Hostname: page-component-cd9895bd7-8ctnn Total loading time: 0 Render date: 2024-12-26T12:59:13.732Z Has data issue: false hasContentIssue false
  • English
  • Français

Comparative experiments of electrical conductivity from whey protein concentrates conventional film and nanofibril film

Published online by Cambridge University Press:  03 February 2020

Chen Guan ,
XueFei He ,
HongHua Xu ,
MeiLi Shao ,
JinYu Ma  and
ZiWen Gao
Chen Guan
Affiliation:
Key Laboratory of Dairy Science, Ministry of Education, Northeast Agricultural University, Harbin150030, China College of Food Science, Heilongjiang Bayi Agricultural University, Daqing163319, China
XueFei He
Affiliation:
Key Laboratory of Dairy Science, Ministry of Education, Northeast Agricultural University, Harbin150030, China
HongHua Xu*
Affiliation:
Key Laboratory of Dairy Science, Ministry of Education, Northeast Agricultural University, Harbin150030, China
MeiLi Shao
Affiliation:
Key Laboratory of Dairy Science, Ministry of Education, Northeast Agricultural University, Harbin150030, China
JinYu Ma
Affiliation:
Key Laboratory of Dairy Science, Ministry of Education, Northeast Agricultural University, Harbin150030, China
ZiWen Gao
Affiliation:
Key Laboratory of Dairy Science, Ministry of Education, Northeast Agricultural University, Harbin150030, China
*
Author for correspondence: Hong-Hua Xu, Email: [email protected]
Get access Rights & Permissions [Opens in a new window]

Abstract

We compared the electrical conductivity from two different aggregates of whey protein concentrates (WPC) film: conventional amorphous aggregation at natural pH (pH 6.5) and amyloid fibrils at a low pH (pH 2.0) far away from the isoelectric point. The two types of film fabricated by these solutions with different aggregate structures showed large variations in electrical conductivity and other properties. The WPC fibril film (pH 2.0) exhibited higher electrical conductivity than that of the conventional WPC film (pH 6.5), improved mechanical properties and oil resistance, due to varying morphology, higher surface hydrophobicity and more (absolute value) surface charge of film-forming solutions. The evidence from this study suggests that fibrilized WPC with high-ordered and β-sheets-rich structures fabricated high electrical conductivity film, which broadens the potential application of fibrils as functional bio-nanomaterials.

Keywords

Electrical conductivityFibrilfilmwhey protein concentrate
Type
Research Article
Information
Journal of Dairy Research , Volume 87 , Issue 1 , February 2020 , pp. 103 - 109
Copyright
Copyright © Hannah Dairy Research Foundation 2020

