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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">foodsyst</journal-id><journal-title-group><journal-title xml:lang="en">Food systems</journal-title><trans-title-group xml:lang="ru"><trans-title>Пищевые системы</trans-title></trans-title-group></journal-title-group><issn pub-type="ppub">2618-9771</issn><issn pub-type="epub">2618-7272</issn><publisher><publisher-name>Федеральный научный центр пищевых систем им. В.М. Горбатова РАН</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="doi">10.21323/2618-9771-2024-7-1-105-113</article-id><article-id custom-type="elpub" pub-id-type="custom">foodsyst-418</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>Use of turbidimetry for determination of heat treatment intensity applied at pasteurization of milk</article-title><trans-title-group xml:lang="ru"><trans-title>Использование турбидиметрии для оценки тепловой нагрузки при пастеризации молока</trans-title></trans-title-group></title-group><contrib-group><contrib contrib-type="author" corresp="yes"><contrib-id contrib-id-type="orcid">https://orcid.org/0000-0003-4443-7573</contrib-id><name-alternatives><name name-style="eastern" xml:lang="ru"><surname>Мягконосов</surname><given-names>Д. С.</given-names></name><name name-style="western" xml:lang="en"><surname>Myagkonosov</surname><given-names>D. S.</given-names></name></name-alternatives><bio xml:lang="ru"><p>Мягконосов Дмитрий Сергеевич — кандидат технических наук, старший научный сотрудник, руководитель направления исследований поприкладной биохимии и энзимологии152613, Ярославская область, Углич, Красноармейский бульвар, 19Teл.: +7–915–973–63–13</p></bio><bio xml:lang="en"><p>Dmitry S. Myagkonosov, Сandidate of Technical Sciences, Senior Researcher, Head of Research Department in Applied Biochemistry and Enzymology19, Krasnoarmeysky Boulevard, Uglich, 152613, Yaroslavl RegionTel.: +7–915–973–63–13</p></bio><email xlink:type="simple">d.myagkonosov@fncps.ru</email><xref ref-type="aff" rid="aff-1"/></contrib><contrib contrib-type="author" corresp="yes"><contrib-id contrib-id-type="orcid">https://orcid.org/0000-0003-0225-6870</contrib-id><name-alternatives><name name-style="eastern" xml:lang="ru"><surname>Топникова</surname><given-names>Е. В.</given-names></name><name name-style="western" xml:lang="en"><surname>Topnikova</surname><given-names>E. V.</given-names></name></name-alternatives><bio xml:lang="ru"><p>Топникова Елена Васильевна — доктор технических наук, заместитель директора по научной работе152613, Ярославская обл., Углич, Красноармейский бульвар, 19Тел.: +7–910–666–93–93</p></bio><bio xml:lang="en"><p>Elena V. Topnikova, Doctor of Technical Sciences, Deputy Director for Research,</p><p>19, Krasnoarmeysky Boulevard, Uglich, 152613, Yaroslavl RegionTel.: +7–915–973–63–13</p></bio><email xlink:type="simple">topnikova.l@yandex.ru</email><xref ref-type="aff" rid="aff-1"/></contrib><contrib contrib-type="author" corresp="yes"><contrib-id contrib-id-type="orcid">https://orcid.org/0000-0001-8326-1932</contrib-id><name-alternatives><name name-style="eastern" xml:lang="ru"><surname>Абрамов</surname><given-names>Д. В.</given-names></name><name name-style="western" xml:lang="en"><surname>Abramov</surname><given-names>D. V.</given-names></name></name-alternatives><bio xml:lang="ru"><p>Абрамов Дмитрий Васильевич — кандидат биологических наук, старший научный сотрудник, руководитель направления биохимическихисследований по сыроделию и маслоделию152613, Ярославская область, Углич, Красноармейский бульвар, 19Teл.: +7–910–970–42–97</p></bio><bio xml:lang="en"><p>Dmitry V. Abramov, Candidate of Biological Sciences, Senior Researcher, Head of Biochemical Research in Cheesemaking and Buttermaking</p><p>19, Krasnoarmeysky Boulevard, Uglich, 152613, Yaroslavl RegionTel.: +7–915–973–63–13</p></bio><email xlink:type="simple">d.abramov@fncps.ru</email><xref ref-type="aff" rid="aff-1"/></contrib><contrib contrib-type="author" corresp="yes"><contrib-id contrib-id-type="orcid">https://orcid.org/0000-0002-7557-6835</contrib-id><name-alternatives><name name-style="eastern" xml:lang="ru"><surname>Кашникова</surname><given-names>О. Г.