Effect of Interaction between Soy Protein Isolate and <i>Nemipterus virgatus</i> Myosin on Its Gel Properties

LIU Zhen; WANG Jinxiang; LI Xuepeng; GAO Ruichang; LI Jianrong; YI Shumin; YANG Qing; WEI Zhengpeng; JI Guangren

doi:10.13386/j.issn1002-0306.2022110207

Volume 44 Issue 16

Aug. 2023

Turn off MathJax

Article Contents

Abstract

References

Science and Technology of Food Industry > 2023 > 44(16): 122-130. > DOI: 10.13386/j.issn1002-0306.2022110207

LIU Zhen, WANG Jinxiang, LI Xuepeng, et al. Effect of Interaction between Soy Protein Isolate and Nemipterus virgatus Myosin on Its Gel Properties[J]. Science and Technology of Food Industry, 2023, 44(16): 122−130. (in Chinese with English abstract). doi: 10.13386/j.issn1002-0306.2022110207.

Citation:

PDF (2003 KB)

Effect of Interaction between Soy Protein Isolate and Nemipterus virgatus Myosin on Its Gel Properties

1.
College of Food Science and Engineering, Bohai University, National Technology Research and Development Sub-center for Surimi and Surimi Products Processing, Jinzhou 121013, China
2.
College of Food and Biotechnology Engineering, Jiangsu University, Zhenjiang 212013, China
3.
Rongcheng Taixiang Food Products Co., Ltd., Ministry of Agriculture Key Laboratory of Frozen Prepared Marine Foods Processing, Weihai 234309, China
4.
Jinzhou Bijiashan Food Co., Ltd., Jinzhou 121007, China

More Information

Received Date: November 20, 2022
Available Online: June 15, 2023

Graphical Abstract

Abstract

Abstract

In this study, myosin isolated from Nemipterus virgatus was added with 0%~8%（w/w）soybean protein isolate (SPI) and the physicochemical, spectroscopic, and gel properties of the composite system were analyzed, in order to investigate the effect of interaction between myosin and SPI on the gel properties of myosin. The results showed that after the addition of SPI, the endogenous fluorescence intensity of the composite system decreased, whereas the ultraviolet absorbance, the total sulfhydryl content, and hydrogen bond as well as hydrophobic interactions increased. These results indicated that there were the hydrophobic interactions, hydrogen bonds, disulfide bonds, and other covalent and non-covalent interactions between SPI and Nemipterus virgatus myosin, which altered the structure and conformation of myosin. Meanwhile, the gel strength, hardness, and β-sheet content of the myosin-SPI composite gels all increased initially and then decreased as the increase addition of SPI. Furthermore, the total sulfhydryl and hydrophobic contents of the myosin-SPI composite system got the highest values when added 4% SPI, which increased by 64.46% and 13.53% compared with the control group, respectively. The gel strength and hardness of the myosin-SPI composite gels were also reached the highest values when added 4% SPI, which increased by 8.66% and 9.21% compared with the control group, respectively. It was also found that a part of α-helices transformed into β-sheets and the gel network was most compact and homogeneous. Therefore, the moderate addition of SPI could promote the aggregation and cross-linking of myosin through the interaction forces such as hydrophobic interactions, hydrogen bonds, and disulfide bonds, and improve the gel properties of myosin.
- Nemipterus virgatus myosin,
- soybean protein isolate,
- interaction,
- gel property

FullText(HTML)

References (39)

