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Cryoprotective Effect of NADES on Frozen-Thawed Mirror Carp Surimi in Terms of Oxidative Denaturation, Structural Properties, and Thermal Stability of Myofibrillar Proteins

Quality degradation due to the formation and growth of ice crystals caused by temperature fluctuations during storage, transportation, or retailing is a common problem in frozen surimi. While commercial antifreeze is used as an ingredient in frozen surimi, its high sweetness does not meet the contem...

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Autores principales: Li, Haijing, Wang, Qian, Li, Wenxin, Xia, Xiufang
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10572836/
https://www.ncbi.nlm.nih.gov/pubmed/37835183
http://dx.doi.org/10.3390/foods12193530
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author Li, Haijing
Wang, Qian
Li, Wenxin
Xia, Xiufang
author_facet Li, Haijing
Wang, Qian
Li, Wenxin
Xia, Xiufang
author_sort Li, Haijing
collection PubMed
description Quality degradation due to the formation and growth of ice crystals caused by temperature fluctuations during storage, transportation, or retailing is a common problem in frozen surimi. While commercial antifreeze is used as an ingredient in frozen surimi, its high sweetness does not meet the contemporary consumer demand for low sugar and low calories. Therefore, the development of new green antifreeze agents to achieve an enhanced frozen-thawed stability of surimi has received more attention. The aim of this study was to develop a cryoprotectant (a mixture of citric acid and trehalose) to enhance the frozen-thawed stability of surimi by inhibiting the oxidative denaturation and structural changes of frozen-thawed mirror carp (Cyprinus carpio L.) surimi myofibrillar protein (MP). The results showed that the amounts of free amine, sulfhydryl, α-helix, intrinsic fluorescence intensity, and thermal stability in the control significantly decreased after five F-T cycles, while the Schiff base fluorescence intensity, amounts of disulfide bonds and surface hydrophobicity significantly increased (p < 0.05). Compared to sucrose + sorbitol (SS), the natural deep eutectic solvents (NADES) effectively inhibited protein oxidation. After five F-T cycles, the α-helix content and Ca(2+)-ATPase activity of the NADES samples were 4.32% and 80.0%, respectively, higher, and the carbonyl content was 17.4% lower than those of the control. These observations indicate that NADES could inhibit oxidative denaturation and enhance the structural stability of MP.
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spelling pubmed-105728362023-10-14 Cryoprotective Effect of NADES on Frozen-Thawed Mirror Carp Surimi in Terms of Oxidative Denaturation, Structural Properties, and Thermal Stability of Myofibrillar Proteins Li, Haijing Wang, Qian Li, Wenxin Xia, Xiufang Foods Article Quality degradation due to the formation and growth of ice crystals caused by temperature fluctuations during storage, transportation, or retailing is a common problem in frozen surimi. While commercial antifreeze is used as an ingredient in frozen surimi, its high sweetness does not meet the contemporary consumer demand for low sugar and low calories. Therefore, the development of new green antifreeze agents to achieve an enhanced frozen-thawed stability of surimi has received more attention. The aim of this study was to develop a cryoprotectant (a mixture of citric acid and trehalose) to enhance the frozen-thawed stability of surimi by inhibiting the oxidative denaturation and structural changes of frozen-thawed mirror carp (Cyprinus carpio L.) surimi myofibrillar protein (MP). The results showed that the amounts of free amine, sulfhydryl, α-helix, intrinsic fluorescence intensity, and thermal stability in the control significantly decreased after five F-T cycles, while the Schiff base fluorescence intensity, amounts of disulfide bonds and surface hydrophobicity significantly increased (p < 0.05). Compared to sucrose + sorbitol (SS), the natural deep eutectic solvents (NADES) effectively inhibited protein oxidation. After five F-T cycles, the α-helix content and Ca(2+)-ATPase activity of the NADES samples were 4.32% and 80.0%, respectively, higher, and the carbonyl content was 17.4% lower than those of the control. These observations indicate that NADES could inhibit oxidative denaturation and enhance the structural stability of MP. MDPI 2023-09-22 /pmc/articles/PMC10572836/ /pubmed/37835183 http://dx.doi.org/10.3390/foods12193530 Text en © 2023 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Li, Haijing
Wang, Qian
Li, Wenxin
Xia, Xiufang
Cryoprotective Effect of NADES on Frozen-Thawed Mirror Carp Surimi in Terms of Oxidative Denaturation, Structural Properties, and Thermal Stability of Myofibrillar Proteins
title Cryoprotective Effect of NADES on Frozen-Thawed Mirror Carp Surimi in Terms of Oxidative Denaturation, Structural Properties, and Thermal Stability of Myofibrillar Proteins
title_full Cryoprotective Effect of NADES on Frozen-Thawed Mirror Carp Surimi in Terms of Oxidative Denaturation, Structural Properties, and Thermal Stability of Myofibrillar Proteins
title_fullStr Cryoprotective Effect of NADES on Frozen-Thawed Mirror Carp Surimi in Terms of Oxidative Denaturation, Structural Properties, and Thermal Stability of Myofibrillar Proteins
title_full_unstemmed Cryoprotective Effect of NADES on Frozen-Thawed Mirror Carp Surimi in Terms of Oxidative Denaturation, Structural Properties, and Thermal Stability of Myofibrillar Proteins
title_short Cryoprotective Effect of NADES on Frozen-Thawed Mirror Carp Surimi in Terms of Oxidative Denaturation, Structural Properties, and Thermal Stability of Myofibrillar Proteins
title_sort cryoprotective effect of nades on frozen-thawed mirror carp surimi in terms of oxidative denaturation, structural properties, and thermal stability of myofibrillar proteins
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10572836/
https://www.ncbi.nlm.nih.gov/pubmed/37835183
http://dx.doi.org/10.3390/foods12193530
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