The Effect of Non-covalent Interaction of Soy Protein Isolate with Quercetin and Rutin on Functional Properties and <i>in Vitro</i> Digestion Characteristics

ZHAO Juyang; YUAN Huiping; SUN Xinmeng; JIN Cong

doi:10.13386/j.issn1002-0306.2021100103

Volume 43 Issue 15

Jul. 2022

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Science and Technology of Food Industry > 2022 > 43(15): 73-80. > DOI: 10.13386/j.issn1002-0306.2021100103

ZHAO Juyang, YUAN Huiping, SUN Xinmeng, et al. The Effect of Non-covalent Interaction of Soy Protein Isolate with Quercetin and Rutin on Functional Properties and in Vitro Digestion Characteristics[J]. Science and Technology of Food Industry, 2022, 43(15): 73−80. (in Chinese with English abstract). doi: 10.13386/j.issn1002-0306.2021100103.

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The Effect of Non-covalent Interaction of Soy Protein Isolate with Quercetin and Rutin on Functional Properties and in Vitro Digestion Characteristics

College of Tourism and Cuisine, Harbin University of Commerce, Harbin 150030, China

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Received Date: October 12, 2021
Available Online: June 01, 2022

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Abstract

Abstract

The changes in functionality (solubility, emulsification, gelation) and digestibility of quercetin-soy protein isolate and rutin-soy protein isolate complexes were analyzed in this paper. The interaction was studied by UV-Vis spectroscopy and fluorescence spectroscopy. The mechanism, the type of fluorescence quenching, the number of binding sites and thermodynamic parameters were analyzed. The results showed that quercetin and rutin could improve the functional properties of SPI. When the addition of quercetin and rutin were 8%, the hardness of SPI gel could be increased by 23.23% and 187.18%, respectively. The EAI, ESI and solubility of SPI increased first and then tended to level off. When the addition amount was 6% and 4%, the emulsifying activity and solubility reached the highest respectively, which were increased by 20.84% and 10.06% compared with SPI. With the increase of rutin addition, the EAI, ESI and solubility of SPI first increased and then decreased slightly. When the addition amount was 4% and 6%, the emulsifying activity and solubility reached the highest respectively, which was 26.17% and 19.27% than that of SPI. In addition, the interaction of quercetin and rutin with SPI could also improve the bioavailability of the protein. Further research on the interaction mechanism between the two flavonoid polyphenols and SPI showed that the fluorescence spectra of the two interacting complexes were blue-shifted, quercetin, rutin and SPI spontaneously combine, and mainly acted through hydrogen bonding and van der Waals forces. The interaction mechanism of quercetin, rutin and SPI was dynamic quenching and static quenching, respectively.
- quercetin,
- rutin,
- solubility,
- emulsification,
- gelation,
- digestibility,
- non-covalent interaction