</given-names></name><name name-style="western" xml:lang="en"><surname>Kashnikova</surname><given-names>O. G.</given-names></name></name-alternatives><bio xml:lang="ru"><p>Кашникова Ольга Геннадьевна — младший научный сотрудник, отдел физической химии152613, Ярославская обл., Углич, Красноармейский бульвар, 19Тел.: +7–962–200–14–15</p></bio><bio xml:lang="en"><p>Olga G. Kashnikova, Junior researcher, Department of Physical Chemistry</p><p>19, Krasnoarmeysky Boulevard, Uglich, 152613, Yaroslavl RegionTel.: +7–915–973–63–13</p></bio><email xlink:type="simple">o.kashnikova@fncps.ru</email><xref ref-type="aff" rid="aff-1"/></contrib></contrib-group><aff-alternatives id="aff-1"><aff xml:lang="ru"><institution>Всероссийский научно-исследовательский институт маслоделия и сыроделия — Углич</institution><country>Россия</country></aff><aff xml:lang="en"><institution>All-Russian Scientific Research Institute of Butter- and Cheesemaking</institution><country>Russian Federation</country></aff></aff-alternatives><pub-date pub-type="collection"><year>2024</year></pub-date><pub-date pub-type="epub"><day>22</day><month>04</month><year>2024</year></pub-date><volume>7</volume><issue>1</issue><fpage>105</fpage><lpage>113</lpage><permissions><copyright-statement>Copyright &amp;#x00A9; Myagkonosov D.S., Topnikova E.V., Abramov D.V., Kashnikova O.G., 2024</copyright-statement><copyright-year>2024</copyright-year><copyright-holder xml:lang="ru">Мягконосов Д.С., Топникова Е.В., Абрамов Д.В., Кашникова О.Г.</copyright-holder><copyright-holder xml:lang="en">Myagkonosov D.S., Topnikova E.V., Abramov D.V., Kashnikova O.G.</copyright-holder><license xml:lang="ru" license-type="creative-commons-attribution" xlink:href="https://creativecommons.org/licenses/by/4.0/" xlink:type="simple"><license-p>Данная работа распространяется под лицензией Creative Commons Attribution 4.0.</license-p></license><license xml:lang="en" 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.fsjour.com/jour/article/view/418">https://www.fsjour.com/jour/article/view/418</self-uri><abstract><p>Express methods for estimating the intensity of heat treatment of milk are necessary in industry and in research work. For this reason, there are many ways to measure this parameter, which are based on different physical principles, including turbidimetric methods. The Harland &amp; Ashworth turbidimetric method has been developed for a long time, however, due to its high reliability and ease of implementation, it is still used in practice. However, this method has a drawback: it takes a long time to perform the analysis. In this regard, the aim of the work is to develop an express method for evaluating the thermal class of milk based on the principle of measuring the concentration of soluble whey proteins. The result is achieved through the use of a turbidimetric measurement method with optimized sample preparation parameters and parameters for measuring the optical density of a suspension of protein aggregates. The method is implemented as follows. The milk sample is mixed with 0.1 N acetate buffer (pH 4.6) in a ratio that allows to obtain a concentration of soluble milk whey proteins from 0.05% to 0.1%. Recommended dilution coefficients: 1:3 for samples of ultra-pasteurized milk and pasteurized milk with high heat treatment intensity; 1:7 for samples of pasteurized milk with low heat treatment intensity and 1:14 for raw milk samples. The solution is filtered on a membrane filter with a pore size of 0.45 microns. The resulting filtrate is mixed with 24% trichloroacetic acid (TCA) in a 1:1 ratio to coagulate soluble whey proteins and form protein aggregates. After holding for 5–10 minutes, the optical density of the suspension of protein aggregates is measured at a wavelength of 650 nm. The content of water-soluble whey proteins in the sample can be calculated according to the calibration curve. The developed method allows to obtain the measurement result in less time than the Harland &amp; Ashworth turbidimetric method.