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

Abdel-Karim, AM, Salama, AH and Hassan, ML (2018) Electrical conductivity and dielectric properties of nanofibrillated cellulose thin films from bagasse. Journal of Physical Organic Chemistry 56, e3851.Google Scholar
Adamcik, J and Mezzenga, R (2011) Proteins fibrils from a polymer physics perspective. Macromolecules 45, 1137–1150.Google Scholar
Ayadi, MA, Leuliet, JC, Chopard, F, Berthou, M and Lebouché, M (2004) Electrical conductivity of whey protein deposit: xanthan Gum effect on temperature dependency. Food and Bioproducts Processing 82, 320–325.Google Scholar
Banerjee, R and Chen, H (1995) Functional properties of edible films using whey protein concentrate. Journal of Dairy Science 78, 1673–1683.Google Scholar
Bolder, SG, Sagis, LM, Venema, P and van der Linden, E (2007a) Effect of stirring and seeding on whey protein fibril formation. Journal of Agricultural and Food Chemistry 55, 5661–5669.10.1021/jf063351rGoogle Scholar
Bolder, SG, Vasbinder, AJ, Sagis, LMC and van der Linden, E (2007b) Heat-induced whey protein isolate fibrils: conversion, hydrolysis, and disulphide bond formation. International Dairy Journal 17, 846–853.Google Scholar
Bolisetty, S, Harnau, L, Jung, JM and Mezzenga, R (2012) Gelation, phase behavior, and dynamics of beta-lactoglobulin amyloid fibrils at varying concentrations and ionic strengths. Biomacromolecules 13, 3241–3252.Google ScholarPubMed
Bolisetty, S, Arcari, M, Adamcik, J and Mezzenga, R (2015) Hybrid amyloid membranes for continuous flow catalysis. Langmuir 31, 13867–13873.Google ScholarPubMed
Brandenberg, AH, Morr, CV and Weller, CL (1992) Gelation of commercial whey protein concentrates: effect of removal of low-molecular-weight components. Journal of Food Science 57, 427–432.10.1111/j.1365-2621.1992.tb05509.xGoogle Scholar
Dave, AC, Loveday, SM, Anema, SG, Jameson, GB and Singh, H (2015) Formation of nano-fibrils from the A, B and C variants of bovine β-lactoglobulin. International Dairy Journal 41, 64–67.10.1016/j.idairyj.2014.09.011Google Scholar
de Castro, RJS, Domingues, MAF, Ohara, A, Okuro, PK, dos Santos, JG, Brexó, RP and Sato, HH (2017) Whey protein as a key component in food systems: physicochemical properties, production technologies and applications. Food Structure 14, 17–29.Google Scholar
Feng, Z, Wu, G, Liu, C, Li, D, Jiang, B and Zhang, X (2018) Edible coating based on whey protein isolate nanofibrils for antioxidation and inhibition of product browning. Food Hydrocolloids 79, 179–188.Google Scholar
Gao, Y, Wen, S, Wang, W, Yan, W, Zhao, Y, Lei, Z and Miao, R (2012) Ultrasonic-assisted production of graphene with high yield in supercritical CO2 and its high electrical conductivity film. Industrial & Engineering Chemistry Research 53, 2839–2845.Google Scholar
Gao, YZ, Xu, HH, Ju, TT and Zhao, XH (2013) The effect of limited proteolysis by different proteases on the formation of whey protein fibrils. Journal of Dairy Science 96, 7383–7392.Google ScholarPubMed
Henriques, M, Gomes, D and Pereira, C (2016) Whey protein edible coatings: recent developments and applications. In Nedović, V, Raspor, P, Lević, J, Tumbas Šaponjac, V, Barbosa-Cánovas, G (eds), Emerging and Traditional Technologies for Safe, Healthy and Quality Food. Food Engineering Series. Cham, Switzerland: Springer, pp. 177–196.Google Scholar
Iwata, KI, Ishizaki, SH, Handa, AK and Tanaka, MU (2000) Preparation and characterization of edible films from fish water-soluble proteins. Fisheries Science 66, 372–378.Google Scholar
Jordens, S, Ruhs, PA, Sieber, C, Isa, L, Fischer, P and Mezzenga, R (2014) Bridging the gap between the nanostructural organization and macroscopic interfacial rheology of amyloid fibrils at liquid interfaces. Langmuir 30, 10090–10097.10.1021/la5020658Google ScholarPubMed
Knowles, TP and Buehler, MJ (2011) Nanomechanics of functional and pathological amyloid materials. Nature Nanotechnology 6, 469–479.Google ScholarPubMed
Knowles, TP, Fitzpatrick, AW, Meehan, S, Mott, HR, Vendruscolo, M, Dobson, CM and Welland, ME (2007) Role of intermolecular forces in defining material properties of protein nanofibrils. Science 318, 1900–1903.Google ScholarPubMed
Knowles, TP, Oppenheim, TW, Buell, AK, Chirgadze, DY and Welland, ME (2010) Nanostructured films from hierarchical self-assembly of amyloidogenic proteins. Nature Nanotechnology 5, 204–207.Google ScholarPubMed
Kumari, M, Mahajan, H, Joshi, R and Gupta, M (2017) Development and structural characterization of edible films for improving fruit quality. Food Packaging and Shelf Life 12, 42–50.Google Scholar
Le, TC, Letendre, M, Ispasszabo, P, Mateescu, MA, Delmaspatterson, G, Yu, HL and Lacroix, M (2000) Development of biodegradable films from whey proteins by cross-linking and entrapment in cellulose. Journal of Agricultural and Food Chemistry 48, 5566–5575.Google Scholar
Li, C, Adamcik, J and Mezzenga, R (2012) Biodegradable nanocomposites of amyloid fibrils and graphene with shape-memory and enzyme-sensing properties. Nature Nanotechnology 7, 421–427.Google ScholarPubMed
Liu, L, Busuttil, K, Zhang, S, Yang, Y, Wang, C, Besenbacher, F and Dong, M (2011) The role of self-assembling polypeptides in building nanomaterials. Physical Chemistry Chemical Physics 13, 17435–17444.Google ScholarPubMed