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References

[1]	FRAGA C G, CROFT K D, KENNEDY D O, et al. The effects of polyphenols and other bioactives on human health[J]. Food Function,2019,10(2):514−528. doi: 10.1039/C8FO01997E
[2]	XIE Y, CHEN J, XIAO A P, et al. Antibacterial activity of polyphenols: Structure-activity relationship and influence of hyperglycemic condition[J]. Molecules,2017,22(11):1913. doi: 10.3390/molecules22111913
[3]	LEPHART E D. Skin aging and oxidative stress: Equol's anti-aging effects via biochemical and molecular mechanism[J]. Ageing Reserch Reviews,2016,31:36−54. doi: 10.1016/j.arr.2016.08.001
[4]	KHAN N, MUKHTAR H. Tea polyphenols in promotion of human health[J]. Nutrients,2018,11(1):39. doi: 10.3390/nu11010039
[5]	BOURVELLEC C L, RENARD G C. Interactions between polyphenols and macromolecules: quantification methods and mechanisms[J]. Critical Reviews in Food Science and Nutrition,2012,52(3):213−248. doi: 10.1080/10408398.2010.499808
[6]	HARSHADRAI M R, DÖRTE C, SASCHA R, et al. Interactions of different phenolic acids and flavonoids with soy proteins[J]. International Journal of Biological Macromolecules,2002,30(3):137−150.
[7]	JIA Z, ZHENG M, TAO F, et al. Effect of covalent modification by (-)-epigallocatechin-3-gallate on physicochemical and functional properties of whey protein isolate[J]. LWT-Food Science and Technology,2016,66:305−310. doi: 10.1016/j.lwt.2015.10.054
[8]	裘乐芸, 邢倩, 邓泽元, 等. 植物多酚与鲢鱼肌球蛋白相互作用及其对肌原纤维蛋白结构和凝胶形成的影响[J]. 中国食品学报,2021,21(5):48−56. [QIU L Y, XING Q, DENG Z Y, et al. Interaction of plant polyphenols with silver carp myosin and its effect on myofibril protein structure and gel formation[J]. Chinese Journal of Food Science,2021,21(5):48−56. QIU L Y, XING Q, DENG Z Y, et al. Interaction of plant polyphenols with silver carp myosin and its effect on myofibril protein structure and gel formation[J]. Chinese Journal of Food Science, 2021, 21(5): 48-56.
[9]	PETZKE K J, SCHUPPE S, ROHN S, et al. Chlorogenic acid moderately decreases the quality of whey proteins in rats[J]. Journal of Agricultural and Food Chemistry,2005,53(9):3714−3720. doi: 10.1021/jf048186z
[10]	刘勤勤. 豆奶茶的制备、特性及机理研究[D]. 无锡: 江南大学, 2015. LIU Q Q. Study on preparation, characteristics and mechanism of soybean milk tea[D]. Wuxi: Jiangnan University, 2015
[11]	SPERONI F, ANON R C, LAMBALLERIE R D. Effects of calcium and high pressure on soybean proteins: A calorimetric study[J]. Food Research International,2010,43(5):1347−1355. doi: 10.1016/j.foodres.2010.03.022
[12]	ZHOU S D, LIN Y F, XU X, et al. Effect of non-covalent and covalent complexation of (-)-epigallocatechin gallate with soybean protein isolate on protein structure and in vitro digestion characteristics[J]. Food Chemistry,2020,309:1−10.
[13]	NAISARG P, SIDDHARTH J, KUAN Y W, et al. Enhanced colloidal stability, solubility and rapid dissolution of resveratrol by nanocomplexation with soy protein isolate[J]. Journal of Colloid and Interface Science,2017,488:1−16. doi: 10.1016/j.jcis.2016.10.085
[14]	PAN Y, XIE Q T, ZHU J, et al. Study on the fabrication andin vitro digestion behavior of curcumin-loaded emulsions stabilized by succinylated whey protein hydrolysates[J]. Food Chemistry,2019,287:76−84. doi: 10.1016/j.foodchem.2019.02.047
[15]	ZOU Y, GUO J, YIN S W, et al. Pickering emulsion gels prepared by hydrogen-bonded Zein/Tannic acid complex colloidal particles[J]. Journal of Agricultural and Food Chemistry,2015,63(33):1−10.
