STUDY OF SODIUM, POTASSIUM, AND CALCIUM SALTS INFLUENCE ON PROTEIN STABILITY BY DIFFERENTIAL SCANNING CALORIMETRY

Abstract Study of protein stability depending on the various technological factors allows to directionally adjust the physicochemical properties of raw meat and the quality of finished meat products. The paper investigates the possibility of using the DSC to study the influence of monovalent and div...

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Main Authors: E. K. Tunieva, I. Dederer
Format: Article
Language:English
Published: The V.M. Gorbatov All-Russian Meat Research  Institute 2016-06-01
Series:Teoriâ i Praktika Pererabotki Mâsa
Subjects:
Online Access:https://www.meatjournal.ru/jour/article/view/7
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spelling doaj-7d6a33c8207c440789d0a88b4e21d41f2021-07-28T21:17:51ZengThe V.M. Gorbatov All-Russian Meat Research  InstituteTeoriâ i Praktika Pererabotki Mâsa2414-438X2414-441X2016-06-0111192410.21323/2414-438X-2016-1-1-19-243STUDY OF SODIUM, POTASSIUM, AND CALCIUM SALTS INFLUENCE ON PROTEIN STABILITY BY DIFFERENTIAL SCANNING CALORIMETRYE. K. Tunieva0I. Dederer1The V.M. Gorbatov All-Russian Meat Research Institute, MoscowMax Rubner Institute (MRI), KulmbachAbstract Study of protein stability depending on the various technological factors allows to directionally adjust the physicochemical properties of raw meat and the quality of finished meat products. The paper investigates the possibility of using the DSC to study the influence of monovalent and divalent salts on protein thermal stability. In order to determine the effect of sodium chloride and its substitutes, potassium and calcium salts, on the thermal stability of proteins, the studies were carried out with grinded pork longissimus muscle samples salted with sodium chloride at level of 2.0% and with salt compositions containing reduced by 50% level of sodium chloride (a mixture of sodium and potassium chlorides; a mixture of sodium, potassium, and calcium chlorides) using the differential scanning calorimeter DSC Q 2000 in the temperature range of 5 °C to 100 °C and the temperature change rate of 1 K/min. It was found that the addition of potassium chloride instead of 50% of sodium chloride had no significant effect on actin and myosin resistance to thermal denaturation. Meat salting using the mixture of sodium, potassium, and calcium chlorides resulted in decrease of myofibrillar proteins stability indicating the destabilizing effect of calcium on actin and myosin. A negative correlation between the magnitude of the ionic strength and the temperature of myosin and actin denaturation has been found. The correlation coefficients were minus 0.99 and minus 0.95 for myosin and actin respectively. Reduction of denaturation temperature for myofibrillar proteins in the presence of calcium chloride opens perspectives to study the possibility of heat treatment at lower temperatures for meat products with reduced sodium content.https://www.meatjournal.ru/jour/article/view/7differential scanning calorimetryactinmyosinprotein denaturation temperature
collection DOAJ
language English
format Article
sources DOAJ
author E. K. Tunieva
I. Dederer
spellingShingle E. K. Tunieva
I. Dederer
STUDY OF SODIUM, POTASSIUM, AND CALCIUM SALTS INFLUENCE ON PROTEIN STABILITY BY DIFFERENTIAL SCANNING CALORIMETRY
Teoriâ i Praktika Pererabotki Mâsa
differential scanning calorimetry
actin
myosin
protein denaturation temperature
author_facet E. K. Tunieva
I. Dederer
author_sort E. K. Tunieva
title STUDY OF SODIUM, POTASSIUM, AND CALCIUM SALTS INFLUENCE ON PROTEIN STABILITY BY DIFFERENTIAL SCANNING CALORIMETRY
title_short STUDY OF SODIUM, POTASSIUM, AND CALCIUM SALTS INFLUENCE ON PROTEIN STABILITY BY DIFFERENTIAL SCANNING CALORIMETRY
title_full STUDY OF SODIUM, POTASSIUM, AND CALCIUM SALTS INFLUENCE ON PROTEIN STABILITY BY DIFFERENTIAL SCANNING CALORIMETRY
title_fullStr STUDY OF SODIUM, POTASSIUM, AND CALCIUM SALTS INFLUENCE ON PROTEIN STABILITY BY DIFFERENTIAL SCANNING CALORIMETRY
title_full_unstemmed STUDY OF SODIUM, POTASSIUM, AND CALCIUM SALTS INFLUENCE ON PROTEIN STABILITY BY DIFFERENTIAL SCANNING CALORIMETRY
title_sort study of sodium, potassium, and calcium salts influence on protein stability by differential scanning calorimetry
publisher The V.M. Gorbatov All-Russian Meat Research  Institute
series Teoriâ i Praktika Pererabotki Mâsa
issn 2414-438X
2414-441X
publishDate 2016-06-01
description Abstract Study of protein stability depending on the various technological factors allows to directionally adjust the physicochemical properties of raw meat and the quality of finished meat products. The paper investigates the possibility of using the DSC to study the influence of monovalent and divalent salts on protein thermal stability. In order to determine the effect of sodium chloride and its substitutes, potassium and calcium salts, on the thermal stability of proteins, the studies were carried out with grinded pork longissimus muscle samples salted with sodium chloride at level of 2.0% and with salt compositions containing reduced by 50% level of sodium chloride (a mixture of sodium and potassium chlorides; a mixture of sodium, potassium, and calcium chlorides) using the differential scanning calorimeter DSC Q 2000 in the temperature range of 5 °C to 100 °C and the temperature change rate of 1 K/min. It was found that the addition of potassium chloride instead of 50% of sodium chloride had no significant effect on actin and myosin resistance to thermal denaturation. Meat salting using the mixture of sodium, potassium, and calcium chlorides resulted in decrease of myofibrillar proteins stability indicating the destabilizing effect of calcium on actin and myosin. A negative correlation between the magnitude of the ionic strength and the temperature of myosin and actin denaturation has been found. The correlation coefficients were minus 0.99 and minus 0.95 for myosin and actin respectively. Reduction of denaturation temperature for myofibrillar proteins in the presence of calcium chloride opens perspectives to study the possibility of heat treatment at lower temperatures for meat products with reduced sodium content.
topic differential scanning calorimetry
actin
myosin
protein denaturation temperature
url https://www.meatjournal.ru/jour/article/view/7
work_keys_str_mv AT ektunieva studyofsodiumpotassiumandcalciumsaltsinfluenceonproteinstabilitybydifferentialscanningcalorimetry
AT idederer studyofsodiumpotassiumandcalciumsaltsinfluenceonproteinstabilitybydifferentialscanningcalorimetry
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