sweet potato protein; High hydrostatic pressure; salt ions; structure; gelation properties
Abstract :
[en] The effects of monovalent (NaCl) and divalent (CaCl2and MgCl2) salts combined with high hydrostatic pressure(HHP) on structure and gelation properties of sweet potato protein (SPP) were investigated. Surface hydro-phobicity and zeta potential of SPP significantly decreased as salts concentration increased. The total amount ofsulfhydryl (-SH-) groups in SPP decreased with addition of NaCl, CaCl2and MgCl2under HHP, whereas thedisulfide bonds (-S-S-) increased from 0.59 to 0.80 and 0.74 μmol/g with addition of 0.1 and 0.2 moL/L of CaCl2combined with HHP, respectively. The α-helical content of SPP was increased by all three salts, but decreased assalts combined with HHP, while β-sheet content was increased at high ionic strength with HHP, especially inpresence of CaCl2and MgCl2, being increased from 30.40 to 33.45 and 33.55 g/100 g, respectively. The storagemodulus (G′) of SPP was enhanced by salts and HHP, even though it decreased at high ionic strength. Texturalproperties and water holding capacity of SPP gels were improved with salt ions by HHP, being attributed to morebound water.
Mu, Tai-Hua; Laboratory of Food Chemistry and Nutrition Science, Institute of Food Science and Technology, Chinese Academy of Agricultural Sciences, Key Laboratory of Agro-Products Processing, Ministry of Agriculture, No. 2 Yuan Ming Yuan West Road, Haidian District, P.O. Box 5109, Beijing, 100193, PR China
Zhang, Miao; Laboratory of Food Chemistry and Nutrition Science, Institute of Food Science and Technology, Chinese Academy of Agricultural Sciences, Key Laboratory of Agro-Products Processing, Ministry of Agriculture, No. 2 Yuan Ming Yuan West Road, Haidian District, P.O. Box 5109, Beijing, 100193, PR China
Richel, Aurore ; Université de Liège - ULiège > Agronomie, Bio-ingénierie et Chimie (AgroBioChem) > SMARTECH
Language :
English
Title :
Effect of salts combined with high hydrostatic pressure on structure and gelation properties of sweet potato protein
Publication date :
2018
Journal title :
LWT - Food Science and Technology
ISSN :
0023-6438
eISSN :
1096-1127
Publisher :
Elsevier, United States
Volume :
93
Pages :
36-44
Peer reviewed :
Peer Reviewed verified by ORBi
Funders :
The authors gratefully acknowledge the earmarked fund for ChinaAgriculture Research System (CARS-10-B21) and National Key R & DProgram of China (2016YFE0133600)
Albarracín, W., Sánchez, I.C., Grau, R., et al. Salt in food processing; usage and reduction: A review. International Journal of Food Science and Technology 46:7 (2011), 1329–1336.
Añón, M.C., De Lamballerie, M., Speroni, F., Influence of NaCl concentration and high pressure treatment on thermal denaturation of soybean proteins. Innovative Food Science & Emerging Technologies 12:4 (2011), 443–450.
Arakawa, T., Timasheff, S.N., Mechanism of protein salting in and salting out by divalent cation salts: Balance between hydration and salt binding. Biochemistry 23:25 (1984), 5912–5923.
Arogundade, L.A., Mu, T.H., Añón, M.C., Heat-induced gelation properties of isoelectric and ultrafiltered sweet potato protein isolate and their gel microstructure. Food Research International 49:1 (2012), 216–225.
Barat, J.M., Pérez-Esteve, E., Aristoy, M.C., et al. Partial replacement of sodium in meat and fish products by using magnesium salts. A review. Plant and Soil 368:1–2 (2013), 179–188.
Bryant, C.M., McClements, D.J., Influence of NaCl and CaCl2 on cold-set gelation of heat-denatured whey protein. Journal of Food Science 65:5 (2000), 801–804.
Cando, D., Herranz, B., Borderías, A.J., Moreno, H.M., Effect of high pressure on reduced sodium chloride surimi gels. Food Hydrocolloids 51 (2015), 176–187.
Cao, L., Su, S., Regenstein, J.M., et al. Ca2+-induced conformational changes of myosin from silver carp (Hypophthalmichthys molitrix) in gelation. Food Biophysics 10:4 (2015), 447–455.
Chen, N., Zhao, M., Chassenieux, C., Nicolai, T., The effect of adding NaCl on thermal aggregation and gelation of soy protein isolate. Food Hydrocolloids 70 (2017), 88–95.
De Maria, S., Ferrari, G., Maresca, P., Effects of high hydrostatic pressure on the conformational structure and the functional properties of bovine serum albumin. Innovative Food Science & Emerging Technologies 33 (2016), 67–75.
Ercili-Cura, D., Lille, M., Legland, D., Gaucel, S., Poutanen, K., Partanen, R., et al. Structural mechanisms leading to improved water retention in acid milk gels by use of transglutaminase. Food Hydrocolloids 30:1 (2013), 419–427.
FAOSTAT, Production quantity [Internet]. 2016, Food and Agricultural Organization http://www.fao.org/faostat/en/#data/QC (Accessed 03 August 2018).
Ganasen, P., Benjakul, S., Chemical composition, physical properties and microstructure of pidan white as affected by different divalent and monovalent cations. Journal of Food Biochemistry 35:5 (2011), 1528–1537.
Grossi, A., Olsen, K., Bolumar, T., et al. The effect of high pressure on the functional properties of pork myofibrillar proteins. Food Chemistry 196 (2016), 1005–1015.
