<?xml version="1.0" encoding="ISO-8859-1"?><article xmlns:mml="http://www.w3.org/1998/Math/MathML" xmlns:xlink="http://www.w3.org/1999/xlink" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance">
<front>
<journal-meta>
<journal-id>2007-1124</journal-id>
<journal-title><![CDATA[Revista mexicana de ciencias pecuarias]]></journal-title>
<abbrev-journal-title><![CDATA[Rev. mex. de cienc. pecuarias]]></abbrev-journal-title>
<issn>2007-1124</issn>
<publisher>
<publisher-name><![CDATA[Instituto Nacional de Investigaciones Forestales, Agrícolas y Pecuarias]]></publisher-name>
</publisher>
</journal-meta>
<article-meta>
<article-id>S2007-11242020000300651</article-id>
<article-id pub-id-type="doi">10.22319/rmcp.v11i3.5214</article-id>
<title-group>
<article-title xml:lang="en"><![CDATA[Changes in myoglobin content in pork Longissimus thoracis muscle during freezing storage]]></article-title>
<article-title xml:lang="es"><![CDATA[Cambios en el contenido de mioglobina en el músculo porcino Longissimus thoracis durante el almacenamiento en congelación]]></article-title>
</title-group>
<contrib-group>
<contrib contrib-type="author">
<name>
<surname><![CDATA[Coria-Hernández]]></surname>
<given-names><![CDATA[Jonathan]]></given-names>
</name>
<xref ref-type="aff" rid="Aff"/>
</contrib>
<contrib contrib-type="author">
<name>
<surname><![CDATA[Meléndez-Pérez]]></surname>
<given-names><![CDATA[Rosalía]]></given-names>
</name>
<xref ref-type="aff" rid="Aff"/>
</contrib>
<contrib contrib-type="author">
<name>
<surname><![CDATA[Méndez-Albores]]></surname>
<given-names><![CDATA[Abraham]]></given-names>
</name>
<xref ref-type="aff" rid="Aff"/>
</contrib>
<contrib contrib-type="author">
<name>
<surname><![CDATA[Arjona-Román]]></surname>
<given-names><![CDATA[José Luis]]></given-names>
</name>
<xref ref-type="aff" rid="Aff"/>
</contrib>
</contrib-group>
<aff id="Af1">
<institution><![CDATA[,Universidad Nacional Autónoma de México Facultad de Estudios Superiores Cuautitlán Unidad de Investigación Multidisciplinaria]]></institution>
<addr-line><![CDATA[Cuautitlán Izcalli Estado de México]]></addr-line>
<country>Mexico</country>
</aff>
<pub-date pub-type="pub">
<day>00</day>
<month>09</month>
<year>2020</year>
</pub-date>
<pub-date pub-type="epub">
<day>00</day>
<month>09</month>
<year>2020</year>
</pub-date>
<volume>11</volume>
<numero>3</numero>
<fpage>651</fpage>
<lpage>668</lpage>
<copyright-statement/>
<copyright-year/>
<self-uri xlink:href="http://www.scielo.org.mx/scielo.php?script=sci_arttext&amp;pid=S2007-11242020000300651&amp;lng=en&amp;nrm=iso"></self-uri><self-uri xlink:href="http://www.scielo.org.mx/scielo.php?script=sci_abstract&amp;pid=S2007-11242020000300651&amp;lng=en&amp;nrm=iso"></self-uri><self-uri xlink:href="http://www.scielo.org.mx/scielo.php?script=sci_pdf&amp;pid=S2007-11242020000300651&amp;lng=en&amp;nrm=iso"></self-uri><abstract abstract-type="short" xml:lang="en"><p><![CDATA[Abstract In this study, pork Longissimus thoracis muscle was used, which was frozen in a chamber and thawed under controlled conditions. The color profile and the surface myoglobin were evaluated. A thermal analysis was performed by modulated differential scanning calorimetry (MDSC), and Fourier-transform infrared spectroscopy with attenuated total reflection (FTIR-ATR). It was found that there were important effects in myoglobin due to the freeze-thawing process in parameters such as pH, luminosity (L*), and chroma values, as well as in activation energies (Ea) and denaturation enthalpy (&#916;H) between myoglobin forms. In raw meat, it was found that there was a greater proportion of deoxymyoglobin, and in frozen-thawed samples, metmyoglobin was the most abundant form, indicating that are significant effects which are correlated with the changes in tri-stimulus coordinates and with the thermal and chemical parameters in pork meat.]]></p></abstract>
<abstract abstract-type="short" xml:lang="es"><p><![CDATA[Resumen En este estudio se utilizó el músculo porcino Longissimus thoracis, el cual se congeló en una cámara y descongeló bajo condiciones controladas. Se evaluó el perfil de color y la mioglobina superficial. Se realizó un análisis térmico mediante calorimetría diferencial de barrido modulada (MDSC) y espectroscopia de infrarrojo por transformada de Fourier con reflectancia total atenuada (FTIR-ATR). Se observaron efectos importantes en la mioglobina debido al proceso de congelación-descongelación en parámetros como el pH, la luminosidad (L*) y el índice de saturación, así como las energías de activación (Ea) y entalpía (&#916;H) de desnaturalización entre las formas de mioglobina. En la carne cruda se encontró una mayor proporción de desoximioglobina y en las muestras congeladas-descongeladas la metamioglobina era la forma más abundante, lo que indica que hay efectos significativos que se correlacionan con los cambios en las coordenadas triestímulo y con los parámetros térmicos y químicos en la carne de cerdo.]]></p></abstract>
<kwd-group>
<kwd lng="en"><![CDATA[Myoglobin]]></kwd>
<kwd lng="en"><![CDATA[Freezing-Thawing]]></kwd>
<kwd lng="en"><![CDATA[Pork Meat]]></kwd>
<kwd lng="en"><![CDATA[MDSC]]></kwd>
<kwd lng="en"><![CDATA[Color profile]]></kwd>
<kwd lng="en"><![CDATA[FTIR spectroscopy]]></kwd>
<kwd lng="es"><![CDATA[Mioglobina]]></kwd>
<kwd lng="es"><![CDATA[Congelación-descongelación]]></kwd>
<kwd lng="es"><![CDATA[Carne de cerdo]]></kwd>
<kwd lng="es"><![CDATA[MDSC]]></kwd>
<kwd lng="es"><![CDATA[Perfil de color]]></kwd>
<kwd lng="es"><![CDATA[FTIR]]></kwd>
<kwd lng="es"><![CDATA[Espectroscopia]]></kwd>
</kwd-group>
</article-meta>
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