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A Pickering emulsion based on sodium starch octenyl succinate (SSOS) was prepared and its effects on the physicochemical properties of hairtail myofibrillar protein gels (MPGs) subjected to multiple freeze-thaw (F-T) cycles were investigated. The whiteness, water-holding capacity, storage modulus (G’) and texture properties of the MPGs were significantly improved by adding 1%–2% Pickering emulsion (P < 0.05). Me anwhile, Raman spectral analysis demonstrated that Pickering emulsion promoted the transformation of secondary structure, enhanced hydrogen bonds and hydrophobic interactions, and promoted the transition of disulfide bond conformation from g-g-g to g-g-t and t-g-t. At an emulsion concentration of 2%, the α-helix content decreased by 10.37%, while the β-sheet content increased by 7.94%, compared to the control. After F-T cycles, the structure of the MPGs was destroyed, with an increase in hardness and a decrease in whiteness and waterholding capacity, however, the quality degradation of MPGs was reduced with 1%–2% Pickering emulsion. These findings demonstrated that SSOS-Pickering emulsions, as potential fat substitutes, can enhance the gel properties and the F-T stability of MPGs.


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Effect of sodium starch octenyl succinate-based Pickering emulsion on the physicochemical properties of hairtail myofibrillar protein gel subjected to multiple freeze-thaw cycles

Show Author's information Huinan Wanga,1Jiaxin Zhangb,1Xinran LiubJinxiang WangbXuepeng Lib( )Jianrong Lia,b,( )
Key Laboratory of Food Nutrition and Safety, Ministry of Education, College of Food Science and Engineering, Tianjin University of Science and Technology, Tianjin 300457, China
College of Food Science and Technology, Bohai University, National R&D Branch Center of Surimi and Surimi Products Processing, Jinzhou 121013, China

1 Co-first author.

Peer review under responsibility of Tsinghua University Press.

Highlights

· SSOS-Pickering emulsion enhanced gel strength (51.7 g•mm) and produced an ordered gel structure.

· SSOS-Pickering emulsion promoted the changes of secondary structures and disulfide bonds of MPGs.

· SSOS-Pickering emulsion improved the freeze-thaw stability of MPGs.

· Pickering emulsions can be used as a potential modifying agent in surimi gels.

Abstract

A Pickering emulsion based on sodium starch octenyl succinate (SSOS) was prepared and its effects on the physicochemical properties of hairtail myofibrillar protein gels (MPGs) subjected to multiple freeze-thaw (F-T) cycles were investigated. The whiteness, water-holding capacity, storage modulus (G’) and texture properties of the MPGs were significantly improved by adding 1%–2% Pickering emulsion (P < 0.05). Me anwhile, Raman spectral analysis demonstrated that Pickering emulsion promoted the transformation of secondary structure, enhanced hydrogen bonds and hydrophobic interactions, and promoted the transition of disulfide bond conformation from g-g-g to g-g-t and t-g-t. At an emulsion concentration of 2%, the α-helix content decreased by 10.37%, while the β-sheet content increased by 7.94%, compared to the control. After F-T cycles, the structure of the MPGs was destroyed, with an increase in hardness and a decrease in whiteness and waterholding capacity, however, the quality degradation of MPGs was reduced with 1%–2% Pickering emulsion. These findings demonstrated that SSOS-Pickering emulsions, as potential fat substitutes, can enhance the gel properties and the F-T stability of MPGs.

Keywords: Pickering emulsion, Freeze-thaw stability, Gel properties, Myofibrillar protein, Intermolecular interactions

References(57)

[1]

Y. Chen, A. Xu, R. Yang, et al., Chemical interactions and rheological properties of hairtail (Trichiurus haumela) surimi: effects of chopping and pressure, Food Biosci. 38 (2020) 100781. https://doi.org/10.1016/j.fbio.2020.

[2]

Y. Cao, L. Zhao, Q. Huang, et al., Water migration, ice crystal formation, and freeze-thaw stability of silver carp surimi as affected by inulin under different additive amounts and polymerization degrees, Food Hydrocoll. 124 (2022) 107267. https://doi.org/10.1016/j.foodhyd.2021.107267.

