Effect of cosolvents (polyols) on structural and foaming properties of soy protein isolate  

https://doi.org/10.17221/35/2016-CJFSCitation:Pan M., Meng X., Jiang L., Yu D., Liu T. (2017): Effect of cosolvents (polyols) on structural and foaming properties of soy protein isolate  . Czech J. Food Sci., 35: 57-66.
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Effect of polyols (mannitol, sorbitol, and xylitol) at three concentrations (5, 10, and 15% w/w) on the structure of soy protein isolates (SPI) was investigated. Changes in foaming properties of SPI were then examined with the addition of polyols at different concentrations. The interactions between SPI and polyols resulted in a substantial decrease in protein surface hydrophobicity and intrinsic tryptophan fluorescence intensity, along with the covering of tyrosine. Furthermore, circular dichroism (CD) spectroscopy of SPI suggested that a more ordered and compact conformation was induced by polyols. Consequently, these structural changes led to lower foamability of SPI. An increase in the viscosity of SPI suspension seemed to be advantageous for improving the foam stability of SPI.
Aewsiri Tanong, Benjakul Soottawat, Visessanguan Wonnop, Wierenga Peter A., Gruppen Harry (2011): Improvement of foaming properties of cuttlefish skin gelatin by modification with N-hydroxysuccinimide esters of fatty acid. Food Hydrocolloids, 25, 1277-1284  https://doi.org/10.1016/j.foodhyd.2010.11.027
Antipova A.S., Semenova M.G. (1997): Influence of sucrose on the thermodynamic properties of the 11S globulin of Vicia faba-dextran-aqueous solvent system. Food Hydrocolloids, 11, 415-421  https://doi.org/10.1016/S0268-005X(97)80039-2
Báez Germán D., Busti Pablo A., Verdini Roxana, Delorenzi Néstor J. (2013): Glycation of heat-treated β-lactoglobulin: Effects on foaming properties. Food Research International, 54, 902-909  https://doi.org/10.1016/j.foodres.2013.08.013
Baier Stefan K., McClements D.Julian (2003): Impact of sorbitol on the thermostability and heat-induced gelation of bovine serum albumin. Food Research International, 36, 1081-1087  https://doi.org/10.1016/j.foodres.2003.09.003
Bolontrade Agustín J., Scilingo Adriana A., Añón María C. (2013): Amaranth proteins foaming properties: Adsorption kinetics and foam formation—Part 1. Colloids and Surfaces B: Biointerfaces, 105, 319-327  https://doi.org/10.1016/j.colsurfb.2012.12.039
Chanasattru Wanlop, Decker Eric A., McClements D. Julian (2007): Modulation of thermal stability and heat-induced gelation of β-lactoglobulin by high glycerol and sorbitol levels. Food Chemistry, 103, 512-520  https://doi.org/10.1016/j.foodchem.2006.08.020
Chanasattru Wanlop, Decker Eric A., Julian McClements D. (2008): Impact of cosolvents (polyols) on globular protein functionality: Ultrasonic velocity, density, surface tension and solubility study. Food Hydrocolloids, 22, 1475-1484  https://doi.org/10.1016/j.foodhyd.2007.09.007
Chen Haiying, Wu Fengfeng, Duan Xiang, Yang Na, Xu Ying, Xu Baocai, Jin Zhengyu, Xu Xueming (2013): Characterization of emulsions prepared by egg yolk phosvitin with pectin, glycerol and trehalose. Food Hydrocolloids, 30, 123-129  https://doi.org/10.1016/j.foodhyd.2012.05.007
Cheung Lamlam, Wanasundara Janitha, Nickerson Michael T. (2014): The Effect of pH and NaCl Levels on the Physicochemical and Emulsifying Properties of a Cruciferin Protein Isolate. Food Biophysics, 9, 105-113  https://doi.org/10.1007/s11483-013-9323-2
Choi Siu-Mei, Ma Ching-Yung (2007): Structural characterization of globulin from common buckwheat (Fagopyrum esculentum Moench) using circular dichroism and Raman spectroscopy. Food Chemistry, 102, 150-160  https://doi.org/10.1016/j.foodchem.2006.05.011
Davis J.P., Foegeding E.A. (2007): Comparisons of the foaming and interfacial properties of whey protein isolate and egg white proteins. Colloids and Surfaces B: Biointerfaces, 54, 200-210  https://doi.org/10.1016/j.colsurfb.2006.10.017
Foegeding E. Allen, Luck P.J., Davis J.P. (2006): Factors determining the physical properties of protein foams. Food Hydrocolloids, 20, 284-292  https://doi.org/10.1016/j.foodhyd.2005.03.014
Galazka Vanda B, Dickinson Eric, Ledward Dave A (2000): Emulsifying properties of ovalbumin in mixtures with sulphated polysaccharides: effects of pH, ionic strength, heat and high-pressure treatment. Journal of the Science of Food and Agriculture, 80, 1219-1229  https://doi.org/10.1002/1097-0010(200006)80:8<1219::AID-JSFA626>3.0.CO;2-W
