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Components with strong adsorption capacity for cholates from buckwheat proteins were screened, separated and purified by several methods, and the effects of ultra-high-pressure (UHP) on the structure and function of buckwheat 13S globulin (BW13SG) were studied. Samples were treated by UHP at different pH (3.0 and 7.0) value(s) and at 100–500 MPa for 10–30 min. The results showed that the tertiary structure of BW13SG was partially denatured and aggregated. The decrease in the unordered structure indicated that UHP resulted in a looser secondary structure of BW13SG. UHP treatment also increased solubility, emulsion activity and stability, foaming capacity and stability. The samples treated at 500 MPa, pH 3.0 for 30 min had the most enhanced functionality. Moreover, under this condition, the sodium cholate and sodium deoxycholate adsorption capacities of BW13SG were both higher than 98% and the adsorption capacity of sodium taurocholate, which can be difficult to adsorb, was higher than 60%.


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Effects of ultra-high-pressure treatment on the structural and functional properties of buckwheat 13S globulin

Show Author's information Yiming Zhoua,bBoya OuyangbLina DubYun WeibXiaoli Zhoub( )Ying XiaobYifen Wangc
State Key Laboratory of Dairy Biotechnology, Shanghai Engineering Research Center of Dairy Biotechnology, Dairy Research Institute, Bright Dairy & Food Co. Ltd., Shanghai 200436, China
School of Perfume and Aroma Technology, Shanghai Institute of Technology, Shanghai 201418, China
Department of Biosystems Engineering, Auburn University, Alabama 36879-5417, USA

Abstract

Components with strong adsorption capacity for cholates from buckwheat proteins were screened, separated and purified by several methods, and the effects of ultra-high-pressure (UHP) on the structure and function of buckwheat 13S globulin (BW13SG) were studied. Samples were treated by UHP at different pH (3.0 and 7.0) value(s) and at 100–500 MPa for 10–30 min. The results showed that the tertiary structure of BW13SG was partially denatured and aggregated. The decrease in the unordered structure indicated that UHP resulted in a looser secondary structure of BW13SG. UHP treatment also increased solubility, emulsion activity and stability, foaming capacity and stability. The samples treated at 500 MPa, pH 3.0 for 30 min had the most enhanced functionality. Moreover, under this condition, the sodium cholate and sodium deoxycholate adsorption capacities of BW13SG were both higher than 98% and the adsorption capacity of sodium taurocholate, which can be difficult to adsorb, was higher than 60%.

Keywords: Structure, Ultra-high-pressure, Buckwheat 13S globulin, Functional characteristics

References(45)

[1]

X.L. Zhou, B.B. Yan, Y. Xiao, et al., Tartary buckwheat protein prevented dyslipidemia in high-fat diet-fed mice associated with gut microbiota changes, Food Chem. Toxicol. 119 (2018) 296-301. https://doi.org/10.1016/j.fct.2018.02.052.

[2]

T. Guo, C. Wan, F. Huang, Preparation and bioactivity evaluation of low salt peptide from sunflower seed meal, Oil Crop Sci. 4 (2019) 118-126. https://doi.org/10.3969/j.issn.2019.02.006.

[3]

X. Wang, N. Ullah, X. Sun, et al., Development and characterization of bacterial cellulose reinforced biocomposite films based on protein from buckwheat distiller's dried grains, Int. J. Biol. Macromol. 96 (2017) 353-360. https://doi.org/10.1016/j.ijbiomac.2016.11.106.

[4]

L. Siracusa, F. Gresta, E. Sperlinga, et al., Effect of sowing time and soil water content on grain yield and phenolic profile of four buckwheat (Fagopyrum esculentum Moench.) varieties in a Mediterranean environment, J. Food Compost. Anal. 62 (2017) 1-7. https://doi.org/10.1016/j.jfca.2017.04.005.

[5]

Z. Ma, M. Liu, W. Sun, et al., Genome-wide identification and expression analysis of the trihelix transcription factor family in tartary buckwheat (Fagopyrum tataricum), BMC Biol. 19 (2019) 340-344. https://doi.org/10.1186/s12870-019-1957-x.