[3]

C. Leygonie, T.J. Britz, L.C. Hoffman, Impact of freezing and thawing on the quality of meat: review, Meat Sci. 91 (2012) 93-98. https://doi.org/10.1016/j.meatsci.2012.01.013.

[4]

N. Walayat, H. Xiong, Z. Xiong, et al., Role of cryoprotectants in surimi and factors affecting surimi gel properties: a review, Food Rev. Int. (2020) 1103-1122. https://doi.org/10.1080/87559129.2020.1768403.

[5]

C. Zhang, Y. Li, X. Xia, et al., Changes in protein oxidation, structure, and thermal stability of chicken breast subjected to ultrasound-assisted immersion freezing during frozen storage, Food Chem. 398 (2022) 133874. https://doi.org/10.1016/j.foodchem.2022.133874.

[6]

N. Lu, J. Ma, D.W. Sun, Enhancing physical and chemical quality attributes of frozen meat and meat products: Mechanisms, techniques and applications, Trends Food Sci. Technol. 124 (2022) 63-85. https://doi.org/10.1016/j.tifs.2022.04.004.

[7]

X. Chen, J. Wu, X. Li, et al., Investigation of the cryoprotective mechanism and effect on quality characteristics of surimi during freezing storage by antifreeze peptides, Food Chem. 371 (2022) 131054. https://doi.org/10.1016/j.foodchem.2021.131054.

[8]

A.J. Borderías, C.A. Tovar, F. Domínguez-Timón, et al., Characterization of healthier mixed surimi gels obtained through partial substitution of myofibrillar proteins by pea protein isolates, Food Hydrocoll. 107 (2020) 105976. https://doi.org/10.1016/j.foodhyd.2020.105976.

[9]

I. Tavernier, W. Wijaya, P. van der Meeren, et al., Food-grade particles for emulsion stabilization, Trends Food Sci. Technol. 50 (2016) 159-174. https://doi.org/10.1016/j.tifs.2016.01.023.

[10]

D.M. Cabezas, G.N. Pascual, J.R. Wagner, et al., Nanoparticles assembled from mixtures of whey protein isolate and soluble soybean polysaccharides. Structure, interfacial behavior and application on emulsions subjected to freeze-thawing, Food Hydrocoll. 95 (2019) 445-453. https://doi.org/10.1016/j.foodhyd.2019.04.040.

[11]

D.y. Zhu, Z.L. Kang, H.j. Ma, et al., Zhou, Effect of sodium chloride or sodium bicarbonate in the chicken batters: a physico-chemical and Raman spectroscopy study, Food Hydrocoll. 83 (2018) 222-228. https://doi.org/10.1016/j.foodhyd.2018.05.014.

[12]

R.E. López-Hernández, S.E. García-Solís, I. Monroy-Rodríguez, et al., Preparation and characterization of canola oil-in-water Pickering emulsions stabilized by barley starch nanocrystals, J. Food Eng. 326 (2022) 111037 https://doi.org/10.1016/j.foodhyd.2020.106206.

[13]

S. Li, B. Zhang, C.P. Tan, et al., Octenylsuccinate quinoa starch granulestabilized Pickering emulsion gels: preparation, microstructure and gelling mechanism, Food Hydrocoll. 91 (2019) 40-47. https://doi.org/10.1016/j.foodhyd.2019.01.001.

[14]

S. Thaiudom, K. Khantarat, Stability and rheological properties of fatreduced mayonnaises by using sodium octenyl succinate starch as fat replacer, Procedia Food Sci. 1 (2011) 315-321. https://doi.org/10.1016/j.profoo.2011.09.049.

[15]

X. Zhao, D. Li, L.J. Wang, et al., Rheological properties and microstructure of a novel starch-based emulsion gel produced by one-step emulsion gelation: effect of oil content, Carbohydr. Polym. 281 (2022) 119061. https://doi.org/10.1016/j.carbpol.2021.119061.

[16]

S. Li, B. Zhang, C. Li, et al., Pickering emulsion gel stabilized by octenylsuccinate quinoa starch granule as lutein carrier: role of the gel network, Food Chem. 305 (2020) 125476. https://doi.org/10.1016/j.foodchem.2019.125476.

