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            <subfield code="a">TAZ-TFG-2015-011</subfield>
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        <datafield tag="041" ind1=" " ind2=" ">
            <subfield code="a">eng</subfield>
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        <datafield tag="100" ind1="1" ind2=" ">
            <subfield code="a">ROMEO OLIVÁN, ANA</subfield>
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        <datafield tag="245" ind1="0" ind2="0">
            <subfield code="a">CARACTERIZACIÓN Y EXTRACCIÓN DE LA LISOZIMA DE LA CLARA DE HUEVO</subfield>
        </datafield>
        <datafield tag="260" ind1=" " ind2=" ">
            <subfield code="a">Zaragoza</subfield>
            <subfield code="b">Universidad de Zaragoza</subfield>
            <subfield code="c">2015</subfield>
        </datafield>
        <datafield tag="506" ind1=" " ind2=" ">
            <subfield code="a">by-nc-sa</subfield>
            <subfield code="b">Creative Commons</subfield>
            <subfield code="c">3.0</subfield>
            <subfield code="u">http://creativecommons.org/licenses/by-nc-sa/3.0/</subfield>
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        <datafield tag="520" ind1=" " ind2=" ">
            <subfield code="a">Lysozyme is a small protein (14kDa) that occurs in almost all body fluids, and tissues of animal organisms. It exhibits bacteriolytic activity due to its ability of breaking bacterial cell walls. The demand of this enzyme has increased because of its diverse uses in pharmacy or food industry. Different methods for isolation have been proposed. Most of them are used in laboratory practice to obtain the pure enzyme of high activity, however only some of these methods are feasible on a commercial scale. The most useful method of lysozyme extraction are chromatography tecnhniques. Other methods, such as crystallization, aqueous two-phase extraction or membrane filtration, have also been reported. In this work, we studied a two-step protocol for the lysozyme extraction from chicken egg white, based on a protein precipitation coupled with chromatography. Three precipitation agents (polyethilenglycol, ammonium sulfate and sodium chloride) and four types of chromatography (cation-exchange chromatography, hydrophobic interaction chromatography, gel filtration chromatography and affinity chromatography) were assayed to determine the efficiency of each methodology. The most efficient methodology was the combination of protein precipitation using 3% polyethilenglycol and ion exchange chromatography, obtaining lysozyme of great purity and the activity was as high as 72 U/ml</subfield>
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        <datafield tag="521" ind1=" " ind2=" ">
            <subfield code="a">Graduado en Biotecnología</subfield>
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        <datafield tag="540" ind1=" " ind2=" ">
            <subfield code="a">Derechos regulados por licencia Creative Commons</subfield>
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            <subfield code="a">ENGIN, EVREN DORUK</subfield>
            <subfield code="e">dir.</subfield>
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        <datafield tag="710" ind1="2" ind2=" ">
            <subfield code="a">Universidad de Zaragoza</subfield>
            <subfield code="b">Bioquímica y Biología Molecular y Celular</subfield>
            <subfield code="c">Bioquímica y Biología Molecular</subfield>
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            <subfield code="a">ANEL BERNAL, ALBERTO</subfield>
            <subfield code="e">ponente</subfield>
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        <datafield tag="856" ind1="0" ind2=" ">
            <subfield code="f">631550@celes.unizar.es</subfield>
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        <datafield tag="856" ind1="4" ind2=" ">
            <subfield code="s">1003651</subfield>
            <subfield code="u">http://zaguan.unizar.es/record/30717/files/TAZ-TFG-2015-011.pdf</subfield>
            <subfield code="y">Memoria (eng)</subfield>
            <subfield code="z">Memoria (eng)</subfield>
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            <subfield code="o">oai:zaguan.unizar.es:30717</subfield>
            <subfield code="p">driver</subfield>
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            <subfield code="a">deposita:2015-04-21</subfield>
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            <subfield code="a">TAZ</subfield>
            <subfield code="b">TFG</subfield>
            <subfield code="c">CIEN</subfield>
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