</p></abstract><trans-abstract xml:lang="ru"><p>Методы быстрой оценки интенсивности тепловой обработки молока необходимы как в промышленности, так и в исследовательской работе. В связи с этим существует множество способов измерений данного показателя, основанных на различных физических принципах, в том числе турбодиметрические методы. Однако данный метод имеет недостаток: для выполнения анализа требуется длительное время. В связи с этим в работе поставлена цель разработать на базе этого принципа измерений экспресс-метод определения растворимых сывороточных белков, характеризующих тепловой класс молока. Результат достигается за счет применения турбидиметрического метода определения с оптимизированными параметрами подготовки пробы и измерения оптической плотности суспензии белковых агрегатов. Метод реализуется следующим образом. Образец молока смешивается с 0,1 N ацетатным буфером (рН 4,6) в соотношении, позволяющем получить концентрацию растворимых сывороточных белков молока от 0,05% до 0,1%. Рекомендованные коэффициенты разведения: 1:3 для образцов ультрапастеризованного молока и пастеризованного молока с высокой интенсивностью термообработки; 1:7 для образцов пастеризованного молока с низкой интенсивностью термообработки и 1:14 для образцов сырого молока. Раствор фильтруют на мембранном фильтре с размером пор 0,45 мкм. Полученный фильтрат смешивают с 24% ТХУ в соотношении 1:1 для коагуляции растворимых сывороточных белков и формирования белковых агрегатов. После выдерживания в течение 5–10 мин оптическую плотность суспензии белковых агрегатов измеряют при длине волны 650 нм. Содержание водорастворимых сывороточных белков в образце может быть рассчитано по калибровочной зависимости. Разработанный метод позволяет получить результат измерений за меньшее время, чем турбидиметрический метод Harland &amp; Ashworth.</p></trans-abstract><kwd-group xml:lang="ru"><kwd>пастеризация</kwd><kwd>тепловая обработка</kwd><kwd>сывороточные белки</kwd><kwd>турбидиметрические методы</kwd></kwd-group><kwd-group xml:lang="en"><kwd>рasteurization</kwd><kwd>heat treatment</kwd><kwd>whey proteins</kwd><kwd>turbidimetric methods</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">Mandal, R., Bag, S. K., Singh, A. P. (2019). Thermal Processing of Milk. Chapter in a book: Recent Technologies in Dairy Science. Today and Tomorrow’s Printers and Publishers, New Delhi, India, 2019.</mixed-citation><mixed-citation xml:lang="en">Mandal, R., Bag, S. K., Singh, A. P. (2019). Thermal Processing of Milk. Chapter in a book: Recent Technologies in Dairy Science. Today and Tomorrow’s Printers and Publishers, New Delhi, India, 2019.</mixed-citation></citation-alternatives></ref><ref id="cit2"><label>2</label><citation-alternatives><mixed-citation xml:lang="ru">Akkerman, M. (2014). The effect of heating processes on milk whey protein denaturation and rennet coagulation properties. Master Thesis. Department of Food Science, Aarhus University. Retrieved from http://www.library.au.dk/fil-eadmin/www.bibliotek.au.dk/fagsider/jordbrug/Specialer/Marije_-master_the-sis.pdf Accessed December 11, 2023.</mixed-citation><mixed-citation xml:lang="en">Akkerman, M. (2014). The effect of heating processes on milk whey protein denaturation and rennet coagulation properties. Master Thesis. Department of Food Science, Aarhus University. Retrieved from http://www.library.au.dk/fil-eadmin/www.bibliotek.au.dk/fagsider/jordbrug/Specialer/Marije_-master_the-sis.pdf Accessed December 11, 2023.