[17]

K.B. Chin, M.Y. Go, Y.L. Xiong, Konjac flour improved textural and water retention properties of transglutaminase-mediated, heat-induced porcine myofibrillar protein gel: Effect of salt level and transglutaminase incubation, Meat Sci. 81 (2009) 565-572. https://doi.org/10.1016/j.meatsci.2008.10.012.

[18]

K. Cen, X. Yu, C. Gao, et al., Effects of quinoa protein Pickering emulsion on the properties, structure and intermolecular interactions of myofibrillar protein gel, Food Chem. 394 (2022) 133456. https://doi.org/10.1016/j.foodchem.2022.133456.

[19]

H. Wang, W. Zhang, X. Liu, et al., Effects of chickpea and peanut protein isolates on the gelling properties of hairtail (Trichiurus haumela) myosin, LWT-Food Sci. Technol. 163 (2022) 113562. https://doi.org/10.1016/j.lwt.2022.113562.

[20]

F. Li, B. Wang, B. Kong, et al., Decreased gelling properties of protein in mirror carp (Cyprinus carpio) are due to protein aggregation and structure deterioration when subjected to freeze-thaw cycles, Food Hydrocoll. 97 (2019) 105223. https://doi.org/10.1016/j.foodhyd.2019.105223.

[21]

H. Mi, Y. Li, C. Wang, et al., The interaction of starch-gums and their effect on gel properties and protein conformation of silver carp surimi, Food Hydrocoll. 112 (2021) 106290. https://doi.org/10.1016/j.foodhyd.2020.106290.

[22]

A.J.P. Alix, G. Pedanou, M. Berjot. Determination of the quantitative secondary structure of proteins by using some parameters of the Raman amide I band. J. Mol. Struct. 174 (1988) 159-164. https://doi.org/10.1016/0022-2860(88)80151-0.

[23]

L. Zhang, Y. Xue, J. Xu, et al., Effects of high-temperature treatment (≥ 100 ℃) on Alaska Pollock (Theragra chalcogramma) surimi gels, J. Food Eng. 115 (2013) 115-120. https://doi.org/10.1016/j.jfoodeng.2012.10.006.

[24]

F. Sun, Q. Huang, T. Hu, et al., Effects and mechanism of modified starches on the gel properties of myofibrillar protein from grass carp, Int. J. Biol. Macromol. 64 (2014) 17-24. https://doi.org/10.1016/j.ijbiomac.2013.11.019.

[25]

J. Yu, H. Xiao, Y. Xue, et al., Effects of soybean phospholipids, ovalbumin, and starch sodium octenyl succinate on the mechanical, microstructural, and flavor properties of emulsified surimi gels, LWT-Food Sci. Technol. (2022) 113260. https://doi.org/10.1016/j.lwt.2022.113260.

[26]

W. Kong, T. Zhang, D. Feng, et al., Effects of modified starches on the gel properties of Alaska Pollock surimi subjected to different temperature treatments, Food Hydrocoll. 56 (2016) 20-28. https://doi.org/10.1016/j.foodhyd.2015.11.023.

[27]

F. Li, X. Du, B. Wang, et al., Inhibiting effect of ice structuring protein on the decreased gelling properties of protein from quick-frozen pork patty subjected to frozen storage, Food Chem. 353 (2021) 129104. https://doi.org/10.1016/j.foodchem.2021.129104.

[28]

A. Gani, S. Benjakul, Impact of virgin coconut oil nanoemulsion on properties of croaker surimi gel, Food Hydrocoll. 82 (2018) 34-44. https://doi.org/10.1016/j.foodhyd.2018.03.037.

[29]

H. Dun, H. Liang, S. Li, et al., Influence of an O/W emulsion on the gelatinization, retrogradation and digestibility of rice starch with varying amylose contents, Food Hydrocoll. 113 (2021) 106547. https://doi.org/10.1016/j.foodhyd.2020.106547.

