Comparison of interaction, structure, and cell proliferation of α-lactalbumin-safflower yellow complex induced by microwave heating or conventional heating.
cell proliferation
microwave heating
safflower yellow
structure
water bath heating
α-lactalbumin
Journal
Journal of the science of food and agriculture
ISSN: 1097-0010
Titre abrégé: J Sci Food Agric
Pays: England
ID NLM: 0376334
Informations de publication
Date de publication:
15 Mar 2023
15 Mar 2023
Historique:
revised:
03
11
2022
received:
04
07
2022
accepted:
05
11
2022
pubmed:
9
11
2022
medline:
4
2
2023
entrez:
8
11
2022
Statut:
ppublish
Résumé
The protein-polyphenol interaction mechanism has always been a research hotspot, but their interaction is affected by heat treatment, which is widely applied in food processing. Moreover, the effects of microwave or water-bath heating on the protein-polyphenol interaction mechanism have been not clarified. The pasteurization condition (65 °C, 30 min) was selected to compare the effects of microwave or water bath on binding behavior, structure, and cell proliferation between α-lactalbumin (α-LA) and safflower yellow (SY), thus providing a guide for the selection of functional dairy processing conditions. Microwave heat treatment of α-LA-SY resulted in stronger fluorescence quenching than that of conventional heat treatment. Moreover, the binding constant K It was demonstrated that microwave heating promoted interaction between α-LA and SY more than water bath heating did. Microwave heat treatment was a safe and effective way to enhance the binding affinity of α-LA to SY, being a potential application in food industry. © 2022 Society of Chemical Industry.
Sections du résumé
BACKGROUND
BACKGROUND
The protein-polyphenol interaction mechanism has always been a research hotspot, but their interaction is affected by heat treatment, which is widely applied in food processing. Moreover, the effects of microwave or water-bath heating on the protein-polyphenol interaction mechanism have been not clarified. The pasteurization condition (65 °C, 30 min) was selected to compare the effects of microwave or water bath on binding behavior, structure, and cell proliferation between α-lactalbumin (α-LA) and safflower yellow (SY), thus providing a guide for the selection of functional dairy processing conditions.
RESULTS
RESULTS
Microwave heat treatment of α-LA-SY resulted in stronger fluorescence quenching than that of conventional heat treatment. Moreover, the binding constant K
CONCLUSION
CONCLUSIONS
It was demonstrated that microwave heating promoted interaction between α-LA and SY more than water bath heating did. Microwave heat treatment was a safe and effective way to enhance the binding affinity of α-LA to SY, being a potential application in food industry. © 2022 Society of Chemical Industry.
Substances chimiques
Lactalbumin
9013-90-5
safflower yellow
1401-20-3
Transcription Factors
0
Water
059QF0KO0R
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
1846-1855Subventions
Organisme : National Natural Science Foundation of China
ID : 32172164
Organisme : Open Project Program of State Key Laboratory of Dairy Biotechnology
ID : SKLDB2021-005
Informations de copyright
© 2022 Society of Chemical Industry.
Références
Buggy AK, Mcmanus JJ, Brodkorb A, Carthy NM and Fenelon MA, Stabilising effect of α-lactalbumin on concentrated infant milk formula emulsions heat treated pre- or post-homogenisation. Dairy Sci Technol 96:845-859 (2017).
Yuan X, Li X, Zhang Z, Mu Z, Gao L and Jiang Z, Effect of ultrasound on structure and functional properties of laccase-catalyzed α-lactalbumin. J Food Eng 223:116-123 (2018).
Li T, Hu P, Dai T, Li P, Ye X, Chen J et al., Comparing the binding interaction between β-lactoglobulin and flavonoids with different structure by multi-spectroscopy analysis and molecular docking. Spectrochim Acta A 201:197-206 (2018).
Wei Z, Wei Y, Rui F, Fang Y and Gao Y, Evaluation of structural and functional properties of protein-EGCG complexes and their ability of stabilizing a model β-carotene emulsion. Food Hydrocolloids 45:337-350 (2015).
Tang L, Gao X, Jia J and Hao M, Comparison of binding interaction between beta-lactoglobulin and three common polyphenols using multi-spectroscopy and modeling methods. Food Chem 228:143-151 (2017).
