Structural modification and solubility enhancement of Glutenin by pH-migration

Abstract

Abstract: The unique amino acid composition of Glu leads to its poor solubility, which greatly limits its application in the food industry. The pH shift treatment can induce structural changes of protein and significantly improve the solubility. Therefore, Glu was modified by pH shifting to improve its properties in this paper. The effects of pH migration treatment on the properties of glutenin were investigated by dynamic light scattering, TEM, fluorescence, FT-IR dichroism. The results showed that pH migration could significantly reduce the particle size of Glu aggregates and increase the surface charge of Glu granules. Increase the hydrophobicity and sulfhydryl group content, decrease the disulfide bond content, the effect of alkali migration was more significant than that of acid migration. In addition, base migration treatment significantly improved the solubility of Glu and play an active role in broadening the application range of Glu in food industry.

Key words: Glutenin, pH migration treatment, surface hydrophobicity, solubility, protein structure

CLC Number:

TS254.9

Bin ZHOU. Structural modification and solubility enhancement of Glutenin by pH-migration[J]. FOOD SCIENCE, 0, (): 0-0.

References

[1] TANG Y, YANG Y, WANG Q, et al.Combined effect of carboxymethylcellulose and salt on structural properties of wheat gluten proteins[J].Food Hydrocolloids, 2019, 97(/):105189-105189
[2]ORTOLAN F, STEEL C J.Protein Characteristics that Affect the Quality of Vital Wheat Gluten to be Used in Baking: A Review[J].Comprehensive Reviews in Food Science Food Safety, 2017, 16(3):369-381
[3]D' OVIDIO R, MASCI S.The low-molecular-weight glutenin subunits of wheat gluten[J].Journal of Cereal Science, 2004, 39(3):321-339
[4]POURMOHAMMADI K, ABEDI E.Hydrolytic enzymes and their directly and indirectly effects on gluten and dough properties: An extensive review[J].Food Science Nutrition, 2021, 9(7):3988-4006
[5]WIESER H.Chemistry of gluten proteins[J].Food Microbiology, 2007, 24(2):115-119
[6] KAMANI M H, SEMWAL J, MOUSAVI KHANEGHAH A.Functional modification of grain proteins by dual approaches: Current progress, challenges, and future perspectives[J].Colloids Surfaces B:Biointerfaces, 2022, 211(/):112306-112306
[7] ZHANG L, HU Y, WANG X, et al.Improving soaking efficiency of soybeans through sweeping frequency ultrasound assisted by parameters optimization[J].Ultrasonics Sonochemistry, 2021, 79(/):105794-105794
[8]BUHLER J M, DEKKERS B L, BRUINS M E, et al.Modifying Faba Bean Protein Concentrate Using Dry Heat to Increase Water Holding Capacity[J].Foods, 2020, 9(8):1077-1092
[9] LIU B, WANG H, HU T, et al.Ball-milling changed the physicochemical properties of SPI and its cold-set gels[J].Journal of Food Engineering, 2017, 195(/):158-165
[10]MAJZOOBI M, ABEDI E, FARAHNAKY A, et al.Functional properties of acetylated glutenin and gliadin at varying pH values[J].Food Chemistry, 2012, 133(4):1402-1407
[11] CHEN W, MA X, WANG W, et al.Preparation of modified whey protein isolate with gum acacia by ultrasound maillard reaction[J].Food Hydrocolloids, 2019, 95(/):298-307
[12]LIU X, WANG C, ZHANG X, et al.Application Prospect of Protein-Glutaminase in the Development of Plant-Based Protein Foods[J].Foods, 2022, 11(3):440-440
[13]SUN Q, MA Z F, ZHANG H, et al.Structural characteristics and functional properties of walnut glutelin as hydrolyzed: effect of enzymatic modification[J].International Journal of Food Properties, 2019, 22(1):265-279
[14] FAN J-L, HAN N, CHEN H-Q.Physicochemical and structural properties of wheat gluten/rice starch dough-like model[J].Journal of Cereal Science, 2021, 98(/):103181-103181
[15] PENG W, KONG X, CHEN Y, et al.Effects of heat treatment on the emulsifying properties of pea proteins[J].Food Hydrocolloids, 2016, 52(/):301-310