Loveday, SM, Wang, XL, Rao, MA, Anema, SG, Creamer, LK and Singh, H (2010) Tuning the properties of β-lactoglobulin nanofibrils with pH, NaCl and CaCl2. International Dairy Journal 20, 571–579.Google Scholar
Loveday, SM, Su, J, Rao, MA, Anema, SG and Singh, H (2011) Effect of calcium on the morphology and functionality of whey protein nanofibrils. Biomacromolecules 12, 3780–3788.Google ScholarPubMed
Mantovani, RA, Pinheiro, AC, Vicente, AA and Cunha, RL (2017) In vitro digestion of oil-in-water emulsions stabilized by whey protein nanofibrils. Food Research International 99(Pt 1), 790–798.Google ScholarPubMed
Mantovani, RA, de Figueiredo Furtado, G, Netto, FM and Cunha, RL (2018) Assessing the potential of whey protein fibril as emulsifier. Journal of Food Engineering 223, 99–108.Google Scholar
Mchugh, TH, Aujard, JF and Krochta, JM (2010) Plasticized whey protein edible films: water vapor permeability properties. Journal of food science 59, 416–419.10.1111/j.1365-2621.1994.tb06980.xGoogle Scholar
Nelson, R, Sawaya, MR, Balbirnie, M, Madsen, AO, Riekel, C, Grothe, R and Eisenberg, D (2005) Structure of the cross-beta spine of amyloid-like fibrils. Nature 435, 773–778.10.1038/nature03680Google ScholarPubMed
Nicolai, T and Durand, D (2013) Controlled food protein aggregation for new functionality. Current Opinion in Colloid & Interface Science 18, 249–256.10.1016/j.cocis.2013.03.001Google Scholar
Nicolai, T, Britten, M and Schmitt, C (2011) β-Lactoglobulin and WPI aggregates: formation, structure and applications. Food Hydrocolloids 25, 1945–1962.10.1016/j.foodhyd.2011.02.006Google Scholar
Oboroceanu, D, Wang, L and Brodkorb, A (2010) Characterization of β-lactoglobulin fibrillar assembly using atomic force microscopy, polyacrylamide gel electrophoresis, and in situ Fourier transform infrared spectroscopy. Journal of Agricultural and Food Chemistry 58, 3667–3673.10.1021/jf9042908Google ScholarPubMed
Pan, YX, Liu, CJ, Zhang, S, Yu, Y and Dong, M (2012) 2D-oriented self-assembly of peptides induced by hydrated electrons. Chemistry 18, 14614–14617.Google ScholarPubMed
Paparcone, R, Keten, S and Buehler, MJ (2010) Atomistic simulation of nanomechanical properties of Alzheimer's Aβ(1–40) amyloid fibrils under compressive and tensile loading. Journal of Biomechanics 43, 1196–1201.10.1016/j.jbiomech.2009.11.026Google ScholarPubMed
Perez, AA, Carrara, CR, Sánchez, CC, Santiago, LG and Patino, JMR (2010) Interfacial and foaming characteristics of milk whey protein and polysaccharide mixed systems. AIChE Journal 56, 1107–1117.Google Scholar
Pérez-Gago, MB, Nadaud, P and Krochta, JM (1999) Water vapor permeability, solubility, and tensile properties of heat-denatured versus native whey protein films. Journal of Food Science 64, 1034–1037.Google Scholar
Pilkington, SM, Roberts, SJ, Meade, SJ and Gerrard, JA (2010) Amyloid fibrils as a nanoscaffold for enzyme immobilization. Biotechnology Progress 26, 93–100.Google ScholarPubMed
Ramos, OL, Pereira, RN, Martins, A, Rodrigues, R, Fucinos, C, Teixeira, JA, Pastrana, L, Malcata, FX and Vicente, AA (2017) Design of whey protein nanostructures for incorporation and release of nutraceutical compounds in food. Critical Reviews in Food Science and Nutrition 57, 1377–1393.Google ScholarPubMed
Rao, SP, Meade, SJ, Healy, JP, Sutton, KH, Larsen, NG, Staiger, MP and Gerrard, JA (2012) Amyloid fibrils as functionalizable components of nanocomposite materials. Biotechnology Progress 28, 248–256.Google ScholarPubMed
Rhim, JW, Gennadios, A, Handa, A, Weller, CL and Hanna, MA (2000) Solubility, tensile, and color properties of modified soy protein isolate films. Journal of Agricultural and Food Chemistry 48, 4937–4941.10.1021/jf0005418Google ScholarPubMed
Schmid, M (2013) Properties of cast films made from different ratios of whey protein isolate, hydrolysed whey protein isolate and glycerol. Materials (Basel) 6, 3254–3269.10.3390/ma6083254Google ScholarPubMed
Schokker, EP, Singh, H, Pinder, DN and Creamer, LK (2000) Heat-induced aggregation of β-lactoglobulin AB at pH 2.5 as influenced by ionic strength and protein concentration. International Dairy Journal 10, 233–240.10.1016/S0958-6946(00)00047-9Google Scholar
Sukyai, P, Anongjanya, P, Bunyahwuthakul, N, Kongsin, K, Harnkarnsujarit, N, Sukatta, U, Sothornvit, R and Chollakup, R (2018) Effect of cellulose nanocrystals from sugarcane bagasse on whey protein isolate-based films. Food Research International 107, 528–535.Google ScholarPubMed
van der Linden, E and Venema, P (2007) Self-assembly and aggregation of proteins. Current Opinion in Colloid & Interface Science 12, 158–165.10.1016/j.cocis.2007.07.010Google Scholar
Wang, D, Ha, Y, Gu, J, Li, Q, Zhang, L and Yang, P (2016) Nanofilms: 2D protein supramolecular nanofilm with exceptionally large area and emergent functions. Advanced Materials 28, 7413–7413.Google ScholarPubMed
Xu, Z and Buehler, MJ (2010) Mechanical energy transfer and dissipation in fibrous beta-sheet-rich proteins. Physical Review E Statistical Nonlinear & Soft Matter Physics 81, 061910.Google ScholarPubMed
Xu, HH, Wang, J, Dong, SR, Cheng, W, Kong, BH and Tan, JY (2016) Acid-responsive properties of fibrils from heat-induced whey protein concentrate. Journal of Dairy Science 99, 6052–6060.10.3168/jds.2015-10823Google ScholarPubMed