[16]	BRODKORB A, EGGER L, ALMINGER M, et al. INFOGEST static in vitro simulation of gastrointestinal food digestion[J]. Nature Protocols,2019,14(4):991−1014. doi: 10.1038/s41596-018-0119-1
[17]	MAO Y, MCCLEMENTS D J. Influence of electrostatic heteroaggregation of lipid droplets on their stability and digestibility under simulated gastrointestinal conditions[J]. Food and Function,2012,3(10):1025−1034. doi: 10.1039/c2fo30108c
[18]	CHEN Z Q, WANG C, GAO X, et al. Interaction characterization of preheated soy protein isolate with cyanidin-3-O-glucoside and their effects on the stability of black soybean seed coat anthocyanins extracts[J]. Food Chemistry,2019,271:266−273. doi: 10.1016/j.foodchem.2018.07.170
[19]	张传英, 彭鑫, 饶恒军, 等. 丹酚酸B与牛血清白蛋白相互作用的光谱学研究[J]. 光谱学与光谱分析,2021,41(6):1701−1707. [ZHANG C Y, PENG X, RAO H J, et al. Spectroscopic study on the interaction between salvianolic acid B and bovine serum albumin[J]. Spectroscopy and Spectral Analysis,2021,41(6):1701−1707. ZHANG C Y, PENG X, RAO H J, et al. Spectroscopic study on the interaction between salvianolic acid B and bovine serum albumin[J]. Spectroscopy and spectral analysis, 2021, 41 (6): 1701-1707.
[20]	WEI Z H, YANG W, FAN R, et al. Evaluation of structural and functional properties of protein-EGCG complexes and their ability of stabilizing a model β-carotene emulsion[J]. Food Hydrocolloids,2015,45:337−350. doi: 10.1016/j.foodhyd.2014.12.008
[21]	贾娜, 孙嘉, 刘丹, 等. 槲皮素对氧化条件下猪肉肌原纤维蛋白结构及凝胶特性的影响[J]. 食品科学,2021,42(10):45−51. [JIA N, SUN J, LIU D, et al. The effect of quercetin on the structure and gel properties of pork myofibril protein under oxidative conditions[J]. Food Science,2021,42(10):45−51. doi: 10.7506/spkx1002-6630-20191103-021 JIA N, SUN J, LIU D, et al. The effect of quercetin on the structure and gel properties of pork myofibril protein under oxidative conditions[J]. Food Science, 2021, 42(10): 45-51 . doi: 10.7506/spkx1002-6630-20191103-021
[22]	胡思. 茶多酚与面筋蛋白相互作用对生鲜面品质影响的研究[D]. 郑州: 河南工业大学, 2016. HU S. Study on the effect of interaction between tea polyphenols and gluten protein on the quality of fresh noodles[D]. Zhengzhou: Henan University of Technology, 2016.
[23]	THUMMANOON P, SOOTTAWAT B, SUTTIRUG P. Effect of phenolic compounds on protein cross-linking and properties of film from fish myofibrillar protein[J]. International Journal of Biological Macromolecules,2012,51(5):774−782. doi: 10.1016/j.ijbiomac.2012.07.010
[24]	许杨杨. 大豆皂苷-蛋白W/O/W型双重乳液的构建及其稳定性研究[D]. 渤海: 渤海大学, 2021. XU Y Y. Construction and stability study of soybean saponin-protein W/O/W double emulsion[D]. Bohai: Bohai University, 2021.
[25]	孙迪. 不同脂肪对肌原纤维蛋白乳化液稳定性及肉糜凝胶特性的影响[D]. 渤海: 渤海大学, 2019. SUN D. The effect of different fats on the stability of myofibrillar protein emulsion and the properties of meat emulsion[D]. Bohai: Bohai University, 2019.
[26]	LI T, WANG L, CHEN Z X, et al. Functional properties and structural changes of rice proteins with anthocyanins complexation[J]. Food Chemistry,2020,331:1−11.
[27]	刘泽宇, 刘焱, 罗灿, 等. 茶多酚对草鱼鱼肉蛋白质流变学特性的影响[J]. 现代食品科技,2015,31(6):50−58. [LIU Z Y, LIU Y, LUO C, et al. Effect of tea polyphenols on protein rheological properties of grass carp[J]. Modern Food Science and Technology,2015,31(6):50−58. LIU Z Y, LIU Y, LUO C, et al. Effect of tea polyphenols on protein rheological properties of grass carp[J]. Modern Food Science and Technology, 2015, 31(6): 50-58.
