Effect of High Intensity Ultrasound on the Conformational and Physicochemical Properties of Soy 7S and 11S Globulin

TIAN Ran; FENG Junran; SUI Xiaonan; JIANG Lianzhou

doi:10.13386/j.issn1002-0306.2021060028

Volume 43 Issue 5

Feb. 2022

Turn off MathJax

Article Contents

Abstract

References

Science and Technology of Food Industry > 2022 > 43(5): 87-97. > DOI: 10.13386/j.issn1002-0306.2021060028

TIAN Ran, FENG Junran, SUI Xiaonan, et al. Effect of High Intensity Ultrasound on the Conformational and Physicochemical Properties of Soy 7S and 11S Globulin[J]. Science and Technology of Food Industry, 2022, 43(5): 87−97. (in Chinese with English abstract). doi: 10.13386/j.issn1002-0306.2021060028.

Citation:

PDF (4905 KB)

Effect of High Intensity Ultrasound on the Conformational and Physicochemical Properties of Soy 7S and 11S Globulin

College of Food, Northeast Agricultural University, Harbin 150030, China

More Information

Received Date: June 02, 2021
Available Online: December 28, 2021

Graphical Abstract

Abstract

Abstract

The effects of high intensity ultrasound treatment (150, 450, 1350 W) on the conformational and physicochemical properties of soy 7S and 11S globulin for different durations (15, 30 min) were investigated. The results showed that ultrasound treatment did not change the primary structures of 7S and 11S, but were able to change the content of the components in the secondary structure. Ultrasound treatment resulted varying degrees of reduction in fluorescence intensity and a significant increase (P<0.05) in surface hydrophobicity (H₀) for 7S and 11S. Particle size distribution measurements showed that the droplets of 7S and 11S were more uniformly distributed after ultrasound treatment and that the stability of the protein solutions was improved. Differential scanning calorimetry (DSC) results showed that the enthalpy (ΔH) decreased from 1.22 J/g to 0.17 J/g for 7S and from 1.41 J/g to 0.53 J/g for 11S after sonication, requiring less energy to unfold the protein structure. In terms of physicochemical properties, the emulsification activity and emulsion stability of 7S and 11S increased significantly (P<0.05) after sonication, and the solubility increased by up to 12.85% and 10.57%, respectively. In addition, cryo-scanning electron microscopy (Cryo-SEM) observations revealed that the microstructure of 7S and 11S changed after sonication from a more ordered reticular aggregated state to a disordered state. Thus, high intensity ultrasound treatment can obviously affect the structure and physicochemical properties of 7S and 11S.
- soy protein,
- 7S/11S,
- high intensity ultrasound,
- structure,
- physicochemical properties

FullText(HTML)

References (60)

