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<article article-type="research-article" dtd-version="1.3" 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" xml:lang="en"><front><journal-meta><journal-id journal-id-type="publisher-id">meat</journal-id><journal-title-group><journal-title xml:lang="en">Theory and practice of meat processing</journal-title><trans-title-group xml:lang="ru"><trans-title>Теория и практика переработки мяса</trans-title></trans-title-group></journal-title-group><issn pub-type="ppub">2414-438X</issn><issn pub-type="epub">2414-441X</issn><publisher><publisher-name>ФГБНУ «Федеральный научный центр пищевых систем им. В.М. Горбатова» РАН</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="doi">10.21323/2414-438X-2019-4-3-4-6</article-id><article-id custom-type="elpub" pub-id-type="custom">meat-117</article-id><article-categories><subj-group subj-group-type="heading"><subject>Research Article</subject></subj-group><subj-group subj-group-type="section-heading" xml:lang="ru"><subject>Статьи</subject></subj-group></article-categories><title-group><article-title>ASSESSING THE EFFECT OF THERMAL TREATMENT ON MEAT PROTEINS USING PROTEOMIC METHODS</article-title><trans-title-group xml:lang="ru"><trans-title>ASSESSING THE EFFECT OF THERMAL TREATMENT ON MEAT PROTEINS USING PROTEOMIC METHODS</trans-title></trans-title-group></title-group><contrib-group><contrib contrib-type="author" corresp="yes"><name-alternatives><name name-style="eastern" xml:lang="ru"><surname>Chernukha</surname><given-names>Irina M.</given-names></name><name name-style="western" xml:lang="en"><surname>Chernukha</surname><given-names>Irina M.</given-names></name></name-alternatives><bio xml:lang="ru"><p>Doctor of technical sciences, professor, corresponding member to the Russian Academy of Sciences, leading research scientist, Experimental clinic-laboratory «Biologically active substances of an animal origin»</p><p>109316, Moscow, Talalikhina str., 26. Tel: +7–495–676–63–21.</p></bio><bio xml:lang="en"><p>Doctor of technical sciences, professor, corresponding member to the Russian Academy of Sciences, leading research scientist, Experimental clinic-laboratory «Biologically active substances of an animal origin»</p><p>109316, Moscow, Talalikhina str., 26. Tel: +7–495–676–63–21.</p></bio><email xlink:type="simple">imcher@inbox.ru</email><xref ref-type="aff" rid="aff-1"/></contrib><contrib contrib-type="author" corresp="yes"><name-alternatives><name name-style="eastern" xml:lang="ru"><surname>Akhremko</surname><given-names>Anastasiya G.</given-names></name><name name-style="western" xml:lang="en"><surname>Akhremko</surname><given-names>Anastasiya G.</given-names></name></name-alternatives><bio xml:lang="ru"><p>Research assistant, Experimental clinic-laboratory «Biologically active substances of an animal origin»</p><p>109316, Moscow, Talalikhina str., 26. Tel.: +7–495–676–92–11.</p></bio><bio xml:lang="en"><p>Research assistant, Experimental clinic-laboratory «Biologically active substances of an animal origin»</p><p>109316, Moscow, Talalikhina str., 26. Tel.: +7–495–676–92–11.</p></bio><email xlink:type="simple">a.ahremko@fncps.ru</email><xref ref-type="aff" rid="aff-1"/></contrib></contrib-group><aff-alternatives id="aff-1"><aff xml:lang="ru">V. M. Gorbatov Federal Research Center for Food Systems of Russian Academy of Sciences<country>Россия</country></aff><aff xml:lang="en">V. M. Gorbatov Federal Research Center for Food Systems of Russian Academy of Sciences<country>Russian Federation</country></aff></aff-alternatives><pub-date pub-type="collection"><year>2019</year></pub-date><pub-date pub-type="epub"><day>15</day><month>10</month><year>2019</year></pub-date><volume>4</volume><issue>3</issue><fpage>4</fpage><lpage>6</lpage><permissions><copyright-statement>Copyright &amp;#x00A9; Chernukha I.M., Akhremko A.G., 2019</copyright-statement><copyright-year>2019</copyright-year><copyright-holder xml:lang="ru">Chernukha I.M., Akhremko A.G.</copyright-holder><copyright-holder xml:lang="en">Chernukha I.M., Akhremko A.G.</copyright-holder><license license-type="creative-commons-attribution" xlink:href="https://creativecommons.org/licenses/by/4.0/" xlink:type="simple"><license-p>This work is licensed under a Creative Commons Attribution 4.0 License.</license-p></license></permissions><self-uri xlink:href="https://www.meatjournal.ru/jour/article/view/117">https://www.meatjournal.ru/jour/article/view/117</self-uri><abstract><p>The results of studying the effect of various temperatures on the protein composition of minced meat from porcine m. longissimus dorsi by two-dimensional electrophoresis are presented. The most complete distribution of protein fractions was observed in fresh raw minced meat, and when it was exposed to negative temperature, there was a sharp decrease in protein components (carbonic anhydrase 3, αβ-crystallin), as well as a decrease in the staining intensity of protein spots of the main constitutive fractions (tropomyosin alpha 1, myosin light chain 1). In the case of heat treatment, structural muscle proteins were retained with some changes in high molecular weight fractions, namely, protein molecules degraded to compounds with a simpler structure. It was noted that fractions of tropomyosin β-chain, triosephosphate isomerase 1, myosin light chains 2 were not detected after minced meat was frozen, while tropomyosin alpha 1 was retained in all samples.</p></abstract><trans-abstract xml:lang="ru"><p>The results of studying the effect of various temperatures on the protein composition of minced meat from porcine m. longissimus dorsi by two-dimensional electrophoresis are presented. The most complete distribution of protein fractions was observed in fresh raw minced meat, and when it was exposed to negative temperature, there was a sharp decrease in protein components (carbonic anhydrase 3, αβ-crystallin), as well as a decrease in the staining intensity of protein spots of the main constitutive fractions (tropomyosin alpha 1, myosin light chain 1). In the case of heat treatment, structural muscle proteins were retained with some changes in high molecular weight fractions, namely, protein molecules degraded to compounds with a simpler structure. It was noted that fractions of tropomyosin β-chain, triosephosphate isomerase 1, myosin light chains 2 were not detected after minced meat was frozen, while tropomyosin alpha 1 was retained in all samples.</p></trans-abstract><kwd-group xml:lang="ru"><kwd>muscle proteins</kwd><kwd>stuffing</kwd><kwd>meat</kwd><kwd>two-dimensional electrophoresis</kwd><kwd>thermal treatment</kwd></kwd-group><kwd-group xml:lang="en"><kwd>muscle proteins</kwd><kwd>stuffing</kwd><kwd>meat</kwd><kwd>two-dimensional electrophoresis</kwd><kwd>thermal treatment</kwd></kwd-group></article-meta></front><back><ref-list><title>References</title><ref id="cit1"><label>1</label><citation-alternatives><mixed-citation xml:lang="ru">Chernukha, I. M., Fedulova, L. V., Kotenkova, E. A., Shishkin, S. S., Kovalev, L. 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