[6]

M.G. Nosworthy, A. Franczyk, A. Zimoch-Korzycka, et al., Impact of processing on the protein quality of pinto bean (Phaseolus vulgaris) and buckwheat (Fagopyrum esculentum Moench) flours and blends, as determined by in vitro and in vivo methodologies, J. Agric. Food Chem. 65 (2017) 3919-3925. https://doi.org/10.1021/acs.jafc.7b00697.

[7]

J.R. Taylor, P.S. Belton, T. Beta, et al., Increasing the utilisation of sorghum, millets and pseudocereals: developments in the science of their phenolic phytochemicals, biofortification and protein functionality, J. Cereal Sci. 59 (2014) 257-275. https://doi.org/10.1016/j.jcs.2013.10.009.

[8]

J.W. Wang, T.J. Ma, F. Shan, et al., Technical optimization and dynamic model for ultrahigh pressure extraction of buckwheat flavone, J. Chinese Cereals Oils Assoc. 12 (2011) 93-99. https://doi.org/10.4271/2011-01-3150.

[9]

Y. Gao, J. Li, C. Chang, et al., Effect of enzymatic hydrolysis on heat stability and emulsifying properties of egg yolk, Food Hydrocoll. 97 (2019) 105224. https://doi.org/10.1016/j.foodhyd.2019.105224.

[10]

C. Wang, J. Wang, D. Zhu, et al., Effect of dynamic ultra-high-pressure homogenization on the structure and functional properties of whey protein, J. Food Sci. Technol. 57 (2020) 1301-1309. https://doi.org/10.1007/s13197-019-04164-z.

[11]

L. Nováková, A. Vaast, C. Stassen, et al., High-resolution peptide separations using nano-LC at ultra-high pressure, Sep Sci. Technol. 36 (2013) 1192-1199. https://doi.org/10.1002/jssc.201201087.

[12]

L. Qiang, Z. Hu, Z. Li, et al., Buckwheat husk-derived hierarchical porous nitrogen-doped carbon materials for high-performance symmetric supercapacitor, J. Porous Mater. 26 (2019) 1217-1225. https://doi.org/10.1007/s10934-019-00723-z.

[13]

N. Toro-Funes, J. Bosch-Fusté, M. Veciana-Nogués, et al., Changes of isoflavones and protein quality in soymilk pasteurised by ultra-high-pressure homogenisation throughout storage, Food Chem. 162 (2014) 47-53. https://doi.org/10.1016/j.foodchem.2014.04.019.

[14]

C. Blayo, O. Vidcoq, F. Lazennec, et al., Effects of high pressure processing (hydrostatic high pressure and ultra-high pressure homogenisation) on whey protein native state and susceptibility to tryptic hydrolysis at atmospheric pressure, Food Res. Int. 79 (2016) 40-53. https://doi.org/10.1016/j.foodres.2015.11.024.

[15]

C. Fernandez-Avila, A. Trujillo, Ultra-high pressure homogenization improves oxidative stability and interfacial properties of soy protein isolate-stabilized emulsions, Food Chem. 209 (2016) 104-113. https://doi.org/10.1016/j.foodchem.2016.04.019.

[16]

C.H. Tang, Functional properties and in vitro digestibility of buckwheat protein products: influence of processing, J. Food Eng. 82 (2007) 568-576. https://doi.org/10.1016/j.lwt.2008.07.012.

[17]

J. Naime Filho, F. Silvério, M. Dos Reis, et al., Adsorption of cholate anions on layered double hydroxides: effects of temperature, ionic strength and pH, J. Mater. Sci. 43 (2008) 6986-6991. https://doi.org/10.1007/s10853-008-2952-z.

[18]

D. Sari, A. Safitri, J. Cairns, et al., Protein profiling of coloring rice (Oryza sativa L.) using SDS-PAGE and experionTM260 analysis, J. Phys. Conf. Ser. 12 (2019) 1146-1153. https://doi.org/10.1088/1742-6596/1146/1/012038.

[19]

H. Chen, J. Shen, K. Chen, et al., Atomic layer deposition of Pt nanoparticles on low surface area zirconium oxide for the efficient base-free oxidation of 5-hydroxymethylfurfural to 2,5-furandicarboxylic acid, Appl. Catal. A: Gen. 555 (2018) 98-107. https://doi.org/10.1016/j.apcata.2018.01.023.