References

[1]	HUANG L R, DING X N, Li Y L, et al. The aggregation, structures and emulsifying properties of soybean protein isolate induced by ultrasound and acid[J]. Food Chemistry,2019,279:114−119. doi: 10.1016/j.foodchem.2018.11.147
[2]	MARUYAMA N, ADACHI M, TAKAHASHI K, et al. Crystal structures of recombinant and native soybean β-conglycinin β homotrimers[J]. European Journal of Biochemistry,2001,268(12):3595−3604. doi: 10.1046/j.1432-1327.2001.02268.x
[3]	KITAMURA K, SHIBASAKI K. Isolation and some physico-chemical properties of the acidic subunits of soybean 11S globulin[J]. Agricultural and Biological Chemistry,1975,39(5):945−951.
[4]	JIANG J, CHEN J, XIONG Y L. Structural and emulsifying properties of soy protein isolate subjected to acid and alkaline pH-shifting processes[J]. Journal of Agricultural and Food Chemistry,2009,57(16):7576−7583. doi: 10.1021/jf901585n
[5]	SUN X Y, ZHANG W, ZHANG L F, et al. Effect of ultrasound‐assisted extraction on the structure and emulsifying properties of peanut protein isolate[J]. Journal of the Science of Food and Agriculture,2021,101(3):1150−1160. doi: 10.1002/jsfa.10726
[6]	MA X B, YAN T Y, HOU F R, et al. Formation of soy protein isolate (SPI)-citrus pectin (CP) electrostatic complexes under a high-intensity ultrasonic field: Linking the enhanced emulsifying properties to physicochemical and structural properties[J]. Ultrasonics sonochemistry,2019,59:104748. doi: 10.1016/j.ultsonch.2019.104748
[7]	MCCLEMENTS D J. Advances in the application of ultrasound in food analysis and processing[J]. Trends in Food Science & Technology,1995,6(9):293−299.
[8]	FAN X J, LI S, ZHANG A, et al. Mechanism of change of the physicochemical characteristics, gelation process, water state, and microstructure of okara tofu analogues induced by high-intensity ultrasound treatment[J]. Food Hydrocolloids,2021,111:106241. doi: 10.1016/j.foodhyd.2020.106241
[9]	O’SULLIVAN J J, PARK M, BEEVERS J, et al. Applications of ultrasound for the functional modification of proteins and nanoemulsion formation: A review[J]. Food Hydrocolloids,2017,71:299−310. doi: 10.1016/j.foodhyd.2016.12.037
[10]	MORALES R, MARTÍNEZ K D, RUIZ-HENESTROSA V M P, et al. Modification of foaming properties of soy protein isolate by high ultrasound intensity: Particle size effect[J]. Ultrasonics Sonochemistry,2015,26:48−55. doi: 10.1016/j.ultsonch.2015.01.011
[11]	ZHENG T, LI X H, TAHA A, et al. Effect of high intensity ultrasound on the structure and physicochemical properties of soy protein isolates produced by different denaturation methods[J]. Food Hydrocolloids,2019,97:105216. doi: 10.1016/j.foodhyd.2019.105216
[12]	MATSUMURA Y, SIRISON J, ISHI T, et al. Soybean lipophilic proteins-Origin and functional properties as affected by interaction with storage proteins[J]. Current Opinion in Colloid & Interface Science,2017,28:120−128.
[13]	JUNG S, RICKERT D, DEAK N, et al. Comparison of Kjeldahl and Dumas methods for determining protein contents of soybean products[J]. Journal of the American Oil Chemists' Society,2003,80(12):1169. doi: 10.1007/s11746-003-0837-3
[14]	MARGULIS M, MARGULIS I. Calorimetric method for measurement of acoustic power absorbed in a volume of a liquid[J]. Ultrasonics Sonochemistry,2003,10(6):343−345. doi: 10.1016/S1350-4177(03)00100-7
[15]	WU D, WU C, MA W C, et al. Effects of ultrasound treatment on the physicochemical and emulsifying properties of proteins from scallops (Chlamys farreri)[J]. Food Hydrocolloids,2019,89:707−714. doi: 10.1016/j.foodhyd.2018.11.032
[16]	TIAN R, FENG J R, HUANG G, et al. Ultrasound driven conformational and physicochemical changes of soy protein hydrolysates[J]. Ultrasonics Sonochemistry,2020,68:105202. doi: 10.1016/j.ultsonch.2020.105202