</mixed-citation></citation-alternatives></ref><ref id="cit3"><label>3</label><citation-alternatives><mixed-citation xml:lang="ru">Mahomud, S., Katsuno, N., Nishizu, T. (2017). Role of whey protein-casein complexes on yoghurt texture. Reviews in Agricultural Science, 5, 1–12. https://doi.org/10.7831/ras.5.1</mixed-citation><mixed-citation xml:lang="en">Mahomud, S., Katsuno, N., Nishizu, T. (2017). Role of whey protein-casein complexes on yoghurt texture. Reviews in Agricultural Science, 5, 1–12. https://doi.org/10.7831/ras.5.1</mixed-citation></citation-alternatives></ref><ref id="cit4"><label>4</label><citation-alternatives><mixed-citation xml:lang="ru">Guinee, T. P. (2021). Effect of high-temperature treatment of milk and whey protein denaturation on the properties of rennet–curd cheese: A review. International Dairy Journal, 121, Article 105095. https://doi.org/10.1016/j.idairyj.2021.105095</mixed-citation><mixed-citation xml:lang="en">Guinee, T. P. (2021). Effect of high-temperature treatment of milk and whey protein denaturation on the properties of rennet–curd cheese: A review. International Dairy Journal, 121, Article 105095. https://doi.org/10.1016/j.idairyj.2021.105095</mixed-citation></citation-alternatives></ref><ref id="cit5"><label>5</label><citation-alternatives><mixed-citation xml:lang="ru">Barraquio, V. L. (2014). Which milk is fresh? International Journal of Dairy Processing and Research, 1(2), 1–6. https://doi.org/10.19070/2379-1578-140002</mixed-citation><mixed-citation xml:lang="en">Barraquio, V. L. (2014). Which milk is fresh? International Journal of Dairy Processing and Research, 1(2), 1–6. https://doi.org/10.19070/2379-1578-140002</mixed-citation></citation-alternatives></ref><ref id="cit6"><label>6</label><citation-alternatives><mixed-citation xml:lang="ru">Cattaneo, S., Masotti, F., Pellegrino, L. (2008). Effects of overprocessing on heat damage of UHT milk. European Food Research and Technology, 226, 1099–1106. https://doi.org/10.1007/s00217-007-0637-5</mixed-citation><mixed-citation xml:lang="en">Cattaneo, S., Masotti, F., Pellegrino, L. (2008). Effects of overprocessing on heat damage of UHT milk. European Food Research and Technology, 226, 1099–1106. https://doi.org/10.1007/s00217-007-0637-5</mixed-citation></citation-alternatives></ref><ref id="cit7"><label>7</label><citation-alternatives><mixed-citation xml:lang="ru">International Dairy Federation. (2022). Heat treatment of milk (Bulletin of the IDF n° 516/2022). https://doi.org/10.56169/XMDR7579</mixed-citation><mixed-citation xml:lang="en">International Dairy Federation. (2022). Heat treatment of milk (Bulletin of the IDF n° 516/2022). https://doi.org/10.56169/XMDR7579</mixed-citation></citation-alternatives></ref><ref id="cit8"><label>8</label><citation-alternatives><mixed-citation xml:lang="ru">U. S. Dairy Export Council. (2018). Reference Manual for U. S. Milk Powders and Microfiltered Ingredients. Retrieved from https://www.thinkusadairy.org/assets/documents/Customer%20Site/C3-Using%20Dairy/C3.7-Resources%20and%20Insights/02-Product%20Resources/USD5163-US-Milk-Powders_LIVE_Web.pdf Accessed December 20, 2023.</mixed-citation><mixed-citation xml:lang="en">U. S. Dairy Export Council. (2018). Reference Manual for U. S. Milk Powders and Microfiltered Ingredients. Retrieved from https://www.thinkusadairy.org/assets/documents/Customer%20Site/C3-Using%20Dairy/C3.7-Resources%20and%20Insights/02-Product%20Resources/USD5163-US-Milk-Powders_LIVE_Web.pdf Accessed December 20, 2023.</mixed-citation></citation-alternatives></ref><ref id="cit9"><label>9</label><citation-alternatives><mixed-citation xml:lang="ru">van den Oever, S. P., Mayer, H. K. (2021). Analytical assessment of the intensity of heat treatment of milk and dairy products. International Dairy Journal, 121, Article 105097. https://doi.org/10.1016/j.idairyj.2021.105097</mixed-citation><mixed-citation xml:lang="en">van den Oever, S. P., Mayer, H. K. (2021). Analytical assessment of the intensity of heat treatment of milk and dairy products. International Dairy Journal, 121, Article 105097. https://doi.org/10.1016/j.idairyj.2021.105097</mixed-citation></citation-alternatives></ref><ref id="cit10"><label>10</label><citation-alternatives><mixed-citation xml:lang="ru">Chang, S., Zhang, Y. (2017) Protein Analysis. Chapter in book: Food Analysis. Springer International Publishing. 2017. https://doi.org/10.1007/978-3-319-45776-5_18</mixed-citation><mixed-citation xml:lang="en">Chang, S., Zhang, Y. (2017) Protein Analysis. Chapter in book: Food Analysis. Springer International Publishing. 