[20]

S. Xue, H. Yang, R. Liu, et al., Applications of high pressure to pre-rigor rabbit muscles affect the functional properties associated with heat-induced gelation, Meat Sci. 129 (2017) 176-184. https://doi.org/10.1016/j.meatsci.2017.03.006.

[21]

C.A. Manassero, S.R. Vaudagna, M.C. Añón, et al., High hydrostatic pressure improves protein solubility and dispersion stability of mineral-added soybean protein isolate, Food Hydrocoll. 43 (2015) 629-635. https://doi.org/10.1016/j.foodhyd.2014.07.020.

[22]

G. Lan, H. Chen, S. Chen, et al., Chemical composition and physicochemical properties of dietary fiber from Polygonatum odoratum as affected by different processing methods, Food Res. Int. 49 (2012) 406-410. https://doi.org/10.1016/j.foodres.2012.07.047.

[23]

Z. Qin, X. Guo, Y. Lin, et al., Effects of high hydrostatic pressure on physicochemical and functional properties of walnut (Juglans regia L.) protein isolate, J. Sci. Food Agric. 93 (2013) 1105-1111. https://doi.org/10.1002/jsfa.5857.

[24]

Z. Hou, M. Zhang, B. Liu, et al., Effect of chitosan molecular weight on the stability and rheological properties of β-carotene emulsions stabilized by soybean soluble polysaccharides, Food Hydrocoll. 26 (2012) 205-211. https://doi.org/10.1016/j.foodhyd.2011.05.013.

[25]

A. Mohammad, R. Mobin, Ionic liquid as separation enhancer in thin-layer chromatography of biosurfactants: mutual separation of sodium cholate, sodium deoxycholate and sodium taurocholate, J. Anal Sci. Technol. 6 (2015) 16-20. https://doi.org/10.1186/s40543-015-0058-1.

[26]

O. Soladoye, P. Shand, M. Dugan, et al., Influence of cooking methods and storage time on lipid and protein oxidation and heterocyclic aromatic amines production in bacon, Food Res. Int. 99 (2017) 660-669. https://doi.org/10.1016/j.foodres.2017.06.029.

[27]

A. Sreedhara, R. Flengsrud, V. Prakash, et al., A comparison of effects of pH on the thermal stability and conformation of caprine and bovine lactoferrin, Int. Dairy J. 20 (2010) 487-494. https://doi.org/10.1016/j.idairyj.2010.02.003.

[28]

I. Franco, M.D. Pérez, E. Castillo, et al., Effect of high pressure on the structure and antibacterial activity of bovine lactoferrin treated in different media, J. Dairy Sci. 80 (2013) 283-290. https://doi.org/10.1017/s0022029913000150.

[29]

C.H. Tang, C.Y. Ma, Effect of high pressure treatment on aggregation and structural properties of soy protein isolate, LWT-Food Sci. Technol. 42 (2009) 606-611. https://doi.org/10.1016/j.lwt.2008.07.012.

[30]

H. Hu, J. Wu, E.C. Li-Chan, et al., Effects of ultrasound on structural and physical properties of soy protein isolate (SPI) dispersions, Food Hydrocoll. 30 (2013) 647-655. https://doi.org/10.1016/j.foodhyd.2012.08.001.

[31]

S. Xue, X. Xu, H. Shan, et al., Effects of high-intensity ultrasound, high-pressure processing, and high-pressure homogenization on the physicochemical and functional properties of myofibrillar proteins, Innov. Food Sci. Emerg. Technol. 45 (2018) 354-360. https://doi.org/10.1016/j.ifset.2017.12.007.

[32]

C. Puppo, N. Chapleau, F. Speroni, et al., Physicochemical modifications of high-pressure-treated soybean protein isolates, J. Agric. Food Chem. 52 (2004) 1564-1571. https://doi.org/10.1021/jf034813t.

[33]

J. Xu, D. Mukherjee, S.K. Chang, Physicochemical properties and storage stability of soybean protein nanoemulsions prepared by ultra-high pressure homogenization, Food Chem. 240 (2018) 1005-1013. https://doi.org/10.1016/j.foodchem.2017.07.077.

