Abstract
Bovine α-lactalbumin (α-LA) is a small (MW 14,178) globular whey protein with good nutritional and functional properties. Its increased availability as a purified protein has made easier the study of the effects of different processing treatments on its structural and techno-functional properties. The consumer demand for fresh foods with longer shelf-life and good sensory qualities led to extensive research in the field of the so-called nonthermal technologies to inactivate microorganisms and enzymes. However, these technologies have also acquired great importance in the field of modification and improvement of structural, physicochemical, and techno-functional properties of food proteins. In this review, the effects of some nonthermal processes (high hydrostatic pressure, pulsed electric fields, high-intensity ultrasound, ultraviolet light, and atmospheric pressure cold plasma) on the properties of α-LA are examined, and the research needs in this field are indicated.
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References
Farrell HM Jr, Jiménez-Flores R, Bleck GT, Brown EM, Butler JE, Creamer LK, Hicks CL, Hollar CM, Ng-Kwai-Hang KF, Swaisgood HE (2004) Nomenclature of the proteins of cows’ milk—sixth revision. J Dairy Sci 87:1641–1674
Layman DK, Lönnerdal B, Fernstrom JD (2018) Applications for α-lactalbumin in human nutrition. Nutr Revs 76:444–460
Velusamy V, Palaniappan L (2011) Compositional analysis of α-lactalbumin. Am J Biochem Molec Biol 1(2):106–120
Permyakov EA (2020) α-Lactalbumin, amazing calcium-binding protein. Biomolecules 10:1210
Kuwajima K (1996) The molten globule state of α-lactalbumin. FASEB J 10:102–109
Reyes-Portillo KA, Quintero-Lira A, Piloni-Martini J, Fajardo-Espinoza FS, Hernández-Sánchez H, Soto-Simentel S (2021) Using BAMLET complex in a functional spreadable cheese elaborated with bovine colostrum. J Food Sci Technol 58(9):3465–3472
Pellegrini A, Thomas U, Bramaz N, Hunziker P, von Fellenberg R (1999) Isolation and identification of three bactericidal domains in the bovine α-lactalbumin molecule. Biochim Biophys Acta 1426:439–448
Stӑnciuc N, Râpeanu G, Bahrim G, Aprodu I (2012) pH and heat-induced structural changes of bovine apo-α-lactalbumin. Food Chem 131:956–963
Stӑnciuc N, Râpeanu G (2010) An overview of bovine α-lactalbumin structure and functionality. Ann Univ Dunarea de Jos of Galati Fasc VI Food Technol 34(2):82–93
Kamau SM, Cheison SC, Chen W, Liu X-M, Lu R-R (2010) Alpha-lactalbumin: its production technologies and bioactive peptides. Compr Rev Food Sci Food Saf 9:197–212
Hendrix T, Griko YV, Privalov PL (2000) A calorimetric study of the influence of calcium on the stability of bovine α-lactalbumin. Biophys Chem 84:27–34
Wehbi Z, Pérez MD, Sánchez L, Pocovi C, Barbana C, Calvo M (2005) Effect of heat treatment on denaturation of bovine α-lactalbumin: determination of kinetic and thermodynamic parameters. J Agric Food Chem 53:9730–9736
Chaplin LC, Lyster RL (1986) Irreversible heat denaturation of bovine α-lactalbumin. J Dairy Res 53:249–258
Haller N, Kulozik U (2020) Continuous centrifugal separation of selectively precipitated α-lactalbumin. Int Dairy J 101:104566
Clark JP (2009) Case studies in food engineering. Springer Science+Business Media, LLC, New York, pp 129 – 145.