References

[1]	LIU J Y, YOSHIDA A, GAO Y L, et al. Purification and characterization of a sarcoplasmic serine proteinase from threadfin bream Nemipterus virgatus muscle[J]. Food Chemistry,2019,284:198−204. doi: 10.1016/j.foodchem.2019.01.024
[2]	ZHU Z W, LANIER T C, FARKAS B E. High pressure effects on heat-induced gelation of threadfin bream (Nemipterus spp.) surimi[J]. Journal of Food Engineering,2015,146:23−27. doi: 10.1016/j.jfoodeng.2014.08.021
[3]	鲍佳彤. 外源添加物对未漂洗鲶鱼鱼糜凝胶形成的影响[D]. 天津: 天津农学院, 2020 BAO J T. Effects of exogenous additives on surimi gel formation in unwashed catfish[D]. Tianjin: Tianjin Agricultural University, 2020.
[4]	叶月华, 钱敏, 刘晓艳, 等. 不同外源物质对淡水鱼鱼糜热诱导凝胶特性增效作用的研究进展[J]. 食品与发酵工业,2021,47(12):285−293. [YE Y H, QIAN M, LIU X Y, et al. Research progress on the enhancement effects of different exogenous substances on thermal-induced gel properties of fresh water fish surimi[J]. Food and Fermentation Industries,2021,47(12):285−293. doi: 10.13995/j.cnki.11-1802/ts.026634 Ye Y H, Qian M, Liu X Y, et al. Research progress on the enhancement effects of different exogenous substances on thermal-induced gel properties of fresh water fish surimi[J]. Food and Fermentation Industries, 2021, 47(12): 285-293. doi: 10.13995/j.cnki.11-1802/ts.026634
[5]	王丽丽, 杨文鸽, 徐大伦, 等. 外源添加物对鱼糜及其制品凝胶性能影响的研究[J]. 核农学报,2015,29(10):1985−1990. [WANG L L, YANG W G, XU D L, et al. Effects of exogenous additives on gel properties of surimi and its products[J]. Journal of Nuclear Agricultural Sciences,2015,29(10):1985−1990. doi: 10.11869/j.issn.100-8551.2015.10.1985 WANG L L, YANG W G, XU D L, et al. Effects of exogenous additives on gel properties of surimi and its products[J]. Journal of Nuclear Agricultural Sciences, 2015, 29(10): 1985-1990. doi: 10.11869/j.issn.100-8551.2015.10.1985
[6]	彭晶. 菜籽蛋白的制备及其对白鲢鱼糜凝胶特性的影响[D]. 武汉: 华中农业大学, 2017 PENG J. Study on the preparation of rapeseed protein and its effect on the gelation of silver carp surumi[D]. Wuhan: Huazhong Agricultural University, 2017.
[7]	BORDERÍAS A J, TOVAR C A, DOMÍNGUEZ-TIMÓN F, et al. Characterization of healthier mixed surimi gels obtained through partial substitution of myofibrillar proteins by pea protein isolates[J]. Food Hydrocolloids,2020,107:105976. doi: 10.1016/j.foodhyd.2020.105976
[8]	WANG H N, ZHANG W, LIU X L, et al. Effects of chickpea and peanut protein isolates on the gelling properties of hairtail (Trichiurus haumela) myosin[J]. LWT-Food Science and Technology,2022,163:113562. doi: 10.1016/j.lwt.2022.113562
[9]	CHEN N N, ZHAO M M, CHASSENIEUX C, et al. The effect of adding NaCl on thermal aggregation and gelation of soy protein isolate[J]. Food Hydrocolloids,2017,70:88−95. doi: 10.1016/j.foodhyd.2017.03.024
[10]	WANG Z J, LIANG J, JIANG L Z, et al. Effect of the interaction between myofibrillar protein and heat-induced soy protein isolates on gel properties[J]. CyTA-Journal of Food,2015,13(4):527−534.
[11]	LUO Y K, SHEN H X, PAN D D, et al. Gel properties of surimi from silver carp (Hypophthalmichthys molitrix) as affected by heat treatment and soy protein isolate[J]. Food Hydrocolloids,2008,22(8):1513−1519. doi: 10.1016/j.foodhyd.2007.10.003
[12]	崔旭海, 毕海丹, 崔晓莹, 等. 不同食用蛋白的添加对鲤鱼鱼糜流变和凝胶特性的影响[J]. 食品工业科技,2018,39(16):195−200, 225. [CUI X H, BI H D, CUI X Y, et al. Effects of the edible protein on rheological and gel properties of carp surimi[J]. Science and Technology of Food Industry,2018,39(16):195−200, 225. doi: 10.13386/j.issn1002-0306.2018.16.035 CUI X H, BI H D, CUI X Y, et al. Effects of the edible protein on rheological and gel properties of carp surimi[J]. Science and Technology of Food Industry, 2018, 39(16): 195-200, 225. doi: 10.13386/j.issn1002-0306.2018.16.035