Mattia CD, Sacchetti G, Mastrocola D, Sarker DK and Pittia P, Surface properties of phenolic compounds and their influence on the dispersion degree and oxidative stability of olive oil O/W emulsions. Food Hydrocolloids 24:652-658 (2010).
Bourassa P, Coté R, Hutchandani S, Samson G and Tajmir-Riahi H-A, The effect of milk alpha-casein on the antioxidant activity of tea polyphenols. J Photochem Photobiol B 128:43-49 (2013).
Cui Z, Kong X, Chen Y, Zhang C and Hua Y, Effects of rutin incorporation on the physical and oxidative stability of soy protein-stabilized emulsions. Food Hydrocolloids 41:1-9 (2014).
Carocho M and Ferreira ICFR, A review on antioxidants, prooxidants and related controversy: natural and synthetic compounds, screening and analysis methodologies and future perspectives. Food Chem Toxicol 51:15-25 (2013).
Jia Y and Jiang H, Dyeing of mulberry silk using natural safflower yellow pigment. Appl Mech Mater 670-671:197-200 (2014).
Mohammadi F and Moeeni M, Analysis of binding interaction of genistein and kaempferol with bovine α-lactalbumin. J Funct Foods 12:458-467 (2015).
Capanoglu E, Altay F and Ozdal T, A review on protein-phenolic interactions and associated changes. Food Res Int 51:954-970 (2013).
Shi R, Chen W, Pan F, Zhao P, He Y, Yu R et al., Characterization of the binding behavior, structure and foaming properties of bovine α-lactalbumin combined with saponin by the multi-spectroscopic and silico approaches. Food Hydrocolloids 124:107259 (2022).
Kulmyrzaev AA, Levieux D and Dufour É, Front-face fluorescence spectroscopy allows the characterization of mild heat treatments applied to milk. Relations with the denaturation of milk proteins. J Agric Food Chem 53:502-507 (2005).
Moon JK and Shibamoto T, Formation of volatile chemicals from thermal degradation of less volatile coffee components: quinic acid, caffeic acid, and chlorogenic acid. J Agric Food Chem 58:5465-5470 (2010).
Rawel HM, Meidtner K and Kroll J, Binding of selected phenolic compounds to proteins. J Agric Food Chem 53:4228-4235 (2005).
Ren C, Xiong W, Peng D, Pei Y and Jing Z, Effects of thermal sterilization on soy protein isolate/polyphenol complexes: aspects of structure, in vitro digestibility and antioxidant activity. Food Res Int 112:284-290 (2018).
Adulvitayakorn S, Azhari S and Hasan H, The effects of conventional thermal, microwave heating, and thermosonication treatments on the quality of sugarcane juice. J Food Process Preserv 44:e14322 (2020).
Bhattacharya M, Punathil L and Basak T, A theoretical analysis on the effect of containers on the microwave heating of materials. Int Commun Heat Mass Transfer 82:145-153 (2017).
Rodríguez-López MI, Mercader-Ros MT, López-Miranda S, Pellicer JA, Pérez-Garrido A, Pérez-Sánchez H et al., Thorough characterization and stability of HP-β-cyclodextrin thymol inclusion complexes prepared by microwave technology: a required approach to a successful application in food industry. J Sci Food Agric 99:1322-1333 (2018).
Duan D, Tu Z, Wang H and Sha X, A comparative analysis of the antigenicity and the major components formed from the glucose/ovalbumin model system under microwave irradiation and conventional heating. J Food Process Preserv 42:e13818 (2018).
Chen W, Li J, Ma Y, Shi R, Yu H, Gantumur M-A et al., Binding interaction and stability of alpha-lactalbumin and retinol: effects of pre- or post-acidification. Food Hydrocolloids 135:108140 (2023).
Beigoli S, Rad AS, Askari A, Darban RA and Chamani J, Isothermal titration calorimetry and stopped flow circular dichroism investigations of the interaction between lomefloxacin and human serum albumin in the presence of amino acids. J Biomol Struct Dyn 37:2265-2282 (2019).