Barbosa-Cánovas GV, Donsi F, Yildiz S, Candoğan K, Pokhrel PR, Guadarrama-Lezama AY (2022) Nonthermal processing technologies for stabilization and enhancement of bioactive compounds in foods. Food Eng Revs 14:63–99
Jadhav HB, Annapure US, Deshmukh RR (2021) Non-thermal technologies for food processing. Front Nutr 8:657090
Jambrak AR (2021) Sustainable nonthermal technologies in extraction, stabilization and application of bioactive compounds. Int J Food Sci Technol 56:4821–4822
Guimãraes JT, Silva EK, Freitas MQ, Meireles MAA, Cruz AG (2018) Non-thermal emerging technologies and their effects on the functional properties of dairy products. Curr Opin Food Sci 22:62–66
Pérez-Andrés JM, Álvarez C, Cullen PJ, Tiwari BK (2019) Effect of cold plasma on the techno-functional properties of animal protein food ingredients. Innovative Food Sci Emerg Technol 58:102205
Huppertz T, Kelly AL, Fox PF (2002) Effects of high pressure on constituents and properties of milk. Int Dairy J 12:561–572
Lee W, Clark S, Swanson BG (2006) Functional properties of high hydrostatic pressure-treated whey protein. J Food Proc Preserv 30:488–501
Lim SY, Swanson BG, Clark S (2007) High hydrostatic pressure modification of whey protein concentrate for improved functional properties. J Dairy Sci 91:1299–1307
Kobashigura Y, Sakurai M, Nitta K (1999) Effect of hydrostatic pressure on unfolding of α-lactalbumin: volumetric equivalence of the molten globule and unfolded state. Protein Sci 8:2765–2772
Jegouic M, Grinberg VY, Guingant A, Haertlé T (1996) Thiol-induced oligomerization of α-lactalbumin at high pressure. J Protein Chem 15(6):501–509
Ahmed J, Ramaswamy HS (2003) Effect of hydrostatic pressure on rheological characteristics of α-lactalbumin. Aust J Dairy Technol 58(3):233–237
Huppertz T, Fox PF, Kelly AL (2004) High pressure-induced denaturation of α-lactalbumin and β-lactoglobulin in bovine milk and whey: a possible mechanism. J Dairy Res 71(4):489–495
He JS, Mu TH, Guo X, Zhu S, Azuma N (2013) Comparison of the gel-forming ability and gel properties of α-lactalbumin, lysozyme and myoglobin in the presence of β-lactoglobulin under high pressure. Food Hydrocolloids 33:415–424
Rodiles-López JO, Arroyo-Maya IJ, Jaramillo-Flores ME, Gutiérrez-López GF, Hernández-Arana A, Barbosa-Cánovas GV, Niranjan K, Hernández-Sánchez H (2010) Effects of high hydrostatic pressure on the structure of bovine α-lactalbumin. J Dairy Sci 93:1420–1428
Rodiles-López JO, Jaramillo-Flores ME, Gutiérrez-López GF, Hernández-Arana A, Fosado-Quiroz RE, Barbosa-Cánovas GV, Hernández-Sánchez H (2008) Effect of hydrostatic pressure on bovine α-lactalbumin functional properties. J Food Eng 87:363–370
Arroyo-Maya IJ, Rodiles-López JO, Cornejo-Mazón M, Gutiérrez-López GF, Hernández-Arana A, Toledo-Núñez C, Barbosa-Cánovas GV, Flores-Flores JO, Hernández-Sánchez H (2012) Effect of different treatments on the ability of α-lactalbumin to form nanoparticles. J Dairy Sci 95:6204–6214
Qayum A, Chen W, Ma L, Li T, Hussain M, Bilawal A (2020) Characterization and comparison of α-lactalbumin pre- and post-emulsion. J Food Eng 269:109743
Zou H, Xu Z, Zhao L, Wang Y, Liao X (2019) Effects of high pressure processing on the interactions of α-lactalbumin and pelargonidin-3-glucoside. Food Chem 285:22–30
Marciniak A, Suwal S, Touhami S, Chamberland J, Pouliot Y, Doyen A (2020) Production of highly purified fractions of α-lactalbumin and β-lactoglobulin from cheese whey using high hydrostatic pressure. J Dairy Sci 103:7939–7950
Touhami S, Chamberland J, Perreault V, Suwal S, Marciniak A, Pouliot Y, Doyen A (2021) Coupling high hydrostatic pressure and ultrafiltration for fractionation of alpha-lactalbumin from skim milk. Sep Sci Technol 56(6):1102–1111
Vanga SK, Wang J, Jayaram S, Raghavan V (2021) Effect of pulsed electric fields and ultrasound processing on proteins and enzymes: a review. Processes 9:722
Zhao W, Tang Y, Lu L, Chen X, Li C (2014) Review: pulsed electric fields processing of protein-based foods. Food Bioprocess Technol 7:114–125
Xiang BY, Ngadi MO, Ochoa-Martínez LA, Simpson MV (2011) Pulsed electric field-induced structural modification of whey protein isolate. Food Bioprocess Technol 4:1341–1348