Guzey Demet, McClements David Julian, Weiss Jochen (2003): Adsorption kinetics of BSA at air–sugar solution interfaces as affected by sugar type and concentration. Food Research International, 36, 649-660  https://doi.org/10.1016/S0963-9969(03)00004-8
Jiang Jiang, Chen Jie, Xiong Youling L. (2009): Structural and Emulsifying Properties of Soy Protein Isolate Subjected to Acid and Alkaline pH-Shifting Processes. Journal of Agricultural and Food Chemistry, 57, 7576-7583  https://doi.org/10.1021/jf901585n
Jiang Lianzhou, Wang Zhongjiang, Li Yang, Meng Xianghe, Sui Xiaonan, Qi Baokun, Zhou Linyi (2014): Relationship between surface hydrophobicity and structure of soy protein isolate subjected to different ionic strength. International Journal of Food Properties, , 140609124113008-  https://doi.org/10.1080/10942912.2013.865057
Kato Akio, Nakai Shuryo (1980): Hydrophobicity determined by a fluorescence probe method and its correlation with surface properties of proteins. Biochimica et Biophysica Acta (BBA) - Protein Structure, 624, 13-20  https://doi.org/10.1016/0005-2795(80)90220-2
Kim Hyun Jung, Kim Byong Ki (2015): Comparison of soy protein concentrates produced using membrane ultrafiltration and acid precipitation. Food Science and Biotechnology, 24, 67-73  https://doi.org/10.1007/s10068-015-0011-5
Kumar Vineet, Chari Ravi, Sharma Vikas K., Kalonia Devendra S. (2011): Modulation of the thermodynamic stability of proteins by polyols: Significance of polyol hydrophobicity and impact on the chemical potential of water. International Journal of Pharmaceutics, 413, 19-28  https://doi.org/10.1016/j.ijpharm.2011.04.011
Kwaambwa H.M., Maikokera R. (2007): A fluorescence spectroscopic study of a coagulating protein extracted from Moringa oleifera seeds. Colloids and Surfaces B: Biointerfaces, 60, 213-220  https://doi.org/10.1016/j.colsurfb.2007.06.015
Lange Reinhard, Balny Claude (2002): UV-visible derivative spectroscopy under high pressure. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1595, 80-93  https://doi.org/10.1016/S0167-4838(01)00336-3
Lau Cathy Ka, Dickinson Eric (2005): Instability and structural change in an aerated system containing egg albumen and invert sugar. Food Hydrocolloids, 19, 111-121  https://doi.org/10.1016/j.foodhyd.2004.04.020
Liang Li, Tajmir-Riahi H. A., Subirade Muriel (2008): Interaction of β-Lactoglobulin with Resveratrol and its Biological Implications. Biomacromolecules, 9, 50-56  https://doi.org/10.1021/bm700728k
Liu S., Elmer C., Low N.H., Nickerson M.T. (2010): Effect of pH on the functional behaviour of pea protein isolate–gum Arabic complexes. Food Research International, 43, 489-495  https://doi.org/10.1016/j.foodres.2009.07.022
Lv Jiao, Zhao Yuan, Wang Jianzhong, Ouyang Jie, Wang Fengjun (2015): Effects of environmental factors on functional properties of Chinese chestnut (Castanea mollissima) protein isolates. European Food Research and Technology, 240, 463-469  https://doi.org/10.1007/s00217-014-2366-x
MARTIN A, GROLLE K, BOS M, STUART M, VANVLIET T (2002): Network Forming Properties of Various Proteins Adsorbed at the Air/Water Interface in Relation to Foam Stability. Journal of Colloid and Interface Science, 254, 175-183  https://doi.org/10.1006/jcis.2002.8592
McClements David Julian (2002): Modulation of Globular Protein Functionality by Weakly Interacting Cosolvents. Critical Reviews in Food Science and Nutrition, 42, 417-471  https://doi.org/10.1080/20024091054210
Moro Andrea, Báez Germán D., Busti Pablo A., Ballerini Griselda A., Delorenzi Néstor J. (2011): Effects of heat-treated β-lactoglobulin and its aggregates on foaming properties. Food Hydrocolloids, 25, 1009-1015  https://doi.org/10.1016/j.foodhyd.2010.09.021
Pallarès Irantzu, Vendrell Josep, Avilés Francesc X., Ventura Salvador (2004): Amyloid Fibril Formation by a Partially Structured Intermediate State of α-Chymotrypsin. Journal of Molecular Biology, 342, 321-331  https://doi.org/10.1016/j.jmb.2004.06.089
PANYAM D (1996): Enhancing the functionality of food proteins by enzymatic modification. Trends in Food Science & Technology, 7, 120-125  https://doi.org/10.1016/0924-2244(96)10012-1
