Abstract
The effect of ball milling on physicochemical, functional and rheological properties and structural characteristics of cold-extruded whey protein isolate (TWPI) was investigated as a function of grinding time. Ball milling decreased the free sulfhydryl content of all the samples. Furthermore, ball milling and cold extrusion could enhance surface hydrophobicity, emulsifying and rheological properties of WPI. The solubility of cold-extruded WPI was far higher than the traditional heat-extruded WPI. The viscoelastic modulus of TWPI, ground by ball milling for 10 h, dramatically increased compared to that of WPI at 85 °C. Scanning electron microscopy revealed that a ball-milling treatment of 2 h remarkably decreased the particle size of all the samples. FTIR demonstrated that ball-milling treatment decreased the ordered secondary structure (α-helix and β-sheet) of WPI. Therefore, a combination of cold extrusion and ball milling could remarkably enhance the emulsifying and rheological properties of WPI, an effective way for providing novel functional ingredients to the dairy industry.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
References
Anandharamakrishnan C, Rielly CD, Agf S (2008) Loss of solubility of α-lactalbumin and β-lactoglobulin during the spray drying of whey proteins. LWT-Food Sci Technol 41:270–277. https://doi.org/10.1016/j.lwt.2007.03.004
Banach JC, Clark S, Lamsal BP (2018) Extrusion modifies some physicochemical properties of milk protein concentrate for improved performance in high-protein nutrition bars. J Sci Food Agric 98:391–399. https://doi.org/10.1002/jsfa.8632
Barth A (2007) Infrared spectroscopy of proteins. BBA Bioenergetics 1767:1073–1101. https://doi.org/10.1016/j.bbabio.2007.06.004
Bolm C, Hernández JG (2018) From synthesis of amino acids and peptides to enzymatic catalysis: a bottom-up approach in mechanochemistry. ChemSusChem 11:1410–1420. https://doi.org/10.1002/cssc.201800113
Brindaban Ranu AS (2014) Ball milling towards green synthesis: applications, projects, challenges. Royal Society of Chemistry, Milton. https://doi.org/10.1039/9781782621980
Britten M, Giroux HJ, Jean Y, Rodrigue N (1994) Composite blends from heat-denatured and undenatured whey protein: emulsifying properties. Int Dairy J 4:25–36. https://doi.org/10.1016/0958-6946(94)90047-7
Burmeister C, Titscher L, Breitung-Faes S, Kwade A (2017) Dry grinding in planetary ball mills: evaluation of a stressing model. Adv Powder Technol 29:191–201. https://doi.org/10.1016/j.apt.2017.11.001
Carter BG, Drake MA (2018) Invited review: the effects of processing parameters on the flavor of whey protein ingredients. J Dairy Sci 101:6691–6702. https://doi.org/10.3168/jds.2018-14571
Chandrapala J, Zisu B, Palmer M, Kentish S, Ashokkumar M (2011) Effects of ultrasound on the thermal and structural characteristics of proteins in reconstituted whey protein concentrate. Ultrason Sonochem 18:951–957. https://doi.org/10.1016/j.ultsonch.2010.12.016
Cho MH, Zheng X, Wang SS, Kim Y, And CTH (1995) Production of natural flavors using a cold extrusion process. ACS Symp Ser 9:120–126. https://doi.org/10.1021/bk-1995-0610.ch009
Hamada D, Segawa S, Goto Y (1996) Non-native α-helical intermediate in the refolding of β-lactoglobulin, a predominantly β-sheet protein. Nat Struct Biol 3:868–873. https://doi.org/10.1038/nsb1096-868
Jiang J, Xiong YL, Chen J (2010) 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 Agric Food Chem 58:8035–8042. https://doi.org/10.1021/jf101045b
Joyce AM, Kelly AL, O’Mahony JA (2018) Controlling denaturation and aggregation of whey proteins during thermal processing by modifying temperature and calcium concentration. Int J Dairy Technol 71:446–453. https://doi.org/10.1111/1471-0307.12507
Khanitta M, Syedsh R (2009) Physicochemical changes in whey protein concentrate texturized by reactive supercritical fluid extrusion. J Food Eng 95:627–635. https://doi.org/10.1016/j.jfoodeng.2009.06.030
Khatkar AB, Kaur A, Khatkar SK, Mehta N (2018) Optimization of processing time, amplitude and concentration for ultrasound-assisted modification of whey protein using response surface methodology. J Food Sci Technol 55:2298–2309. https://doi.org/10.1007/s13197-018-3147-5
