momento da fadiga (VFCFadiga). Os biomarcadores séricos foram quantificados nos momentos basal, antes e 1, 6, 12, 24, 48 e 72 h após os TEIs. Aplicou-se análise de variância de dois fatores para amostras repetidas no tempo seguida por teste de Tukey e correlação de Pearson (P≤0,05). Elevação (P≤0,05) das velocidades correspondentes a VLL e VFCFadiga evidenciou melhora da aptidão aeróbia do grupo T. Observou-se aumento (P≤0,05) na atividade sérica de CK e AST, com valores máximos após 6 h em ambos os TEIs, com retorno aos valores basais após 12-24 h. Em conjunto, a avaliação do comportamento dos biomarcadores musculares revelou recuperação do tecido muscular após os TEIs. A cTnI e a mioglobina não se alteraram. A CK-MB apresentou pico de elevação (P≤0,05) após 1 h e retorno aos valores basais após 12 h em ambos os TEIs, apontando ausência de lesões musculares cardíacas. Observou-se forte correlação entre CK-AST (P=0,849) e correlação moderada entre CK-CK-MB (0,493) e AST-CK-MB (0,501). Parece que as atividades séricas da CK e AST podem sofrer interferência da venopunção jugular. Conclui-se que o exercício intenso provocou aumento fisiológico das atividades séricas das enzimas musculares e cardíacas com rápida recuperação, sem indicativo de lesões. O protocolo de condicionamento físico melhorou o rendimento dos cães, mas não influenciou a atividade sérica das enzimas musculares e cardíacas. Para o monitoramento desportivo em cães a CK-MB foi o biomarcador mais confiável. / The main physiological or pathological alterations induced by exercise on skeletal or cardiac musculature can be identified using serum biomarkers. While studies on the dynamics of such biomarkers are consolidated in humans and horses, they are virtually inexistent on maximum exercise and training among dogs. This study aimed to determine the kinetics of the muscle serum biomarkers creatine kinase (CK), aspartate aminotransferase (AST), and myoglobin and of cardiac biomarkers cardiac troponin I (cTnI) and creatine kinase isoenzyme MB (CK-MB) of dogs subjected to intense effort and aerobic conditioning. The effect of venipuncture on the biomarkers was also assessed. Eighteen healthy Beagle dogs were assigned to three groups: sedentary (S), untrained (U), and trained (T). The dogs were subjected to two incremental effort tests (IET-1 and IET-2) so that their lactate vs. velocity curve (LVC) could be obtained. It was verified whether LVC followed an exponential model. The eight-week training program was carried out on a treadmill with speed set to 70-80% of the velocity at lactate threshold (VLT). The velocity corresponding to the heart rate at the moment of fatigue (VHRFatigue) was determined. Serum biomarkers were quantified at the baseline, before, and 1, 6, 12, 24, 48, and 72 h after the IETs. Two-factor analysis of variance was applied for samples repeated over time followed by Tukey’s test and Pearson correlation (P≤0.05). The increase (P≤0.05) in the velocyties corresponding to VLT and VHRFatigue indicated an improvement in aerobic fitness of group T. Serum activity of CK and AST increased (P≤0.05), reached maximum values after 6 h in both IETs, and returned to baseline levels after 12-24 h. As a whole, the assessment of the behavior of muscle biomarkers showed recovery of muscle tissues after the IETs. Levels of cTnI and myoglobin were unaltered. Peak CK-MB (P≤0.05) was observed 1 h into the IETs and returned to baseline levels 12 h after they finished, indicating no cardiac muscle lesions. A strong correlation between CK and AST (P=0.849) and moderate correlations between CK and CK-MB (0.493) and AST and CK-MB were observed. Apparently, serum activities of CK and AST may be impacted by jugular venipuncture. It is concluded that intense exercise led to a physiological increase in serum activities of muscle and cardiac enzymes with rapid recovery and no apparent lesions. The physical conditioning protocol improved the performance of the dogs, but did not impact the serum activity of muscle and cardiac enzymes. CK-MB was the most reliable sports monitoring biomarker in dogs. / CNPq: 132811/2016-2

O ferro (Fe) é um oligoelemento capaz de aceitar e doar elétrons. Tal propriedade o torna extremamente útil em diversos componentes importantes ao bom funcionamento do organismo e da célula. O Fe está associado a algumas proteínas, está presente em citocromos, em moléculas que se ligam ao oxigênio (hemoglobina e mioglobina) e em uma grande variedade de enzimas. O aumento e a diminuição da sua oferta levam a alterações na expressão de RNAs mensageiros e proteínas responsáveis pela sua própria homeostase. Sabe-se que a expressão de vários genes envolvidos no metabolismo do Fe é regulada pós-transcricionalmente, por meio de mecanismo que é desencadeado por sua ligação em regiões não traduzíveis presentes em mRNAs específicos, o que interfere no seu grau de poliadenilação, e por conseguinte, na estabilidade e na tradução do transcrito. A Mb é uma heme-proteína de 18,8 kDa, altamente expressa no tecido muscular esquelético e cardíaco, e que pertence a mesma família da hemoglobina. Sabendo-se que cerca de 15% do Fe existente no organismo está presente nos músculos, no presente trabalho avaliamos se a suplementação e restrição de Fe, a curto e longo prazo, alteram a expressão gênica da Mb no músculo oxidativo Soleus (S), glicolítico Extensor Digital Longo (EDL) e no cardíaco. Observamos que a restrição de Fe, a longo prazo, provocou um aumento na expressão gênica e protéica da