[34]

G.S. Li, Y.T. Chen, S.F. Xuan, et al., Effects of ultra-high pressure on the biochemical properties and secondary structure of myofibrillar protein from Oratosquilla oratoria muscle, J. Food Process. Eng. 42 (2019) 13231. https://doi.org/10.1111/jfpe.13231.

[35]

R. Chagas, C.A. Laia, R.B. Ferreira, et al., Sulfur dioxide induced aggregation of wine thaumatin-like proteins: role of disulfide bonds, Food Chem. 259 (2018) 166-174. https://doi.org/10.1016/j.foodchem.2018.03.115.

[36]

Z. Duan, W. Duan, F. Li, et al., Effect of carboxymethylation on properties of fucoidan from Laminaria japonica: antioxidant activity and preservative effect on strawberry during cold storage, Postharvest Biol. Technol. 151 (2019) 127-133. https://doi.org/10.1186/s13065-018-0402-9.

[37]

N. Acelas, E. Flórez, Chloride adsorption on Fe-and Al-(hydr) oxide: estimation of Gibbs free energies, Adsorp. 24 (2018) 243-248. https://doi.org/10.1007/s10450-018-9939-0.

[38]

H. Zhou, L. Ding, Z. Wu, et al., Hydrogen sulfide reduces RAGE toxicity through inhibition of its dimer formation, Free Radic. Biol. Med. 104 (2017) 262-271. https://doi.org/10.1016/j.freeradbiomed.2017.01.026.

[39]

C. Arzeni, K. Martínez, P. Zema, et al., Comparative study of high intensity ultrasound effects on food proteins functionality, J. Food Eng. 108 (2012) 463-472. https://doi.org/10.1016/S0026-0495(00)80082-7.

[40]

L. Jiang, J. Wang, Y. Li, et al., Effects of ultrasound on the structure and physical properties of black bean protein isolates, Food Res. Int. 62 (2014) 595-601. https://doi.org/10.1016/j.foodres.2014.04.022.

[41]

H. Bouaouina, A. Desrumaux, C. Loisel, et al., Functional properties of whey proteins as affected by dynamic high-pressure treatment, Int. Dairy J. 16 (2006) 275-284. https://doi.org/10.1016/j.idairyj.2005.05.004.

[42]

E. Molina, A. Papadopoulou, D. Ledward, Emulsifying properties of high pressure treated soy protein isolate and 7S and 11S globulins, Food Hydrocoll. 15 (2001) 263-269. https://doi.org/10.1016/S0268-005X(01)00023-6.

[43]

J. Zhang, Z.W. Wang, Soluble dietary fiber from Canna edulis Ker by-product and its enzymatic and antioxidant activities, Food Biotechnol. 25 (2011) 336-350. https://doi.org/10.1080/08905436.2011.617256.

[44]

L. Mirmoghtadaie, S.S. Aliabadi, S.M. Hosseini, Recent approaches in physical modification of protein functionality, Food Chem. 199 (2016) 619-627. https://doi.org/10.1016/j.foodchem.2015.12.067.

[45]

B. Yuan, J. Ren, M. Zhao, et al., Effects of limited enzymatic hydrolysis with pepsin and high-pressure homogenization on the functional properties of soybean protein isolate, LWT-Food Sci. Technol. 46 (2012) 453-459. https://doi.org/10.1016/j.lwt.2011.12.001.

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Publication history

Received: 07 August 2020
Revised: 14 September 2020
Accepted: 16 November 2020
Published: 28 April 2022
Issue date: July 2022

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© 2022 Beijing Academy of Food Sciences. Publishing services by Elsevier B.V. on behalf of KeAi Communications Co., Ltd.

Acknowledgements

Acknowledgements

The authors grateful acknowledge the financial support by the Open Project Program of State Key Laboratory of Dairy Biotechnology (No. SKLDB2018-002), National Natural Science Foundation of China (No. 31871805 & No. 31501437), Shanghai Municipal Education Commission (Plateau Discipline Construction Program) and China Agriculture Research System (CARS-08-D2).

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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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