Influence of heat treatment on structure, interfacial rheology and emulsifying properties of peanut protein isolate

Zhang Y., Xiong W., Lei L., Pei Y., He L., Ai T., Li Y., Li B., Jiang Y., Liu X., Wang L. (2019): Influence of heat treatment on structure, interfacial rheology and emulsifying properties of peanut protein isolate. Czech J. Food Sci., 37: 212-220.

download PDF

The influence of heat treatment on the protein size, zeta potential, surface hydrophobicity, secondary structure, interfacial rheology and creaming stability of peanut protein isolate (PPI) was studied. Heat treatment of PPI increased the protein size, surface hydrophobicity and interface diffusion rate, and decreased the protein zeta potential, particularly heat treatment at 80°C for 30 min (PPI-80), which increased the surface hydrophobicity from 117.33 ± 2.77 to 253.24 ± 2.47. Interfacial rheology results demonstrated that the heat treatment promoted the absorption of PPI at the oil-water interface, which might be due to the increase of surface hydrophobicity. In contrast, the heat treatment at 90°C resulted in slightly lower surface hydrophobicity and Kdiff compared with PPI-80 due to the hydrolysis of partial protein aggregates during high temperature. Moreover, heat-treated PPI showed better emulsifying properties than unheated PPI. These results would be useful to expand the utilization of PPI products in the food processing industry.