Mb, apenas no músculo Soleus, sem alterar o grau de poliadenilação do transcrito, enquanto a suplementação não alterou os parâmetros avaliados em nenhum dos tecidos. A administração aguda de Fe não alterou a expressão gênica e protéica da Mb, nem o grau de poliadenilação do transcrito em nenhum dos tecidos estudados. Estes resultados sugerem que a regulação da expressão da Mb pelo Fe se dá apenas transcricionalmente, e de maneira tecido específica. / Iron is a trace element that can accept and donate electrons. This property makes iron extremely important to several components involved with the proper functioning of the organism and cells. Iron is associated with some proteins, is present in cytochromes, molecules that bind to oxygen (hemoglobin and myoglobin) and a variety of enzymes. The increase and decrease of its offer lead to changes in the expression of mRNAs and proteins responsible for their own homeostasis. It is known that the expression of several genes involved in the metabolism of iron is regulated post-transcriptionally through a mechanism that is triggered by its binding in non-translatable regions of specific mRNAs, which interferes with their polyadenylation, and as a consequence, with the stability and translation of the transcripts. Mb is a heme-protein with 18,8 kDa, highly expressed in skeletal and cardiac muscle, and it belongs to the same family of hemoglobin. About 15% of iron in the body is present in muscle tissue. Thus, this study aimed to investigate if long- and short-term Fe supplementation and restriction affect Mb gene expression in the oxidative Soleus (S), glycolitic Extensorum Digitalis Longus (EDL), and cardiac muscles. It was shown that long- term Fe restriction increased Mb mRNA and protein expression only in S muscle, without interfering in the transcript polyadenylation, whereas Fe supplementation did not alter any parameter evaluated in the three tissues. The short-term iron administration did not change the Mb mRNA, polyadenylation and protein expression in any of the tissues studied. The present results indicate that the regulation of Mb gene expression by iron occurs only at transcriptional level and in a tissue specific manner.

O presente estudo teve como objetivo avaliar a utilização de campo magnético pulsado (CMP) de baixa intensidade na preservação da qualidade microbiológica, cor e estabilidade oxidativa de carne bovina moída durante armazenamento aeróbio refrigerado. Amostras moídas de peixinho bovino (músculo Supraspinatus) foram expostas a CMP por 2 horas às frequências de 1, 30 ou 60 Hz ou, em outra etapa, expostas a CMP de 1 Hz de frequência por 2 horas ou continuamente por 12 dias. Amostras controle não foram expostas ao CMP. As amostras foram armazenadas a 4ºC por até 12 dias, e avaliadas a cada seis dias por meio de análise microbiológica de contagem total de bactérias mesófilas aeróbias, e a cada dois dias por meio de análises físico-químicas e bioquímicas: pH, cor instrumental (escala CIELAB), mioglobina e oxidação lipídica. A exposição ao CMP de 1 Hz por 2 horas reduziu a contagem de mesófilos aeróbios com relação ao controle em 1,3 ciclos logarítmicos no 12º dia de armazenamento refrigerado. Os conteúdos de metamioglobina das amostras expostas por 2 horas ao CMP, independente da frequência de pulso, foram significativamente menores com relação ao controle no 6º dia de armazenamento refrigerado. Os demais parâmetros de qualidade não sofreram alteração significativa com relação ao controle durante o armazenamento e não foi verificado efeito das diferentes frequências de CMP. Conclui-se que campo magnético pulsado de baixa intensidade (ordem de mili Tesla) apresenta potencial para ser utilizado como tecnologia inovadora, em combinação com a refrigeração, na preservação de carnes frescas. Todavia, mais estudos são necessários para melhor entendimento dos mecanismos de ação de campo magnético, principalmente em alimentos. / This study aimed to evaluate the use of low intensity pulsed magnetic field (PMF) in the preservation of microbiological quality, color and oxidative stability of ground beef during aerobic refrigerated storage. Ground beef samples of chuck tender (Supraspinatus muscle) were exposed to PMF for 2 hours at frequencies of 1, 30 and 60 Hz or, in another step, they were exposed to a 1 Hz PMF for 2 hours or continuously for 12 days. Control samples were not exposed to PMF. Samples were stored at 4ºC for up to 12 days, and evaluated every six days through microbiological analysis of total aerobic mesophilic bacteria count, and every two days through physicochemical and biochemical analysis of pH, instrumental color (CIELAB scale), myoglobin and lipid oxidation. Exposure to 1 Hz PMF for 2 hours reduced the growth of aerobic mesophiles in relation to the control by 1.3 logarithmic cycles in the 12th day of refrigerated storage. Metmyoglobin content of samples exposed to the PMF for 2 hours, regardless of the pulse frequency, were significantly lower compared to the control in the 6th day of refrigerated storage. The other quality parameters did not change significantly during storage compared to the control and it was not observed effect of different PMF frequencies. We concluded that low intensity pulsed magnetic field (order of mili Tesla) has the potential to be used as innovative technology, in combination with refrigeration, in fresh meat preservation. However, more studies are needed to better understand the mechanisms of action of magnetic field, mainly in foods.