2017. https://doi.org/10.1007/978-3-319-45776-5_18</mixed-citation></citation-alternatives></ref><ref id="cit11"><label>11</label><citation-alternatives><mixed-citation xml:lang="ru">Miralles, B., Bartolomé, B., Amigo, L., Ramos, M. (2000). Comparison of three methods to determine the whey protein to total protein ratio in milk. Journal of Dairy Science, 83, 2759–2765. https://doi.org/10.3168/jds.S0022-0302(00)75171-X</mixed-citation><mixed-citation xml:lang="en">Miralles, B., Bartolomé, B., Amigo, L., Ramos, M. (2000). Comparison of three methods to determine the whey protein to total protein ratio in milk. Journal of Dairy Science, 83, 2759–2765. https://doi.org/10.3168/jds.S0022-0302(00)75171-X</mixed-citation></citation-alternatives></ref><ref id="cit12"><label>12</label><citation-alternatives><mixed-citation xml:lang="ru">Melfsen, A., Hartung, E., Haeussermann, A. (2012). Accuracy of milk composition analysis with near infrared spectroscopy in diffuse reflection mode. Biosystems Engineering, 112(3), 210–217. https://doi.org/10.1016/j.biosystemseng.2012.04.003</mixed-citation><mixed-citation xml:lang="en">Melfsen, A., Hartung, E., Haeussermann, A. (2012). Accuracy of milk composition analysis with near infrared spectroscopy in diffuse reflection mode. Biosystems Engineering, 112(3), 210–217. https://doi.org/10.1016/j.biosystemseng.2012.04.003</mixed-citation></citation-alternatives></ref><ref id="cit13"><label>13</label><citation-alternatives><mixed-citation xml:lang="ru">Etzion, Y., Linker, R., Cogan, U., Shmulevich, I. (2004). Determination of protein concentration in raw milk by mid-infrared fourier transform infrared/attenuated total reflectance spectroscopy. Journal of Dairy Science, 87(9), 2779–2788. https://doi.org/10.3168/jds.S0022-0302(04)73405-0</mixed-citation><mixed-citation xml:lang="en">Etzion, Y., Linker, R., Cogan, U., Shmulevich, I. (2004). Determination of protein concentration in raw milk by mid-infrared fourier transform infrared/attenuated total reflectance spectroscopy. Journal of Dairy Science, 87(9), 2779–2788. https://doi.org/10.3168/jds.S0022-0302(04)73405-0</mixed-citation></citation-alternatives></ref><ref id="cit14"><label>14</label><citation-alternatives><mixed-citation xml:lang="ru">Filgueiras, M. F., Borges, E. M. (2022). Quick and cheap colorimetric quantification of proteins using 96-well-plate images. Journal of Chemical Education, 99(4), 1778–1787. https://doi.org/10.1021/acs.jchemed.1c00756</mixed-citation><mixed-citation xml:lang="en">Filgueiras, M. F., Borges, E. M. (2022). Quick and cheap colorimetric quantification of proteins using 96-well-plate images. Journal of Chemical Education, 99(4), 1778–1787. https://doi.org/10.1021/acs.jchemed.1c00756</mixed-citation></citation-alternatives></ref><ref id="cit15"><label>15</label><citation-alternatives><mixed-citation xml:lang="ru">Assink Junior, E. J., de Jesus, P. C., Borges, E. M. (2023). Ehey protein analysis using the lowry assay and 96-well-plate digital images acquired using smartphones. Journal of Chemical Education, 100(6), 2329–2338. https://doi.org/10.1021/acs. jchemed.2c00830</mixed-citation><mixed-citation xml:lang="en">Assink Junior, E. J., de Jesus, P. C., Borges, E. M. (2023). Ehey protein analysis using the lowry assay and 96-well-plate digital images acquired using smartphones. Journal of Chemical Education, 100(6), 2329–2338. https://doi.org/10.1021/acs. jchemed.2c00830</mixed-citation></citation-alternatives></ref><ref id="cit16"><label>16</label><citation-alternatives><mixed-citation xml:lang="ru">Jeanson, S., Dupont, D., Grattard, N., Rolet-Répécaud, O. (1999). Characterization of the heat treatment undergone by milk using two inhibition ELISAs for quantification of native and heat denatured α-lactalbumin. Journal of Agricultural and Food Chemistry, 47(6), 2249–2254. https://doi.org/10.1021/jf9809232</mixed-citation><mixed-citation xml:lang="en">Jeanson, S., Dupont, D., Grattard, N., Rolet-Répécaud, O. (1999). Characterization of the heat treatment undergone by milk using two inhibition ELISAs for quantification of native and heat denatured α-lactalbumin. Journal of Agricultural and Food Chemistry, 47(6), 2249–2254. https://doi.org/10.1021/jf9809232</mixed-citation></citation-alternatives></ref><ref id="cit17"><label>17</label><citation-alternatives><mixed-citation xml:lang="ru">Lu, Y., Fu, T.