[13]	武雅琴, 王莉莎, 邹咪, 等. 热诱导大豆分离蛋白对肌原纤维蛋白凝胶特性的影响[J]. 食品与发酵工业,2019,45(10):60−65. [WU Y Q, WANG L S, ZOU M, et al. Effects of heat-induced soy protein isolate on gel properties of myofibrillar proteins[J]. Food and Fermentation Industries,2019,45(10):60−65. doi: 10.13995/j.cnki.11-1802/ts.018951 WU Y Q, WANG L S, ZOU M, et al. Effects of heat-induced soy protein isolate on gel properties of myofibrillar proteins[J]. Food and Fermentation Industries, 2019, 45(10): 60-65. doi: 10.13995/j.cnki.11-1802/ts.018951
[14]	LIN D Q, ZHANG L T, LI R J, et al. Effect of plant protein mixtures on the microstructure and rheological properties of myofibrillar protein gel derived from red sea bream (Pagrosomus major)[J]. Food Hydrocolloids,2019,96:537−545. doi: 10.1016/j.foodhyd.2019.05.043
[15]	MI H B, ZHAO Y M, LI Y, et al. Combining effect of soybean protein isolate and transglutaminase on the gel properties of Zhikong scallop (Chlamys farreri) adductor muscle[J]. LWT-Food Science and Technology,2021,138:110727. doi: 10.1016/j.lwt.2020.110727
[16]	PARK J W, LANIER T C. Scanning calorimetric behavior of tilapia myosin and actin due to processing of muscle and protein purification[J]. Journal of Food Science,1989,54(1):49−51. doi: 10.1111/j.1365-2621.1989.tb08564.x
[17]	李政翰. 玉米淀粉-脂肪酸-带鱼肌球蛋白间的相互作用机制研究[D]. 锦州: 渤海大学, 2020 LI Z H. Interaction mechanism of corn starch-fatty acid-hairtail myosin[D]. Jinzhou: Bohai University, 2020.
[18]	YONGSAWATDIGUL J, PARK J W. Thermal denaturation and aggregation of threadfin bream actomyosin[J]. Food Chemistry,2003,83(3):409−416. doi: 10.1016/S0308-8146(03)00105-5
[19]	SUN L C, LIN Y C, LIU W F, et al. Effect of pH shifting on conformation and gelation properties of myosin from skeletal muscle of blue round scads (Decapterus maruadsi)[J]. Food Hydrocolloids,2019,93:137−145. doi: 10.1016/j.foodhyd.2019.02.026
[20]	GÓMEZ-GUILLÉN M C, BORDERÍAS A J, MONTERO P, et al. Chemical interactions of nonmuscle proteins in the network of sardine (Sardina pilchardus) muscle gels[J]. LWT-Food Science and Technology,1997,30(6):602−608. doi: 10.1006/fstl.1997.0239
[21]	SHIMADA M, TAKAI E, EJIMA D, et al. Heat-induced formation of myosin oligomer-soluble filament complex in high-salt solution[J]. International Journal of Biological Macromolecules,2015,73:17−22. doi: 10.1016/j.ijbiomac.2014.11.005
[22]	NIU H L, LI Y, HAN J C, et al. Gelation and rheological properties of myofibrillar proteins influenced by the addition of soybean protein isolates subjected to an acidic pH treatment combined with a mild heating[J]. Food Hydrocolloids,2017,70:269−276. doi: 10.1016/j.foodhyd.2017.04.001
[23]	CAO Y Y, XIA T L, ZHOU G H, et al. The mechanism of high pressure-induced gels of rabbit myosin[J]. Innovative Food Science & Emerging Technologies,2012,16:41−46.
[24]	DU X, ZHAO M, PAN N, et al. Tracking aggregation behaviour and gel properties induced by structural alterations in myofibrillar protein in mirror carp (Cyprinus carpio) under the synergistic effects of pH and heating. Food Chemistry, 2021, 362: 130222.
[25]	WANG K Q, LUO S Z, ZHONG X Y, et al. Changes in chemical interactions and protein conformation during heat-induced wheat gluten gel formation[J]. Food Chemistry,2017,214:393−399. doi: 10.1016/j.foodchem.2016.07.037
[26]	TANG C H, YANG X Q, CHEN Z, et al. Physicochemical and structural characteristics of sodium caseinate biopolymers induced by microbial transglutaminase[J]. Journal of Food Biochemistry,2005,29(4):402−421. doi: 10.1111/j.1745-4514.2005.00038.x