[16]VERAVERBEKE W S, DELCOUR J A.Wheat protein composition and properties of wheat glutenin in relation to breadmaking functionality[J].Critical Reviews in Food Science and Nutrition, 2002, 42(3):179-208
[17]JAMBRAK A R, MASON T J, LELAS V, et al.Effect of ultrasound treatment on solubility and foaming properties of whey protein suspensions[J].Journal of Food Engineering, 2008, 86(2):281-287
[18]JIANG J, XIONG Y L, CHEN J.pH Shifting Alters Solubility Characteristics and Thermal Stability of Soy Protein Isolate and Its Globulin Fractions in Different pH,Salt Concentration,and Temperature Conditions[J].Journal of Agricultural and Food Chemistry, 2010, 58(13):8035-8042
[19]Grosch W, Wieser H.Redox Reactions in Wheat Dough as Affected by Ascorbic Acid[J].Journal of Cereal Science, 1999, 29(1):1-16
[20]周向军，董瑞红，高义霞.偏移结合温和热处理对蚕豆分离蛋白结构和功能的影响[J].食品与发酵工业, 2019, 45(1):100-108
[21] XIONG W, WANG Y, ZHANG C, et al.High intensity ultrasound modified ovalbumin: Structure, interface and gelation properties[J].Ultrasonics Sonochemistry, 2016, 31(/):302-309
[22] SHOKRI S, JAVANMARDI F, MOHAMMADI M, et al.Effects of ultrasound on the techno-functional properties of milk proteins: A systematic review[J].Ultrasonics Sonochemistry, 2022, 83(/):105938-105938
[23] JIANG S, DING J, 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
[24]Hettiarachchy N S, Kalapathy U, Myers D J.Alkali-Modified Soy Protein with Improved Adhesive and Hydrophobic Properties[J].Journal of the American Oll Chemlsts' Society, 1995, 72(12):1461-1464
[25] YANG J, DUAN Y, GENG F, et al.Ultrasonic-assisted pH shift-induced interfacial remodeling for enhancing the emulsifying and foaming properties of perilla protein isolate[J].Ultrasonics Sonochemistry, 2022, 89(/):106108-106108
[26] ALAVI F, CHEN L, WANG Z, et al.Consequences of heating under alkaline pH alone or in the presence of maltodextrin on solubility, emulsifying and foaming properties of faba bean protein[J].Food Hydrocolloids, 2021, 112(/):106335-106335
[27] LEE H, YILDIZ G, DOS SANTOS L C, et al.Soy protein nano-aggregates with improved functional properties prepared by sequential pH treatment and ultrasonication[J].Food Hydrocolloids, 2016, 55(/):200-209
[28] Mirian M, Sakuno, Shinya M, et al.Adsorption and Structural Change of -Lactoglobulin at the Diacylglycerol-Water Interface[J].Langmuir, 2008, 24(/):11483-11488
[29] HE S, ZHAO J, CAO X, et al.Low pH-shifting treatment would improve functional properties of black turtle bean (Phaseolus vulgaris L.) protein isolate with immunoreactivity reduction[J].Food Chemistry, 2020, 330(/):127217-127217
[30]ZHENG L, ZHAO Y, XIAO C, et al.Mechanism of the discrepancy in the enzymatic hydrolysis efficiency between defatted peanut flour and peanut protein isolate by Flavorzyme[J].Food Chemistry, 2015, 168(1):100-106
[31] TIAN Y, ZHANG Z, ZHANG P, et al.The role of conformational state of pH-shifted β-conglycinin on the oil/water interfacial properties and emulsifying capacities[J].Food Hydrocolloids, 2020, 108(/):105990-105990
[32]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
[33] ROUSSEL J C.Mechanisms of gelation of sardine proteins: influence of thermal processing and of various additives on the texture and protein solubility of kamaboko gels[J].International Journal of Food Science and Technology, 1990, 25(/):260-280
[34]JIANG J, XIONG Y L, CHEN J.Role of β-conglycinin and glycinin subunits in the pH-shifting-induced structural and physicochemical changes of soy protein isolate[J].Journal of Food Science, 2011, 76(2):C293-C302
[35] ZHANG J, LIU Q, CHEN Q, et al.Synergistic modification of pea protein structure using high-intensity ultrasound and pH-shifting technology to improve solubility and emulsification[J].Ultrasonics Sonochemistry, 2022, 88(/):106099-106099
[36] YILDIZ G, ANDRADE J, ENGESETH N E, et al.Functionalizing soy protein nano-aggregates with pH-shifting and mano-thermo-sonication[J].Journal of Colloid and Interface Science, 2017, 505(/):836-846