Koch L, Emin MA, Schuchmann HP (2017) Influence of processing conditions on the formation of whey protein-citrus pectin conjugates in extrusion. J Food Eng 193:1–9. https://doi.org/10.1016/j.jfoodeng.2016.08.012
Liu B, Wang H, Hu T, Zhang P, Zhang Z, Pan S, Hu H (2017) Ball-milling changed the physicochemical properties of SPI and its cold-set gels. J Food Eng 195:158–165. https://doi.org/10.1016/j.jfoodeng.2016.10.006
Manoi K, Rizvi SSH (2008) Rheological characterizations of texturized whey protein concentrate-based powders produced by reactive supercritical fluid extrusion. Food Res Int 41:786–796. https://doi.org/10.1016/j.foodres.2008.07.001
Manoi K, Rizvi SSH (2009) Emulsification mechanisms and characterizations of cold, gel-like emulsions produced from texturized whey protein concentrate. Food Hydrocoll 23:1837–1847. https://doi.org/10.1016/j.foodhyd.2009.02.011
Mcclements DJ, Monahan FJ, Kinsella JE (1993) Disulfide bond formation affects stability of whey protein isolate emulsions. J Food Sci 58:1036–1039. https://doi.org/10.1111/j.1365-2621.1993.tb06106.x
Monder C, Ramstad PE (1953) The effect of ball-milling upon certain properties of proteins. Arch Biochem Biophys 46:376–384. https://doi.org/10.1016/0003-9861(53)90209-4
Mudgal P, Daubert CR, Foegeding EA (2011) Effects of protein concentration and CaCl2 on cold-set thickening mechanism of β-lactoglobulin at low pH. Int Dairy J 21:319–326. https://doi.org/10.1016/j.idairyj.2010.11.014
Mustapha NA, Ruttarattanamongkol K, Rizvi SSH (2012) The effects of supercritical fluid extrusion process on surface hydrophobicity of whey protein concentrate and its relation to storage and heat stability of concentrated emulsions. Food Res Int 48:470–477. https://doi.org/10.1016/j.foodres.2012.05.015
Nalesnik CA, Onwulata CI, Tunick MH, Phillips JG, Tomasula PM (2007) The effects of drying on the properties of extruded whey protein concentrates and isolates. J Food Eng 80:688–694. https://doi.org/10.1016/j.jfoodeng.2006.06.029
Nir I, Feldman Y, Aserin A, Garti N (2010) Surface properties and emulsification behavior of denatured soy proteins. J Food Sci 59:606–610. https://doi.org/10.1111/j.1365-2621.1994.tb05573.x
O’Loughlin IB, Kelly PM, Murray BA, Fitzgerald RJ, Brodkorb A (2015) Concentrated whey protein ingredients: a Fourier transformed infrared spectroscopy investigation of thermally induced denaturation. Int J Dairy Technol 68:349–356. https://doi.org/10.1111/1471-0307.12239
Onwulata CI (2012) Thermal and non-thermal extrusion of protein products. Adv Food Extrus Technol. https://doi.org/10.1201/b11286-12
Onwulata CI, Tunick MH, Qi PX (2011) Extrusion texturized dairy proteins: processing and application. Adv Food Nutr Res 62:173–200. https://doi.org/10.1016/b978-0-12-385989-1.00005-3
Pearce KN, Kinsella JE (1978) Emulsifying properties of proteins: evaluation of a turbidimetric technique. J Agric Food Chem 26:716–723. https://doi.org/10.1021/jf60217a041
Qi PX, Onwulata CI (2011a) Physical properties, molecular structures, and protein quality of texturized whey protein isolate: effect of extrusion moisture content. J Dairy Sci 94:2231–2244. https://doi.org/10.3168/jds.2010-3942
Qi PX, Onwulata CI (2011b) Physical properties, molecular structures, and protein quality of texturized whey protein isolate: effect of extrusion temperature. J Agric Food Chem 59:4668–4675. https://doi.org/10.1021/jf2011744
Qi PX, Ren D, Xiao Y, Tomasula PM (2015) Effect of homogenization and pasteurization on the structure and stability of whey protein in milk. J Dairy Sci 98:2884–2897. https://doi.org/10.3168/jds.2014-8920
Rahaman T, Vasiljevic T, Ramchandran L (2015) Conformational changes of β-lactoglobulin induced by shear, heat, and pH-effects on antigenicity. J Dairy Sci 98:4255–4265. https://doi.org/10.3168/jds.2014-9010
Rattray W, Jelen P (1995) Viscous behaviour of whey protein concentrate dispersions. Int Dairy J 5:673–684. https://doi.org/10.1016/0958-6946(95)00018-x
Resch JJ, Daubert CR (2002) Rheological and physicochemical properties of derivatized whey protein concentrate powders. Int J Food Prop 5:419–434. https://doi.org/10.1081/jfp-120005795