Ragone Raffaele, Colonna Giovanni, Balestrieri Ciro, Servillo Luigi, Irace Gaetano (1984): Determination of tyrosine exposure in proteins by second-derivative spectroscopy. Biochemistry, 23, 1871-1875  https://doi.org/10.1021/bi00303a044
Raikos Vassilios, Campbell Lydia, Euston Stephen R. (2007): Effects of sucrose and sodium chloride on foaming properties of egg white proteins. Food Research International, 40, 347-355  https://doi.org/10.1016/j.foodres.2006.10.008
Semenova Maria G, Antipova Anna S, Belyakova Larisa E (2002): Food protein interactions in sugar solutions. Current Opinion in Colloid & Interface Science, 7, 438-444  https://doi.org/10.1016/S1359-0294(02)00079-1
Shang Li, Wang Yizhe, Jiang Junguang, Dong Shaojun (2007): pH-Dependent Protein Conformational Changes in Albumin:Gold Nanoparticle Bioconjugates:  A Spectroscopic Study. Langmuir, 23, 2714-2721  https://doi.org/10.1021/la062064e
Stănciuc Nicoleta, Râpeanu Gabriela, Bahrim Gabriela, Aprodu Iuliana (2012): pH and heat-induced structural changes of bovine apo-α-lactalbumin. Food Chemistry, 131, 956-963  https://doi.org/10.1016/j.foodchem.2011.09.087
Stănciuc Nicoleta, Aprodu Iuliana, Ioniță Elena, Bahrim Gabriela, Râpeanu Gabriela (2015): Exploring the process–structure–function relationship of horseradish peroxidase through investigation of pH- and heat induced conformational changes. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, 147, 43-50  https://doi.org/10.1016/j.saa.2015.03.023
Tong Ping, Gao Jinyan, Chen Hongbing, Li Xin, Zhang Yin, Jian Shan, Wichers Harry, Wu Zhihua, Yang Anshu, Liu Fahui (2012): Effect of heat treatment on the potential allergenicity and conformational structure of egg allergen ovotransferrin. Food Chemistry, 131, 603-610  https://doi.org/10.1016/j.foodchem.2011.08.084
Vagenende Vincent, Yap Miranda G. S., Trout Bernhardt L. (2009): Mechanisms of Protein Stabilization and Prevention of Protein Aggregation by Glycerol. Biochemistry, 48, 11084-11096  https://doi.org/10.1021/bi900649t
Wu Wei, Zhang Caimeng, Kong Xiangzhen, Hua Yufei (2009): Oxidative modification of soy protein by peroxyl radicals. Food Chemistry, 116, 295-301  https://doi.org/10.1016/j.foodchem.2009.02.049
Xue Feng, Li Chen, Zhu Xiangwei, Wang Lufeng, Pan Siyi (2013): Comparative studies on the physicochemical properties of soy protein isolate-maltodextrin and soy protein isolate-gum acacia conjugate prepared through Maillard reaction. Food Research International, 51, 490-495  https://doi.org/10.1016/j.foodres.2013.01.012
Yang Xin, Foegeding E. Allen (2010): Effects of sucrose on egg white protein and whey protein isolate foams: Factors determining properties of wet and dry foams (cakes). Food Hydrocolloids, 24, 227-238  https://doi.org/10.1016/j.foodhyd.2009.09.011
Yin Shou-Wei, Tang Chuan-He, Wen Qi-Biao, Yang Xiao-Quan, Li Lin (2008): Functional properties and in vitro trypsin digestibility of red kidney bean (Phaseolus vulgaris L.) protein isolate: Effect of high-pressure treatment. Food Chemistry, 110, 938-945  https://doi.org/10.1016/j.foodchem.2008.02.090
Yuan Yang, Wan Zhi-Li, Yin Shou-Wei, Yang Xiao-Quan, Qi Jun-Ru, Liu Guo-Qin, Zhang Ye (2013): Characterization of complexes of soy protein and chitosan heated at low pH. LWT - Food Science and Technology, 50, 657-664  https://doi.org/10.1016/j.lwt.2012.07.034
Zhang J., Liang L., Tian Z., Chen L., Subirade M. (2012): Preparation and in vitro evaluation of calcium-induced soy protein isolate nanoparticles and their formation mechanism study. Food Chemistry, 133, 390-399  https://doi.org/10.1016/j.foodchem.2012.01.049
Zhang Yating, Tan Chen, Eric Karangwa, Abbas Shabbar, Liu Fengru, Zhang Xiaoming, Xia Shuqin, Jia Chengsheng (2015): Effect of limited enzymatic hydrolysis on physico-chemical properties of soybean protein isolate-maltodextrin conjugates. International Journal of Food Science & Technology, 50, 226-232  https://doi.org/10.1111/ijfs.12624
ZHAO W, YANG R (2008): The effect of pulsed electric fields on the inactivation and structure of lysozyme. Food Chemistry, 110, 334-343  https://doi.org/10.1016/j.foodchem.2008.02.008
Zhao Juyang, Dong Fujia, Li Yuanyuan, Kong Baohua, Liu Qian (2015): Effect of freeze–thaw cycles on the emulsion activity and structural characteristics of soy protein isolate. Process Biochemistry, 50, 1607-1613  https://doi.org/10.1016/j.procbio.2015.06.021
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