-J. (2020). Performance of commercial colorimetric assays for quantitation of total soluble protein in thermally treated milk samples. Food Analytical Methods, 13, 1337–1345. https://doi.org/10.1007/s12161-020-01748-w</mixed-citation><mixed-citation xml:lang="en">Lu, Y., Fu, T.-J. (2020). Performance of commercial colorimetric assays for quantitation of total soluble protein in thermally treated milk samples. Food Analytical Methods, 13, 1337–1345. https://doi.org/10.1007/s12161-020-01748-w</mixed-citation></citation-alternatives></ref><ref id="cit18"><label>18</label><citation-alternatives><mixed-citation xml:lang="ru">Harland, H. A., Ashworth, U. S. (1947). A rapid method for estimation of whey proteins as an indication of baking quality of nonfat dry-milk solids. Food Research, 12(3), 247–251. https://doi.org/10.1111/j.1365-2621.1947.tb16416.x</mixed-citation><mixed-citation xml:lang="en">Harland, H. A., Ashworth, U. S. (1947). A rapid method for estimation of whey proteins as an indication of baking quality of nonfat dry-milk solids. Food Research, 12(3), 247–251. https://doi.org/10.1111/j.1365-2621.1947.tb16416.x</mixed-citation></citation-alternatives></ref><ref id="cit19"><label>19</label><citation-alternatives><mixed-citation xml:lang="ru">Patel, H. A., Anema, S. G., Holroyd, S. E., Singh, H., Creamer, L. K. (2007). Methods to determine denaturation and aggregation of proteins in low-, mediumand high-heat skim milk powders. Le Lait, 87(4–5), 251–268. http://doi.org/10.1051/lait:2007027</mixed-citation><mixed-citation xml:lang="en">Patel, H. A., Anema, S. G., Holroyd, S. E., Singh, H., Creamer, L. K. (2007). Methods to determine denaturation and aggregation of proteins in low-, mediumand high-heat skim milk powders. Le Lait, 87(4–5), 251–268. http://doi.org/10.1051/lait:2007027</mixed-citation></citation-alternatives></ref><ref id="cit20"><label>20</label><citation-alternatives><mixed-citation xml:lang="ru">Zhao, Z., Corredig, M., Gaygadzhiev, Z. (2019). Short communication: Determination of the whey protein index in milk protein concentrates. Journal of Dairy Science, 102(9), 7760–7764. https://doi.org/10.3168/jds.2019-16547</mixed-citation><mixed-citation xml:lang="en">Zhao, Z., Corredig, M., Gaygadzhiev, Z. (2019). Short communication: Determination of the whey protein index in milk protein concentrates. Journal of Dairy Science, 102(9), 7760–7764. https://doi.org/10.3168/jds.2019-16547</mixed-citation></citation-alternatives></ref><ref id="cit21"><label>21</label><citation-alternatives><mixed-citation xml:lang="ru">GEA Niro analytical methods. (2009). Whey Protein Nitrogen Index. GEA Niro Method No. A 21 a. Retrieved from https://www.yumpu.com/en/document/read/6894617/whey-protein-nitrogen-index-wpn-gea-niro Accessed December 20, 2023.</mixed-citation><mixed-citation xml:lang="en">GEA Niro analytical methods. (2009). Whey Protein Nitrogen Index. GEA Niro Method No. A 21 a. Retrieved from https://www.yumpu.com/en/document/read/6894617/whey-protein-nitrogen-index-wpn-gea-niro Accessed December 20, 2023.</mixed-citation></citation-alternatives></ref><ref id="cit22"><label>22</label><citation-alternatives><mixed-citation xml:lang="ru">Visser, S., Slangen, C. J., Robben, A. J. P. M. (1992). Determination of molecular mass distributions of whey protein hydrolysates by high-pergomance sizeexclusion chromatography. Journal of Chromatography A, 599(1–2), 205–209. https://doi.org/10.1016/0021-9673(92)85474-8</mixed-citation><mixed-citation xml:lang="en">Visser, S., Slangen, C. J., Robben, A. J. P. M. (1992). Determination of molecular mass distributions of whey protein hydrolysates by high-pergomance sizeexclusion chromatography. Journal of Chromatography A, 599(1–2), 205–209. https://doi.org/10.1016/0021-9673(92)85474-8</mixed-citation></citation-alternatives></ref><ref id="cit23"><label>23</label><citation-alternatives><mixed-citation xml:lang="ru">Montgomery, D. C. (2013). Design and analysis of experiments. John Wiley &amp; Sons, Inc. Hoboken, NJ, United States, 2013.