[17]	KATO A, NAKAI S. Hydrophobicity determined by a fluorescence probe method and its correlation with surface properties of proteins[J]. Biochimica et Biophysica acta (BBA)-Protein Structure,1980,624(1):13−20. doi: 10.1016/0005-2795(80)90220-2
[18]	LOWRY O H, ROSEBROUGH N J, FARR A L, et al. Protein measurement with the Folin phenol reagent[J]. Journal of Biological Chemistry,1951,193:265−275. doi: 10.1016/S0021-9258(19)52451-6
[19]	REN C, XIONG W F, LI J, et al. Comparison of binding interactions of cyanidin-3-O-glucoside to β-conglycinin and glycinin using multi-spectroscopic and thermodynamic methods[J]. Food Hydrocolloids,2019,92:155−162. doi: 10.1016/j.foodhyd.2019.01.053
[20]	NAZARI B, MOHAMMADIFAR M A, SHOJAEE-ALIABADI S, et al. Effect of ultrasound treatments on functional properties and structure of millet protein concentrate[J]. Ultrasonics Sonochemistry,2018,41:382−388. doi: 10.1016/j.ultsonch.2017.10.002
[21]	JAMDAR S, HARIKUMAR P. A rapid autolytic method for the preparation of protein hydrolysate from poultry viscera[J]. Bioresource Technology,2008,99(15):6934−6940. doi: 10.1016/j.biortech.2008.01.023
[22]	WHITBY C P, FORNASIERO D, RALSTON J. Effect of adding anionic surfactant on the stability of Pickering emulsions[J]. Journal of Colloid and Interface Science,2009,329(1):173−181. doi: 10.1016/j.jcis.2008.09.056
[23]	SUI X N, ZHANG T Y, JIANG L Z. Soy protein: Molecular structure revisited and recent advances in processing technologies[J]. Annual Review of Food Science and Technology,2020,12:119−147.
[24]	O'SULLIVAN J, MURRAY B, FLYNN C, et al. The effect of ultrasound treatment on the structural, physical and emulsifying properties of animal and vegetable proteins[J]. Food hydrocolloids,2016,53:141−154. doi: 10.1016/j.foodhyd.2015.02.009
[25]	O'SULLIVAN J, ARELLANO M, PICHOT R, et al. The effect of ultrasound treatment on the structural, physical and emulsifying properties of dairy proteins[J]. Food Hydrocolloids,2014,42:386−396. doi: 10.1016/j.foodhyd.2014.05.011
[26]	JACKSON M, MANTSCH H H. The use and misuse of FTIR spectroscopy in the determination of protein structure[J]. Critical reviews in Biochemistry and Molecular biology,1995,30(2):95−120. doi: 10.3109/10409239509085140
[27]	VERA A, VALENZUELA M, YAZDANI-PEDRAM M, et al. Conformational and physicochemical properties of quinoa proteins affected by different conditions of high-intensity ultrasound treatments[J]. Ultrasonics Sonochemistry,2019,51:186−196. doi: 10.1016/j.ultsonch.2018.10.026
[28]	ZHAO J, HE J, DANG Y L, et al. Ultrasound treatment on the structure of goose liver proteins and antioxidant activities of its enzymatic hydrolysate[J]. Journal of Food Biochemistry,2020,44(1):e13091.
[29]	XU B, YUAN J, WANG L, et al. Effect of multi-frequency power ultrasound (MFPU) treatment on enzyme hydrolysis of casein[J]. Ultrasonics Sonochemistry,2020,63:104930. doi: 10.1016/j.ultsonch.2019.104930
[30]	MA X B, HOU F R, ZHAO H H, et al. Conjugation of soy protein isolate (SPI) with pectin by ultrasound treatment[J]. Food Hydrocolloids,2020,108:106056. doi: 10.1016/j.foodhyd.2020.106056
[31]	LI K, FU L, ZHAO Y Y, et al. Use of high-intensity ultrasound to improve emulsifying properties of chicken myofibrillar protein and enhance the rheological properties and stability of the emulsion[J]. Food Hydrocolloids,2020,98:105275. doi: 10.1016/j.foodhyd.2019.105275
[32]	ZOU H N, ZHAO N, SUN S, et al. High-intensity ultrasonication treatment improved physicochemical and functional properties of mussel sarcoplasmic proteins and enhanced the stability of oil-in-water emulsion[J]. Colloids and Surfaces A:Physicochemical and Engineering Aspects,2020,589:124463. doi: 10.1016/j.colsurfa.2020.124463