[28]	YAN M Y, LI B F, ZHAO X, et al. Physicochemical properties of gelatin gels from walleye pollock (Theragra chalcogramma) skin cross-linked by gallic acid and rutin[J]. Food Hydrocolloids,2011,25(5):907−914. doi: 10.1016/j.foodhyd.2010.08.019
[29]	MARIJA S, JELENA R, JANA O, et al. Binding affinity between dietary polyphenols and β-lactoglobulin negatively correlates with the protein susceptibility to digestion and total antioxidant activity of complexes formed[J]. Food Chemistry,2013,136(3-4):1263−1271. doi: 10.1016/j.foodchem.2012.09.040
[30]	NAZ S , SIDDIQI R , DEW T P , et al. Epigallocatechin-3-gallate inhibits lactase but is alleviated by salivary proline-rich proteins[J]. Journal of Agricultural & Food Chemistry,2011,59(6):2734−2738.
[31]	王菡, 李高华, 陈涛, 等. 基于广谱性单克隆抗体免疫分析有机磷农药残留[J]. 食品安全质量检测学报,2015,6(11):4399−4408. [WANG H, LI G H, CHEN T, et al. Immunoassay of organophosphorus pesticide residues based on broad-spectrum monoclonal antibody[J]. Journal of Food Safety and Quality Inspection,2015,6(11):4399−4408. WANG H, LI G H, CHEN T, et al. Immunoassay of organophosphorus pesticide residues based on broad-spectrum monoclonal antibody[J]. Journal of food safety and quality inspection, 2015, 6 (11): 4399-4408.
[32]	王启明, 唐瑜婉, 李春翼, 等. NaCl浓度对麦醇溶蛋白与槲皮素相互作用的影响[J]. 食品科学,2021,42(8):29−39. [WANG Q M, TANG Y W, LI C Y, et al. Effect of NaCl concentration on the interaction between gliadin and quercetin[J]. Food Science,2021,42(8):29−39. doi: 10.7506/spkx1002-6630-20200724-329 WANG Q M, TANG Y W, LI C Y, et al. Effect of NaCl concentration on the interaction between gliadin and quercetin [J]. Food Science, 2021, 42 (8): 29-39. doi: 10.7506/spkx1002-6630-20200724-329
[33]	ZHANG Y Z, XIANG X, PING M, et al. Spectroscopic studies on the interaction of Congo red with bovine serum albumin[J]. Spectrochim Acta A,2009,72:907−914. doi: 10.1016/j.saa.2008.12.007
[34]	苗向硕, 吴伟, 吴晓娟. 表没食子儿茶素没食子酸酯和米糠蛋白的相互作用[J]. 中国粮油学报,2019,34(12):19−26. [MIAO X S, WU W, WU X J. Interaction between epigallocatechin gallate and rice bran protein[J]. Chinese Journal of Grain and Oil,2019,34(12):19−26. doi: 10.3969/j.issn.1003-0174.2019.12.005 MIAO X S, WU W, WU X J. Interaction between epigallocatechin gallate and rice bran protein[J]. Chinese Journal of Grain and Oil, 2019, 34 (12): 19-26. doi: 10.3969/j.issn.1003-0174.2019.12.005
[35]	张超, 傅玉颖, 沈亚丽, 等. 不同带电特性的壳聚糖/酪蛋白相互作用研究[J]. 中国食品学报,2021,21(2):63−71. [ZHANG C, FU Y Y, SHEN Y L, et al. Study on chitosan/casein interaction with different charging characteristics[J]. Chinese Journal of Food,2021,21(2):63−71. ZHANG C, FU Y Y, SHEN Y L, et al. Study on chitosan/casein interaction with different charging characteristics [J]. Chinese Journal of Food, 2021, 21(2): 63-71.
[36]	CHEN W J, WANG W J, MA X B, et al. Effect of pH-shifting treatment on structural and functional properties of whey protein isolate and its interaction with (-)-epigallocatechin-3-gallate[J]. Food Chemistry,2019,274:234−241. doi: 10.1016/j.foodchem.2018.08.106
[37]	李楠, 王国振, 曾永明, 等. 薰衣草花色苷与牛血清蛋白非共价相互作用研究[J]. 化学研究与应用,2021,33(6):1004−1011. [LI N, WANG G Z, ZENG Y M, et al. Study on non covalent interaction between Lavender anthocyanins and bovine serum protein[J]. Chemical Research and Application,2021,33(6):1004−1011. doi: 10.3969/j.issn.1004-1656.2021.06.003 LI N, WANG G Z, ZENG Y M, et al. Study on non covalent interaction between Lavender anthocyanins and bovine serum protein[J]. Chemical Research and Application, 2021, 33 (6): 1004-1011. doi: 10.3969/j.issn.1004-1656.2021.06.003