[30]

R. Jia, T. Katano, Y. Yoshimoto, et al., Sweet potato starch with low pasting temperature to improve the gelling quality of surimi gels after freezing, Food Hydrocoll. 81 (2018) 467-473. https://doi.org/10.1016/j.foodhyd.2018.03.024.

[31]

Y. Michiaki, K. Shiro, Hydrolytic action of salmon cathepsins B and L to muscle structural proteins in respect of muscle softening, Nippon. Suisan. 7(10) (1991) 1917-1922. https://doi.org/10.2331/suisan.57.1917.

[32]

S. Benjakul, W. Visessanguan, C. Thongkaew, et al., Effect of frozen storage on chemical and gel-forming properties of fish commonly used for surimi production in Thailand, Food Hydrocoll. 19 (2005) 197-207. https://doi.org/10.1016/j.foodhyd.2004.05.004.

[33]

J. Connell, Aggregation of cod myosin during frozen storage, Nature 183 (1959) 664-665. https://doi.org/10.1038/183664a0.

[34]

M. Fan, T. Hu, S. Zhao, et al., Gel characteristics and microstructure of fish myofibrillar protein/cassava starch composites, Food Chem. 218 (2017) 221-230. https://doi.org/10.1016/j.foodchem.2016.09.068.

[35]

X. Zhou, H. Chen, F. Lyu, et al., Physicochemical properties and microstructure of fish myofibrillar protein-lipid composite gels: effects of fat type and concentration, Food Hydrocoll. 90 (2019) 433-442. https://doi.org/10.1016/j.foodhyd.2018.12.032.

[36]

N. Buamard, S. Benjakul, Effect of ethanolic coconut husk extract and preemulsification on properties and stability of surimi gel fortified with seabass oil during refrigerated storage, LWT-Food Sci. Technol. 108 (2019) 160-167. https://doi.org/10.1016/j.lwt.2019.03.038.

[37]

E. Puolanne, M. Halonen, Theoretical aspects of water-holding in meat, Meat Sci. 86 (2010) 151-165. https://doi.org/10.1016/j.meatsci.2010.04.038.

[38]

Y. Xu, Y. Lv, H. Zhao, et al., Diacylglycerol pre-emulsion prepared through ultrasound improves the gel properties of golden thread surimi, Ultrason. Sonochem. 82 (2022) 105915. https://doi.org/10.1016/j.ultsonch.2022.105915.

[39]

Y. Wang, W. Wang, H. Jia, et al., Using cellulose nanofibers and its palm oil Pickering emulsion as fat substitutes in emulsified sausage, J. Food Sci. 83 (2018) 1740-1747. https://doi.org/10.1111/1750-3841.14164.

[40]

R.M. Syamaladevi, K.N. Manahiloh, B. Muhunthan, et al., Understanding the Influence of state/phase transitions on ice recrystallization in Atlantic Salmon (Salmo salar) during frozen storage, Food Biophys. 7 (2011) 57-71. https://doi.org/10.1007/s11483-011-9243-y.

[41]

M. Tan, Z. Lin, Y. Zu, et al., Effect of multiple freeze-thaw cycles on the quality of instant sea cucumber: emphatically on water status of by LFNMR and MRI, Food Res. Int. 109 (2018) 65-71. https://doi.org/10.1016/j.foodres.2018.04.029.

[42]

L. Fan, D. Ruan, J. Shen, et al., The role of water and oil migration in juiciness loss of stuffed fish ball with the fillings of pig fat/meat as affected by freeze-thaw cycles and cooking process, LWT-Food Sci. Technol. 159 (2022) 113244. https://doi.org/10.1016/j.lwt.2022.113244.

[43]
T.C. Lanier, Interactions of muscle and nonmuscle proteins affecting heat-set gel rheology, in: N. Parris, R. Barford (Eds.), Interactions of food proteins, ACS Publicatins, 1991, pp. 268-284. https://doi.org/10.1021/bk-1991-0454.ch019.
DOI
[44]

X. Feng, F. Zhang, Y. Chen, et al., Effects of adding quinoa protein Pickering emulsion on freeze-thaw stability of fish surimi gel, Scientia Agricultura Sinica 10 (2022) 2038-2046.