[33]	WANG J Y, YANG Y L, TANG X Z, et al. Effects of pulsed ultrasound on rheological and structural properties of chicken myofibrillar protein[J]. Ultrasonics Sonochemistry,2017,38:225−233. doi: 10.1016/j.ultsonch.2017.03.018
[34]	WANG F, ZHANG Y Z, XU L, et al. An efficient ultrasound-assisted extraction method of pea protein and its effect on protein functional properties and biological activities[J]. LWT,2020,127:109348. doi: 10.1016/j.lwt.2020.109348
[35]	XIONG W F, WANG Y T, ZHANG C L, et al. High intensity ultrasound modified ovalbumin: Structure, interface and gelation properties[J]. Ultrasonics Sonochemistry,2016,31:302−309. doi: 10.1016/j.ultsonch.2016.01.014
[36]	WEN Q H, TU Z C, ZHANG L, et al. Effect of high intensity ultrasound on the gel and structural properties of Ctenopharyngodon idellus myofibrillar protein[J]. Journal of Food Biochemistry,2017,41(1):e12288. doi: 10.1111/jfbc.12288
[37]	LI Y H, CHENG Y, ZHANG Z L, et al. Modification of rapeseed protein by ultrasound-assisted pH shift treatment: Ultrasonic mode and frequency screening, changes in protein solubility and structural characteristics[J]. Ultrasonics Sonochemistry,2020,69:105240. doi: 10.1016/j.ultsonch.2020.105240
[38]	ZHANG M C, LI F F, DIAO X P, et al. Moisture migration, microstructure damage and protein structure changes in porcine longissimus muscle as influenced by multiple freeze-thaw cycles[J]. Meat Science,2017,133:10−18. doi: 10.1016/j.meatsci.2017.05.019
[39]	CAI L, ZHANG W D, CAO A L, et al. Effects of ultrasonics combined with far infrared or microwave thawing on protein denaturation and moisture migration of Sciaenops ocellatus (red drum)[J]. Ultrasonics Sonochemistry,2019,55:96−104. doi: 10.1016/j.ultsonch.2019.03.017
[40]	LI Z Y, WANG J Y, ZHENG B D, et al. Impact of combined ultrasound-microwave treatment on structural and functional properties of golden threadfin bream (Nemipterus virgatus) myofibrillar proteins and hydrolysates[J]. Ultrasonics Sonochemistry,2020,65:105063. doi: 10.1016/j.ultsonch.2020.105063
[41]	KHATKAR A B, KAUR A, KHATKAR S K, et al. Characterization of heat-stable whey protein: Impact of ultrasound on rheological, thermal, structural and morphological properties[J]. Ultrasonics Sonochemistry,2018,49:333−342. doi: 10.1016/j.ultsonch.2018.08.026
[42]	LIU R, LIU Q, XIONG S B, et al. Effects of high intensity unltrasound on structural and physicochemical properties of myosin from silver carp[J]. Ultrasonics Sonochemistry,2017,37:150−157. doi: 10.1016/j.ultsonch.2016.12.039
[43]	ARREDONDO-PARADA I, TORRES-ARREOLA W, SUÁREZ-JIMÉNEZ G M, et al. Effect of ultrasound on physicochemical and foaming properties of a protein concentrate from giant squid (Dosidicus gigas) mantle[J]. LWT,2020,121:108954. doi: 10.1016/j.lwt.2019.108954
[44]	GÜLSEREN İ, GÜZEY D, BRUCE B D, et al. Structural and functional changes in ultrasonicated bovine serum albumin solutions[J]. Ultrasonics Sonochemistry,2007,14(2):173−183. doi: 10.1016/j.ultsonch.2005.07.006
[45]	PAN M M, XU F R, WU Y, et al. Application of ultrasound-assisted physical mixing treatment improves in vitro protein digestibility of rapeseed napin[J]. Ultrasonics Sonochemistry,2020,67:105136. doi: 10.1016/j.ultsonch.2020.105136
[46]	ZHANG Z L, WANG Y, JIANG H, et al. Effect of dual-frequency ultrasound on the formation of lysinoalanine and structural characterization of rice dreg protein isolates[J]. Ultrasonics Sonochemistry,2020,67:105124. doi: 10.1016/j.ultsonch.2020.105124
[47]	ZHANG C, LI X A, WANG H, et al. Ultrasound-assisted immersion freezing reduces the structure and gel property deterioration of myofibrillar protein from chicken breast[J]. Ultrasonics Sonochemistry,2020,67:105137. doi: 10.1016/j.ultsonch.2020.105137