Gupta, U.C., Gupta, S.C., Sources and deficiency diseases of mineral nutrients in human health and nutrition: A review. Pedosphere 24:1 (2014), 13–38.
Hamada, M., Ishizaki, S., Nagai, T., Variation of SH content and kamaboko-gel forming ability of shark muscle protein by electrolysis. Journal of Shimonoseki University of Fisheries 42 (1994), 131–135.
Han, M., Wang, P., Xu, X., et al. Low-field NMR study of heat-induced gelation of pork myofibrillar proteins and its relationship with microstructural characteristics. Food Research International 62 (2014), 1175–1182.
He, R., He, H.Y., Chao, D., Ju, X., Aluko, R., Effects of high pressure and heat treatments on physicochemical and gelation properties of rapeseed protein isolate. Food and Bioprocess Technology 7:5 (2014), 1344–1353.
Jiang, L., Wang, Z., Li, Y., Meng, X., Sui, X., Qi, B., et al. Relationship between surface hydrophobicity and structure of soy protein isolate subjected to different ionic strength. International Journal of Food Properties 18:5 (2015), 1059–1074.
Khan, N.M., Mu, T.H., Sun, H.N., et al. Effects of high hydrostatic pressure on secondary structure and emulsifying behavior of sweet potato protein. High Pressure Research 35:2 (2015), 189–202.
Kuhn, K.R., Cavallieri, Â.L.F., Da Cunha, R.L., Cold-set whey protein-flaxseed gum gels induced by mono or divalent salt addition. Food Hydrocolloids 25:5 (2011), 1302–1310.
Lakemond, C.M., de Jongh, H.H., Paques, M., van Vliet, T., Gruppen, H., et al. Gelation of soy glycinin; influence of pH and ionic strength on network structure in relation to protein conformation. Food Hydrocolloids 17:3 (2003), 365–377.
Liang, Y., Guo, B., Zhou, A., et al. Effect of high pressure treatment on gel characteristics and gel formation mechanism of bighead carp (Aristichthys nobilis) surimi gels. Journal of Food Processing and Preservation 40 (2016), 1–8.
Mecit, H.O., Kathryn, L.M., Michael, J.M., Moshe, R., Monitoring the effects of divalent ions (Mn+2 and Ca+2) in heat-set whey protein gels. LWT-Food Science and Technology 56 (2014), 93–100.
Mu, T.H., Tan, S.S., Xue, Y.L., The amino acid composition, solubility and emulsifying properties of sweet potato protein. Food Chemistry 112:4 (2009), 1002–1005.
Qin, Z., Guo, X., Lin, Y., Chen, J., Liao, X., Hu, X., et al. Effects of high hydrostatic pressure on physicochemical and functional properties of walnut (Juglans regia L.) protein isolate. Journal of the Science of Food and Agriculture 93:5 (2013), 1105–1111.
Sun, M.J., Mu, T.H., Zhang, M., et al. Nutritional assessment and effects of heat processing on digestibility of Chinese sweet potato protein. Journal of Food Composition and Analysis 26:1 (2012), 104–110.
Tabilo-Munizaga, G., Gordon, T.A., Villalobos-Carvajal, R., Moreno-Osorio, L., Salazar, F.N., Pérez-Won, M., et al. Effects of high hydrostatic pressure (HHP) on the protein structure and thermal stability of Sauvignon blanc wine. Food Chemistry 155 (2014), 214–220.
Tobin, B.D., O'Sullivan, M.G., Hamill, R.M., Kerry, J.P., The impact of salt and fat level variation on the physiochemical properties and sensory quality of pork breakfast sausages. Meat Science 93:2 (2013), 145–152.
Wang, M., Chen, X., Zou, Y., Chen, H., Xue, S., Qian, C., et al. High-pressure processing-induced conformational changes during heating affect water holding capacity of myosin gel. International Journal of Food Science and Technology 52 (2016), 724–732.
Whitmore, L., Wallace, B.A., DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data. Nucleic Acids Research 32:suppl 2 (2004), W668–W673.
Wu, L., Wu, T., Wu, J., Chang, R., Lan, X., Wei, K., et al. Effects of cations on the “salt in” of myofibrillar proteins. Food Hydrocolloids 58 (2016), 179–183.
Xue, S.W., Yang, H.J., Wang, H.H., et al. High-pressure effects on the molecular aggregation and physicochemical properties of myosin in relation to heat gelation. Food Research International 99 (2017), 413–418.
Zhang, Y.H., Huang, L.H., Tang, S.X., et al. Effect of ionic strength on formation and microstructure of self-assembly globulin nanofibrils and gels. Digest Journal of Nanomaterials and Biostructures 9:3 (2014), 951–957.
Zhang, Z., Yang, Y., Tang, X., Chen, Y., You, Y., Chemical forces and water holding capacity study of heat-induced myofibrillar protein gel as affected by high pressure. Food Chemistry 188 (2015), 111–118.
Zhang, Z., Yang, Y., Tang, X., Chen, Y., You, Y., Chemical forces study of heat-induced myofibrillar protein gel as affected by partial substitution of NaCl with KCl, MgCl2 and CaCl2. CyTA - journal of Food 14:2 (2016), 239–247.
Zhou, J.Z., Zhang, H., Gao, L., Wang, L., Qian, H.F., Influence of pH and ionic strength on heat-induced formation and rheological properties of cottonseed protein gels. Food and Bioproducts Processing 96 (2015), 27–34.