</mixed-citation><mixed-citation xml:lang="en">Montgomery, D. C. (2013). Design and analysis of experiments. John Wiley &amp; Sons, Inc. Hoboken, NJ, United States, 2013.</mixed-citation></citation-alternatives></ref><ref id="cit24"><label>24</label><citation-alternatives><mixed-citation xml:lang="ru">Mahmoud, R., Brown, R. J., Ernstrom, C. A. (1990). Factors affecting measurement of undenatured whey protein nitrogen in dried whey by a modified Harland-Ashworth test. Journal of Dairy Science, 73(7), 1694–1699. https://doi.org/10.3168/jds.S0022-0302(90)78845-5</mixed-citation><mixed-citation xml:lang="en">Mahmoud, R., Brown, R. J., Ernstrom, C. A. (1990). Factors affecting measurement of undenatured whey protein nitrogen in dried whey by a modified Harland-Ashworth test. Journal of Dairy Science, 73(7), 1694–1699. https://doi.org/10.3168/jds.S0022-0302(90)78845-5</mixed-citation></citation-alternatives></ref><ref id="cit25"><label>25</label><citation-alternatives><mixed-citation xml:lang="ru">Guan, R.-F., Liu, D.-H., Ye, X.-Q., Yang, K. (2005). Use of fluorometry for determination of skim milk powder adulteration in fresh milk. Journal of Zhejiang University-SCIENCE B, 6(11), 1101–1106. https://doi.org/10.1631/jzus.2005.B1101</mixed-citation><mixed-citation xml:lang="en">Guan, R.-F., Liu, D.-H., Ye, X.-Q., Yang, K. (2005). Use of fluorometry for determination of skim milk powder adulteration in fresh milk. Journal of Zhejiang University-SCIENCE B, 6(11), 1101–1106. https://doi.org/10.1631/jzus.2005.B1101</mixed-citation></citation-alternatives></ref><ref id="cit26"><label>26</label><citation-alternatives><mixed-citation xml:lang="ru">Rajalingam, D., Loftis, C., Xu, J. J., Kumar, T. K. S. (2009). Trichloroacetic acid-induced protein precipitation involves the reversible association of a stable partially structured intermediate. Protein Science, 18(5), 980–993. https://doi.org/10.1002/pro.108</mixed-citation><mixed-citation xml:lang="en">Rajalingam, D., Loftis, C., Xu, J. J., Kumar, T. K. S. (2009). Trichloroacetic acid-induced protein precipitation involves the reversible association of a stable partially structured intermediate. Protein Science, 18(5), 980–993. https://doi.org/10.1002/pro.108</mixed-citation></citation-alternatives></ref><ref id="cit27"><label>27</label><citation-alternatives><mixed-citation xml:lang="ru">Sivaraman, T., Kumar, T. K. S., Jayaraman, G., Yu, C. (1997). The Mechanism of 2,2,2-trichloroacetic acid-induced protein precipitation. Journal of Protein Chemistry, 16(4), 291–297. https://doi.org/10.1023/A:1026357009886</mixed-citation><mixed-citation xml:lang="en">Sivaraman, T., Kumar, T. K. S., Jayaraman, G., Yu, C. (1997). The Mechanism of 2,2,2-trichloroacetic acid-induced protein precipitation. Journal of Protein Chemistry, 16(4), 291–297. https://doi.org/10.1023/A:1026357009886</mixed-citation></citation-alternatives></ref><ref id="cit28"><label>28</label><citation-alternatives><mixed-citation xml:lang="ru">Lynch, J. M., Barbano D. M., Fleming J. R. (1998). Indirect and direct determination of the casein content of milk by kjeldahl nitrogen analysis: Collaborative study. Journal of AOAC INTERNATIONAL, 81(4), 763–774. https://doi.org/10.1093/jaoac/81.4.763</mixed-citation><mixed-citation xml:lang="en">Lynch, J. M., Barbano D. M., Fleming J. R. (1998). Indirect and direct determination of the casein content of milk by kjeldahl nitrogen analysis: Collaborative study. Journal of AOAC INTERNATIONAL, 81(4), 763–774. https://doi.org/10.1093/jaoac/81.4.763</mixed-citation></citation-alternatives></ref><ref id="cit29"><label>29</label><citation-alternatives><mixed-citation xml:lang="ru">Kuramoto, S., Jenness, R., Coulter, S. T., Choi, R. P. (1959). Standardization