[48]	DABBOUR M, HE R, MINTAH B, et al. Changes in functionalities, conformational characteristics and antioxidative capacities of sunflower protein by controlled enzymolysis and ultrasonication action[J]. Ultrasonics Sonochemistry,2019,58:104625. doi: 10.1016/j.ultsonch.2019.104625
[49]	DE FIGUEIREDO FURTADO G, MANTOVANI R A, CONSOLI L, et al. Structural and emulsifying properties of sodium caseinate and lactoferrin influenced by ultrasound process[J]. Food Hydrocolloids,2017,63:178−188. doi: 10.1016/j.foodhyd.2016.08.038
[50]	ZOU Y, XU P P, WU H H, et al. Effects of different ultrasound power on physicochemical property and functional performance of chicken actomyosin[J]. International Journal of Biological Macromolecules,2018,113:640−647. doi: 10.1016/j.ijbiomac.2018.02.039
[51]	SOBRAL P A, PALAZOLO G G, WAGNER J R. Thermal behavior of soy protein fractions depending on their preparation methods, individual interactions, and storage conditions[J]. Journal of Agricultural and Food Chemistry,2010,58(18):10092−10100. doi: 10.1021/jf101957f
[52]	SUN Q X, CHEN Q, XIA X F, et al. Effects of ultrasound-assisted freezing at different power levels on the structure and thermal stability of common carp (Cyprinus carpio) proteins[J]. Ultrasonics Sonochemistry,2019,54:311−320. doi: 10.1016/j.ultsonch.2019.01.026
[53]	MIR N A, RIAR C S, SINGH S. Physicochemical, molecular and thermal properties of high-intensity ultrasound (HIUS) treated protein isolates from album (Chenopodium album) seed[J]. Food Hydrocolloids,2019,96:433−441. doi: 10.1016/j.foodhyd.2019.05.052
[54]	ARZENI C, MARTÍNEZ K, ZEMA P, et al. Comparative study of high intensity ultrasound effects on food proteins functionality[J]. Journal of Food Engineering,2012,108(3):463−472. doi: 10.1016/j.jfoodeng.2011.08.018
[55]	JIANG S S, DING J Z, ANDRADE J, et al. Modifying the physicochemical properties of pea protein by pH-shifting and ultrasound combined treatments[J]. Ultrasonics Sonochemistry,2017,38:835−842. doi: 10.1016/j.ultsonch.2017.03.046
[56]	O’DONNELL C, TIWARI B, BOURKE P, et al. Effect of ultrasonic processing on food enzymes of industrial importance[J]. Trends in Food Science & Technology,2010,21(7):358−367.
[57]	SUI X N, BI S, QI B K, et al. Impact of ultrasonic treatment on an emulsion system stabilized with soybean protein isolate and lecithin: Its emulsifying property and emulsion stability[J]. Food Hydrocolloids,2017,63:727−734. doi: 10.1016/j.foodhyd.2016.10.024
[58]	ZHANG H, CLAVER I P, ZHU K X, et al. The effect of ultrasound on the functional properties of wheat gluten[J]. Molecules,2011,16(5):4231−4240. doi: 10.3390/molecules16054231
[59]	BA F, URSU A V, LAROCHE C, et al. Haematococcus pluvialis soluble proteins: Extraction, characterization, concentration/fractionation and emulsifying properties[J]. Bioresource Technology,2016,200:147−152. doi: 10.1016/j.biortech.2015.10.012
[60]	JIN J, MA H L, WANG K, et al. Effects of multi-frequency power ultrasound on the enzymolysis and structural characteristics of corn gluten meal[J]. Ultrasonics Sonochemistry,2015,24:55−64. doi: 10.1016/j.ultsonch.2014.12.013

Supplements (0)

Cited By

Cited by

Periodical cited type(5)

1.	巢瑾，周令欣，银飞燕，罗茜，赵萌萌，袁勇，吴浩人，李跑，蒋立文. 基于香气指纹图谱和多元化学计量法对黄金茶2号等级的判别分析. 食品科学. 2023(04): 321-328 .
2.	武珊珊，尤名南，潘朦，王玮，郭巧，丁其欢，周雪芳. 白茶香气成分及影响因素研究进展. 食品安全质量检测学报. 2023(12): 1-14 .
3.	卢丹敏，巢瑾，银飞燕，刘福益，柯中楠，叶汉钟，黄建安，刘仲华. 单丛茶香气物质基础分析. 食品科学. 2022(08): 288-296 .
4.	严学芬，许应芬，李海燕，刘燕. 基于顶空固相微萃取法-气相色谱-质谱法和相对气味活度值分析13种凤凰单丛茶香气成分. 食品安全质量检测学报. 2022(17): 5459-5467 .
5.	李殿威，类彦波，陈明明，宋妍，钱丽丽，左峰. 基于HS-SPME-GC-MS对五常稻花香米挥发性指纹图谱构建. 粮食与油脂. 2022(11): 33-39 .