Croguennec Thomas, Renault Anne, Beaufils Sylvie, Dubois Jean-Jacques, Pezennec Stéphane (2007): Interfacial properties of heat-treated ovalbumin. Journal of Colloid and Interface Science, 315, 627-636
Delahaije Roy J. B. M., Wierenga Peter A., van Nieuwenhuijzen Neleke H., Giuseppin Marco L. F., Gruppen Harry (2013): Protein Concentration and Protein-Exposed Hydrophobicity as Dominant Parameters Determining the Flocculation of Protein-Stabilized Oil-in-Water Emulsions. Langmuir, 29, 11567-11574
Delahaije Roy J.B.M., Gruppen Harry, Giuseppin Marco L.F., Wierenga Peter A. (2014): Quantitative description of the parameters affecting the adsorption behaviour of globular proteins. Colloids and Surfaces B: Biointerfaces, 123, 199-206
Feng Xiao-Long, Liu Hong-Zhi, Shi Ai-Min, Liu Li, Wang Qiang, Adhikari Benu (2014): Effects of transglutaminase catalyzed crosslinking on physicochemical characteristics of arachin and conarachin-rich peanut protein fractions. Food Research International, 62, 84-90
Graham D.E, Phillips M.C (1979): Proteins at liquid interfaces. Journal of Colloid and Interface Science, 70, 427-439
Gong Kui-Jie, Shi Ai-Min, Liu Hong-Zhi, Liu Li, Hu Hui, Adhikari Benu, Wang Qiang (2016): Emulsifying properties and structure changes of spray and freeze-dried peanut protein isolate. Journal of Food Engineering, 170, 33-40
Palazolo Gonzalo G., Sorgentini Delia A., Wagner Jorge R. (2004): Emulsifying properties and surface behavior of native and denatured whey soy proteins in comparison with other proteins. Creaming stability of oil-in-water emulsions. Journal of the American Oil Chemists' Society, 81, 625-632
He Xuan-Hui, Liu Hong-Zhi, Liu Li, Zhao Guan-Li, Wang Qiang, Chen Qiong-Ling (2014): Effects of high pressure on the physicochemical and functional properties of peanut protein isolates. Food Hydrocolloids, 36, 123-129
KIOKIAS S, DIMAKOU C, OREOPOULOU V (2007): Effect of heat treatment and droplet size on the oxidative stability of whey protein emulsions. Food Chemistry, 105, 94-100
SAIO KYOKO, TERASHIMA MASAHIKO, WATANABE TOKUJI (1975): FOOD USE OF SOYBEAN 7S AND 11S PROTEINS Changes in Basic Groups of Soybean Proteins by High Temperature Heating. Journal of Food Science, 40, 541-544
Li Chen, Xue Haoran, Chen Zhiyan, Ding Qiao, Wang Xingguo (2014): Comparative studies on the physicochemical properties of peanut protein isolate–polysaccharide conjugates prepared by ultrasonic treatment or classical heating. Food Research International, 57, 1-7
Li Fang, Kong Xiangzhen, Zhang Caimeng, Hua Yufei (2011): Effect of heat treatment on the properties of soy protein-stabilised emulsions. International Journal of Food Science & Technology, 46, 1554-1560
Mahmoudi Najet, Axelos Monique A. V., Riaublanc Alain (2011): Interfacial properties of fractal and spherical whey protein aggregates. Soft Matter, 7, 7643-
MARTINEZ K, SANCHEZ C, RUIZHENESTROSA V, RODRIGUEZPATINO J, PILOSOF A (2007): Effect of limited hydrolysis of soy protein on the interactions with polysaccharides at the air–water interface. Food Hydrocolloids, 21, 813-822
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
Murray B.S. (2002): Interfacial rheology of food emulsifiers and proteins. Current Opinion in Colloid & Interface Science, 7: 426–431.
Nicolai Taco, Britten Michel, Schmitt Christophe (2011): β-Lactoglobulin and WPI aggregates: Formation, structure and applications. Food Hydrocolloids, 25, 1945-1962
Peng Weiwei, Kong Xiangzhen, Chen Yeming, Zhang Caimeng, Yang Yuexi, Hua Yufei (2016): Effects of heat treatment on the emulsifying properties of pea proteins. Food Hydrocolloids, 52, 301-310
Petruccelli S., Anon M. C. (1995): Thermal Aggregation of Soy Protein Isolates. Journal of Agricultural and Food Chemistry, 43, 3035-3041
Qin Li‐Qiang, Xun Pengcheng, Bujnowski Deborah, Daviglus Martha L., Van Horn Linda, Stamler Jeremiah, He Ka (2011): Higher Branched-Chain Amino Acid Intake Is Associated with a Lower Prevalence of Being Overweight or Obese in Middle-Aged East Asian and Western Adults. The Journal of Nutrition, 141, 249-254
Rodríguez Patino Juan M., Rodríguez Niño M. Rosario, Sánchez Cecilio Carrera (1999): Adsorption of Whey Protein Isolate at the Oil−Water Interface as a Function of Processing Conditions:  A Rheokinetic Study. Journal of Agricultural and Food Chemistry, 47, 2241-2248
Ruffin Emilie, Schmit Tiffany, Lafitte Géraldine, Dollat Jean-Marie, Chambin Odile (2014): The impact of whey protein preheating on the properties of emulsion gel bead. Food Chemistry, 151, 324-332
Sellmeyer Deborah E, Stone Katie L, Sebastian Anthony, Cummings Steven R (2001): A high ratio of dietary animal to vegetable protein increases the rate of bone loss and the risk of fracture in postmenopausal women. The American Journal of Clinical Nutrition, 73, 118-122
Tergesen J.F. (2010): Perspective sustainability points to plant proteins. Food Technology, 64: 88.
Wan Zhi-Li, Guo Jian, Yang Xiao-Quan (2015): Plant protein-based delivery systems for bioactive ingredients in foods. Food & Function, 6, 2876-2889
Wang Jin-Mei, Xia Ning, Yang Xiao-Quan, Yin Shou-Wei, Qi Jun-Ru, He Xiu-Ting, Yuan De-Bao, Wang Li-Juan (2012): Adsorption and Dilatational Rheology of Heat-Treated Soy Protein at the Oil–Water Interface: Relationship to Structural Properties. Journal of Agricultural and Food Chemistry, 60, 3302-3310
Wu Haiwen, Wang Qiang, Ma Tiezheng, Ren Jiajia (2009): Comparative studies on the functional properties of various protein concentrate preparations of peanut protein. Food Research International, 42, 343-348
Xiao Jie, Li Yunqi, Li Ji, Gonzalez Alejandro Perez, Xia Qiuyang, Huang Qingrong (2014): Structure, Morphology, and Assembly Behavior of Kafirin. Journal of Agricultural and Food Chemistry, 63, 216-224
Xiong Wenfei, Wang Yuntao, Zhang Chunlan, Wan Jiawei, Shah Bakht Ramin, Pei Yaqiong, Zhou Bin, Li Jin, Li Bin (2016): High intensity ultrasound modified ovalbumin: Structure, interface and gelation properties. Ultrasonics Sonochemistry, 31, 302-309
Zhang Qiu-Ting, Tu Zong-Cai, Xiao Hui, Wang Hui, Huang Xiao-Qin, Liu Guang-Xian, Liu Cheng-Mei, Shi Yan, Fan Liang-Liang, Lin De-Rong (2014): Influence of ultrasonic treatment on the structure and emulsifying properties of peanut protein isolate. Food and Bioproducts Processing, 92, 30-37
download PDF

© 2021 Czech Academy of Agricultural Sciences | Prohlášení o přístupnosti