Axelrod R, Beyrer M, Mathys A (2022) Impact of the electric field intensity and treatment time on whey protein aggregate formation. J Dairy Sci 105:6589–6600
Sui Q, Roginski H, Williams RPW, Versteeg C, Wan J (2011) Effect of pulsed electric field and thermal treatment on the physicochemical and functional properties of whey protein isolate. Int Dairy J 21:206–213
Robles-López MR, Robles de la Torre RR, Camarillo-Cadena M, Hernández-Arana A, Welti-Chanes JS, Hernández-Sánchez H (2012) Effect of pulsed electric fields on the structure of α-lactalbumin. Rev Mex Ing Quim 11(3):373–382
Xu FY, Wen QH, Wang R, Li J, Chen BR, Zeng XA (2021) Enhanced synthesis of succinylated whey protein isolate by pulsed electric field pretreatment. Food Chem 363:129892
Bhaskaracharya RK, Kentish S, Ashokkumar M (2009) Selected applications of ultrasonics in food processing. Food Eng Rev 1:31–49
Ortega-Rivas E (2012) Non-thermal food engineering operations. Springer, New York
Povey MJW (1989) Ultrasonics in food engineering part II. Applications J Food Eng 9:1–20
Wang Q, Tolkach A, Kulozik U (2006) Quantitative assessment of thermal denaturation of bovine α-lactalbumin via low-intensity ultrasound, HPLC, and DSC. J Agric Food Chem 54:6501–6506
Velusamy V, Palaniappan L (2016) Effect of pH and glucose on the stability of α-lactalbumin. Food Biophys 11:108–115
Kavitha K, Palaniappan L (2019) Hydrophobicity character of α-lactalbumin nanoparticles: an ultrasonic study. Sci Technol J 7(2):95–101
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(5):951–957
Hoseini SM, Housaindokht MR, Izadyar M, Izadi-Najafabadi R (2017) Effect of ultrasound on the chemical and thermal stability of alpha-lactalbumin. J Acoust Eng Soc Iran 5(1):56–63
Chandrapala J, Zisu B, Kentish M, Ashokkumar M (2012) The effects of high-intensity ultrasound on the structural and functional properties of α-lactalbumin, β-lactoglobulin and their mixtures. Food Res Int 48:940–943
Jambrak AR, Mason TJ, Lelas V, Krešić G (2010) Ultrasonic effect on physicochemical and functional properties of α-lactalbumin. LWT Food Sci Technol 43:254–262
Qayum A, Hussain M, Li M, Li J, Shi R, Li T, Anwar A, Ahmed Z, Hou J, Jiang Z (2021) Gelling, microstructure and water-holding capacity properties of alpha-lactalbumin emulsion gel: impact of combined ultrasound pretreatment and laccase cross-linking. Food Hydrocolloids 110:106122
Koutchma T (2008) UV light for processing foods. Ozone Sci Eng 30:1–6
Gómez-López VM, Jubinville E, Rodríguez-López MI, Trudel-Ferland M, Bouchard S, Jean J (2021) Inactivation of foodborne viruses by UV light: a review. Foods 10:3141
Pattison DI, Rahmanto AS, Davies MJ (2012) Photo-oxidation of proteins. Photochem Photobiol Sci 11:38–53
Dalsgaard TK, Otzen D, Nielsen JH, Larsen LB (2007) Changes in structures of milk proteins upon photo-oxidation. J Agric Food Chem 55:10968–10976
Zhao Z, Engholm-Keller K, Poojary MM, Boelt SG, Rogowska-Wrzesinska A, Skibsted LH, Davies MJ, Lund MN (2020) Generation of aggregates of α-lactalbumin by UV-B light exposure. J Agric Food Chem 68:6701–6714
Sharma S, Singh RK (2020) Cold plasma treatment of dairy proteins in relation to functionality enhancement. Trends Food Sci Technol 102:30–36
Segat A, Misra NN, Cullen PJ, Innocente N (2015) Atmospheric pressure cold plasma (ACP) treatment of whey protein isolate model solution. Innovative Food Sci Emerg Technol 29:247–254
Ng SW, Lu P, Rulikowska A, Boehm D, O’Neill G (2021) The effect of atmospheric cold plasma treatment on the antigenic properties of bovine milk casein and whey proteins. Food Chem 342:128283
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The author received financial support from the Instituto Politécnico Nacional (Grants 20120690 and 20210460).
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Hernández-Sánchez, H. Effect of Nonthermal Processing on the Structural and Techno-Functional Properties of Bovine α-Lactalbumin. Food Eng Rev 15, 187–195 (2023). https://doi.org/10.1007/s12393-023-09340-8
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DOI: https://doi.org/10.1007/s12393-023-09340-8