[27]	ZHANG L, WANG P, YANG Z Y, et al. Molecular dynamics simulation exploration of the interaction between curcumin and myosin combined with the results of spectroscopy techniques[J]. Food Hydrocolloids,2020,101:105455. doi: 10.1016/j.foodhyd.2019.105455
[28]	ACHARYA D P, SANGUANSRI L, AUGUSTIN M A. Binding of resveratrol with sodium caseinate in aqueous solutions[J]. Food Chemistry,2013,141(2):1050−1054. doi: 10.1016/j.foodchem.2013.03.037
[29]	LÜ Y Q, XU L L, SU Y J, et al. Effect of soybean protein isolate and egg white mixture on gelation of chicken myofibrillar proteins under salt/-free conditions[J]. LWT-Food Science and Technology,2021,149:111871. doi: 10.1016/j.lwt.2021.111871
[30]	邓立青. 不同辅料添加量对铜盘鱼鱼糜凝胶强度的影响[J]. 肉类工业,2020,40(8):19−22. [DENG L Q. Effect of the addition amount of different auxiliary material on the gel strength of copper plate fish surimi[J]. Meat Industry,2020,40(8):19−22. DENG L Q. Effect of the addition amount of different auxiliary material on the gel strength of copper plate fish surimi[J]. Meat Industry, 2020, 40(8): 19-22.
[31]	ZHOU X X, CHEN T, LIN H H, et al. Physicochemical properties and microstructure of surimi treated with egg white modified by tea polyphenols[J]. Food Hydrocolloids,2019,90:82−89. doi: 10.1016/j.foodhyd.2018.07.031
[32]	于繁千惠, 孔文俊, 韦依侬, 等. 小麦蛋白和谷氨酰胺转氨酶对120 ℃高温处理鱼糜凝胶特性影响的研究[J]. 食品工业科技,2016,37(21):81−85. [YU F Q H, KONG W J, WEI Y N, et al. Effects of wheat protein and transglutaminase on gel properties of surimi heated at 120 ℃ high temperature[J]. Science and Technology of Food Industry,2016,37(21):81−85. YU F Q H, KONG W J, WEI Y N, et al. Effects of wheat protein and transglutaminase on gel properties of surimi heated at 120 ℃ high temperature[J]. Science and Technology of Food Industry, 2016, 37(21): 81-85.
[33]	王聪. 淀粉和亲水胶体对白鲢鱼鱼糜凝胶特性的增效作用研究[D]. 锦州: 渤海大学, 2019 WANG C. Synergistic effect of starch and hydrocolloid on gel properties of silver carp surimi[D]. Jinzhou: Bohai University, 2019.
[34]	LI T F, ZHAO J X, HUANG J, et al. Improvement of the quality of surimi products with overdrying potato starches[J]. Journal of Food Quality,2017,2017:1−5.
[35]	CHEN J X, DENG T Y, WANG C, et al. Effect of hydrocolloids on gel properties and protein secondary structure of silver carp surimi[J]. Journal of the Science of Food and Agriculture,2020,100(5):2252−2260. doi: 10.1002/jsfa.10254
[36]	YUAN L, YU J M, MU J L, et al. Effects of deacetylation of konjac glucomannan on the physico-chemical properties of surimi gels from silver carp (Hypophthalmichthys molitrix)[J]. RSC Advances,2019,9(34):19828−19836. doi: 10.1039/C9RA03517F
[37]	汪坤霞. 莲藕淀粉对鲢鱼鱼糜凝胶特性的影响[D]. 武汉: 华中农业大学, 2017 WANG K X. Effects of lotus starch on gelation properties of silver carp surimi[D]. Wuhan: Huazhong Agricultural University, 2017.
[38]	杨玲玲. 卵白蛋白-大豆分离蛋白对肉糜凝胶特性的影响[D]. 南昌: 江西农业大学, 2020 YANG L L. Effect of ovalbumin-soybean protein isolate on gelation characteristics of meat[D]. Nanchang: Jiangxi Agricultural University, 2020.
[39]	姜鹏飞, 于文静, 朱凯悦, 等. 多糖对罗非鱼鱼糜凝胶化行为的影响[J]. 中国食品学报,2023,23(1):87−99. [JIANG P F, YU W J, ZHU K Y, et al. Effect of polysaccharides on gelation behavior of tilapia surimi[J]. Chinese Journal of Food Science,2023,23(1):87−99. doi: 10.16429/j.1009-7848.2023.01.009 JIANG P F, YU W J, ZHU K Y, et al. Effect of polysaccharides on gelation behavior of tilapia surimi[J]. Chinese Journal of Food Science, 2023, 23(1): 87-99. doi: 10.16429/j.1009-7848.2023.01.009