of the Harland-Ashworth test for whey protein nitrogen. Journal of Dairy Science, 42(1), 28–38. https://doi.org/10.3168/jds.S0022-0302(59)90520-X</mixed-citation><mixed-citation xml:lang="en">Kuramoto, S., Jenness, R., Coulter, S. T., Choi, R. P. (1959). Standardization of the Harland-Ashworth test for whey protein nitrogen. Journal of Dairy Science, 42(1), 28–38. https://doi.org/10.3168/jds.S0022-0302(59)90520-X</mixed-citation></citation-alternatives></ref><ref id="cit30"><label>30</label><citation-alternatives><mixed-citation xml:lang="ru">Silver, F. H., Birk, D. E. (1983). Kinetic analysis of collagen fibrillogenesis: I. Use of turbidity-time data. Collagen and Related Research, 3, 393–405. https://doi. org/10.1016/S0174-173X(83)80020-X</mixed-citation><mixed-citation xml:lang="en">Silver, F. H., Birk, D. E. (1983). Kinetic analysis of collagen fibrillogenesis: I. Use of turbidity-time data. Collagen and Related Research, 3, 393–405. https://doi. org/10.1016/S0174-173X(83)80020-X</mixed-citation></citation-alternatives></ref><ref id="cit31"><label>31</label><citation-alternatives><mixed-citation xml:lang="ru">Mehalebi, S., Nicolai, T., Durand, D. (2008). Light scattering study of heat-denatured globular protein aggregates. International Journal of Biological Macromolecules, 43(2), 129–135. https://doi.org/10.1016/j.ijbiomac.2008.04.002</mixed-citation><mixed-citation xml:lang="en">Mehalebi, S., Nicolai, T., Durand, D. (2008). Light scattering study of heat-denatured globular protein aggregates. International Journal of Biological Macromolecules, 43(2), 129–135. https://doi.org/10.1016/j.ijbiomac.2008.04.002</mixed-citation></citation-alternatives></ref><ref id="cit32"><label>32</label><citation-alternatives><mixed-citation xml:lang="ru">Xiao, F., Huang, J.-C. H., Zhang, B.-J., Cui, C-w. (2009). Effects of low temperature on coagulation kinetics and floc surface morphology using alum. Desalination, 237(1–3), 201–213. https://doi.org/10.1016/j.desal.2007.12.033 33. Pearce, K. N., Kinsella, J. E. (1978). Emulsifying properties of proteins: evaluation of a turbidimetric technique. Journal of Agricultural and Food Chemistry, 26(3), 716–723. https://doi.org/10.1021/jf60217a041</mixed-citation><mixed-citation xml:lang="en">Xiao, F., Huang, J.-C. H., Zhang, B.-J., Cui, C-w. (2009). Effects of low temperature on coagulation kinetics and floc surface morphology using alum. Desalination, 237(1–3), 201–213. https://doi.org/10.1016/j.desal.2007.12.033 33. Pearce, K. N., Kinsella, J. E. (1978). Emulsifying properties of proteins: evaluation of a turbidimetric technique. Journal of Agricultural and Food Chemistry, 26(3), 716–723. https://doi.org/10.1021/jf60217a041</mixed-citation></citation-alternatives></ref><ref id="cit33"><label>33</label><citation-alternatives><mixed-citation xml:lang="ru">Berlin, A. A., Kislenko, V. N., Moldovanov, M. A. (1992). Mathematical model of suspension flocculation kinetics. Colloid and Polymer Science, 270, 1042–1045. https://doi.org/10.1007/BF00655974</mixed-citation><mixed-citation xml:lang="en">Berlin, A. A., Kislenko, V. N., Moldovanov, M. A. (1992). Mathematical model of suspension flocculation kinetics. Colloid and Polymer Science, 270, 1042–1045. https://doi.org/10.1007/BF00655974</mixed-citation></citation-alternatives></ref><ref id="cit34"><label>34</label><citation-alternatives><mixed-citation xml:lang="ru">Stoscheck, C. M. (1990). Quantitation of protein. Chapter in a book: Methods in Enzymology. V. 182. Guide to Protein Purification. Academic Press, Inc. 1990. https://doi.org/10.1016/0076-6879(90)82008-P</mixed-citation><mixed-citation xml:lang="en">Stoscheck, C. M. (1990). Quantitation of protein. Chapter in a book: Methods in Enzymology. V. 182. Guide to Protein Purification. Academic Press, Inc. 1990. https://doi.org/10.1016/0076-6879(90)82008-P</mixed-citation></citation-alternatives></ref></ref-list><fn-group><fn fn-type="conflict"><p>The authors declare that there are no conflicts of interest present.</p></fn></fn-group></back></article>