[45]

Q. Fang, L. Shi, Z. Ren, et al., Effects of emulsified lard and TGase on gel properties of threadfin bream (Nemipterus virgatus) surimi, LWT-Food Sci. Technol. 146 (2021) 111513. https://doi.org/10.1016/j.lwt.2021.111513.

[46]

N.Z. Ballin, R. Lametsch, Analytical methods for authentication of fresh vs. thawed meat - a review, Meat Sci. 80 (2008) 151-158. https://doi.org/10.1016/j.meatsci.2007.12.024.

[47]

X. Zhou, S. Jiang, D. Zhao, et al., Changes in physicochemical properties and protein structure of surimi enhanced with camellia tea oil, LWT-Food Sci. Technol. 84 (2017) 562-571. https://doi.org/10.1016/j.lwt.2017.03.026.

[48]

J. Chen, T. Deng, C. Wang, et al., Effect of hydrocolloids on gel properties and protein secondary structure of silver carp surimi, J. Sci. Food Agr. 100 (2020) 2252-2260. https://doi.org/10.1002/jsfa.10254

[49]

I. Sánchez-González, A. Rodríguez-Casado, M. Careche, et al., Raman analysis of surimi gelation by addition of wheat dietary fibre, Food Chem. 112 (2009) 162-168. https://doi.org/10.1016/j.foodchem.2008.05.054.

[50]

S.M. Choi, C.Y. Ma, Structural characterization of globulin from common buckwheat (Fagopyrum esculentum Moench) using circular dichroism and Raman spectroscopy, Food Chem. 102 (2007) 150-160. https://doi.org/10.1016/j.foodchem.2006.05.011.

[51]

M. Guo, S. Liu, M. Ismail, et al., Changes in the myosin secondary structure and shrimp surimi gel strength induced by dense phase carbon dioxide, Food Chem. 227 (2017) 219-226. https://doi.org/10.1016/j.foodchem.2017.01.050.

[52]

C. Yu, F. Wu, Y. Cha, et al., Effects of high-pressure homogenization on functional properties and structure of mussel (Mytilus edulis) myofibrillar proteins, Int. J. Biol. Macromol. 118 (2018) 741-746. https://doi.org/10.1016/j.ijbiomac.2018.06.134.

[53]

A. Amiri, P. Sharifian, N. Soltanizadeh, Application of ultrasound treatment for improving the physicochemical, functional and rheological properties of myofibrillar proteins, Int. J. Biol. Macromol. 111 (2018) 139-147. https://doi.org/10.1016/j.ijbiomac.2017.12.167.

[54]

C. Li, Y.L. Xiong, Disruption of secondary structure by oxidative stress alters the cross-linking pattern of myosin by microbial transglutaminase, Meat Sci. 108 (2015) 97-105. https://doi.org/10.1016/j.meatsci.2015.05.024.

[55]

M. Pan, F. Xu, Y. Wu, et al., Application of ultrasound-assisted physical mixing treatment improves in vitro protein digestibility of rapeseed napin, Ultrason. Sonochem. 67 (2020) 105136. https://doi.org/10.1016/j.ultsonch.2020.105136.

[56]

J. Guo, Y. Zhou, K. Yang, et al., Effect of low-frequency magnetic field on the gel properties of pork myofibrillar proteins, Food Chem. 274 (2019) 775-781. https://doi.org/10.1016/j.foodchem.2018.09.028.

[57]

A.M. Herrero, Raman spectroscopy a promising technique for quality assessment of meat and fish: a review, Food Chem. 107 (2008) 1642-1651. https://doi.org/10.1016/j.foodchem.2007.10.014.

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Publication history

Received: 27 August 2022
Revised: 13 September 2022
Accepted: 04 October 2022
Published: 25 September 2023
Issue date: March 2024

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© 2024 Beijing Academy of Food Sciences. Publishing services by Tsinghua University Press.

Acknowledgements

Acknowledgements

This work was supported by the National Natural Science Foundation of China (U20A2067, 32272360). The authors would like to express gratitude to all the reviewers who participated in the review, as well as MJEditor (www.mjeditor.com) for providing English editing services during the preparation of this manuscript.

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This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).

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