Smeller L, Goossens K, Heremans K (1995) Determination of the secondary structure of proteins at high pressure. Vib Spectrosc 8:199–203. https://doi.org/10.1016/0924-2031(94)00032-c
Smithers GW (2008) Whey and whey proteins—from ‘gutter-to-gold’. Int Dairy J 18:695–704. https://doi.org/10.1016/j.idairyj.2008.03.008
Sun C et al (2015a) Combined superfine grinding and heat-shearing treatment for the microparticulation of whey proteins. Food Bioprocess Technol 9:378–386. https://doi.org/10.1007/s11947-015-1629-2
Sun C, Wu T, Liu R, Liang B, Tian Z, Zhang E, Zhang M (2015b) Effects of superfine grinding and microparticulation on the surface hydrophobicity of whey protein concentrate and its relation toemulsions stability. Food Hydrocoll 51:512–518. https://doi.org/10.1016/j.foodhyd.2015.05.027
Sun C, Liu R, Ni K, Wu T, Luo X, Liang B, Zhang M (2016) Reduction of particle size based on superfine grinding: effects on structure, rheological and gelling properties of whey protein concentrate. J Food Eng 186:69–76. https://doi.org/10.1016/j.jfoodeng.2016.03.002
Thomas CR, Geer D (2011) Effects of shear on proteins in solution. Biotechnol Lett 33:443–456. https://doi.org/10.1007/s10529-010-0469-4
Vakifahmetoglu C, Buldu M, Karakuscu A, Ponzoni A, Assefa D, Soraru GD (2015) High surface area carbonous components from emulsion derived SiOC and their gas sensing behavior. J Eur Ceram Soc 35:4447–4452. https://doi.org/10.1016/j.jeurceramsoc.2015.08.030
Van der Plancken I, Van Loey A, Hendrickx ME (2005) Changes in sulfhydryl content of egg white proteins due to heat and pressure treatment. J Agric Food Chem 53:5726–5733. https://doi.org/10.1021/jf050289&%23x002B;
Visschers RW, de Jongh HH (2005) Disulphide bond formation in food protein aggregation and gelation. Biotechnol Adv 23:75–80. https://doi.org/10.1016/j.biotechadv.2004.09.005
Walkenstrom P, Windhab EJ, Hermansson A (1998) Shear-induced structuring of particulate whey protein gels. Food Hydrocoll 12:459–468. https://doi.org/10.1016/s0268-005x(98)00064-2
Xu Y, Wang C, Fu X, Huang Q, Zhang B (2017) Effect of pH and ionic strength on the emulsifying properties of two Octenylsuccinate starches in comparison with gum Arabic. Food Hydrocoll 76:96–102. https://doi.org/10.1016/j.foodhyd.2017.02.015
Yu GQ, Warkentin T, Niu Z, Khan NA, Yu P (2015) Molecular basis of processing-induced changes in protein structure in relation to intestinal digestion in yellow and green type pea (Pisum sativum L.): a molecular spectroscopic analysis. Spectrochim Acta A Mol Biomol Spectrosc 151:980–988. https://doi.org/10.1016/j.saa.2015.06.050
Yu C, Cha Y, Wu F, Fan W, Xu X, Du M (2017) Effects of ball-milling treatment on mussel (Mytilus edulis) protein: structure, functional properties and invitro digestibility. Int J Food Sci Technol 53:683–691. https://doi.org/10.1111/ijfs.13643
Zhao SX, An SG, Wang SZ, Wei SY, Zhang SB (2015) Protein modifications after foxtail millet extrusion: solubility and molecular weight. Adv J Food Sci Technol 7:522–529. https://doi.org/10.19026/ajfst.7.1353
Zhou XM, Li YX (2011) Influence of the measurement on superfine powder by different laser particle analyzer. Adv Mater Res 308–310:2446–2449. https://doi.org/10.4028/www.scientific.net/amr.308-310.2446
Acknowledgements
This study was supported by the project for the Academic Research Program of Northeast Agricultural University (no. 16XG21) and the Natural Science Foundation of Heilongjiang Province of China (no. C2017029).
Author information
Authors and Affiliations
Corresponding authors
Ethics declarations
Conflict of interest
On behalf of all authors, the corresponding author states that there is no conflict of interest.
Additional information
Publisher’s Note
Springer Nature remains neutral with regard to jurisdictional claims in published maps and institutional affiliations.
Rights and permissions
About this article
Cite this article
Yang, N., Li, T., Ma, L. et al. Characterization and structure of cold-extruded whey protein isolate: impact of ball milling. Appl Nanosci 9, 423–433 (2019). https://doi.org/10.1007/s13204-018-0913-7
Received:
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1007/s13204-018-0913-7