Li M, Li J, Huang Y, Gao Z, Jiang Z and Mu Z, Insight into comparison of binding interactions and biological activities of whey protein isolate exposed prior to two structurally different sterols. Food Chem 405:134827 (2023).
Li J, Liu Y, Li T, Gantumur M-A, Qayum A, Bilawal A et al., Non-covalent interaction and digestive characteristics between α-lactalbumin and safflower yellow: impacts of microwave heating temperature. LWT Food Sci Technol 159:113206 (2022).
Nooshin A, Vahid S, Mohammad RS and Jamshidkhan C, Investigation of the interaction between human serum albumin and two drugs as binary and ternary systems. Eur J Drug Metab Pharmacokinet 41:705-721 (2016).
Manna A and Chakravorti S, Role of block copolymer-micelle nanocomposites in dye-bovine serum albumin binding: a combined experimental and molecular docking study. Mol Biosyst 9:246-257 (2013).
Li J, Huang Y, Zhang W, Bilawal A, Sukhbaatar N, Tsembeltsogt B et al., Insight into binding mechanism between three whey proteins and mogroside V by multi-spectroscopic and silico methods: impacts on structure and foaming properties. Food Hydrocolloids 135:108207 (2023).
Li J, Fu J, Ma Y, He Y, Fu R and Qayum A, Low temperature extrusion promotes transglutaminase cross-linking of whey protein isolate and enhances its emulsifying properties and water holding capacity. Food Hydrocolloids 125:107410 (2022).
Zhu H, Wang X, Pan H, Dai Y, Li N, Wang L et al., The mechanism by which safflower yellow decreases body fat mass and improves insulin sensitivity in HFD-induced obese mice. Front Pharmacol 7:127 (2016).
Chandrapala J, Zisu B, Palmer M, Kentish S and Ashokkumar M, Effects of ultrasound on the thermal and structural characteristics of proteins in reconstituted whey protein concentrate. Ultrason Sonochem 8:951-957 (2010).
Gomaa AI, An investigation of effects of microwave treatment on the structure, enzymatic hydrolysis, and nutraceutical properties of β-lactoglobulin. J Food Eng 114:183-191 (2010).
Jacob J, Chia LHL and Boey FYC, Thermal and non-thermal interaction of microwave radiation with materials. J Mater Sci 30:5321-5327 (1995).
Al-Jundi AN, Elucidation of nonthermal effects of microwave irradiation on the unfolding pathways of β-lactoglobulin and hemoglobin MSc thesis. McGill University, Montreal, Canada (2004).
Moeiniafshari AA, Zarrabi A and Bordbar AK, Exploring the interaction of naringenin with bovine beta-casein nanoparticles using spectroscopy. Food Hydrocolloids 51:1-6 (2015).
Dai T, Chen J, McClements DJ, Hu P, Ye X, Liu C et al., Protein-polyphenol interactions enhance the antioxidant capacity of phenolics: analysis of rice glutelin-procyanidin dimer interactions. Food Funct 10:765-774 (2019).
Gomaa AI, Nsonzi F, Sedman J and Ismail AA, Enhanced unfolding of bovine β-lactoglobulin structure using microwave treatment: a multi-spectroscopic study. Food Biophys 11:370-379 (2016).
Chamani J, Moosavi-Movahedi AA and Hakimelahi GH, Structural changes in β-lactoglobulin by conjugation with three different kinds of carboxymethyl cyclodextrins. Thermochim Acta 432:106-111 (2005).
Zhang L, Xu L, Tu Z, Wang H, Luo J and Ma T, Mechanisms of isoquercitrin attenuates ovalbumin glycation: investigation by spectroscopy, spectrometry and molecular docking. Food Chem 309:125667 (2020).
Hosseinzadeh M, Nikjoo S, Zare N, Delavar D, Beigoli S and Chamani J, Characterization of the structural changes of human serum albumin upon interaction with single-walled and multi-walled carbon nanotubes: spectroscopic and molecular modeling approaches. Res Chem Intermed 45:401-423 (2019).
Hao S, Chen C, Zhao S, Ge F, Liu D, Shi D et al., Interaction of gallic acid with trypsin analyzed by spectroscopy. J Food Drug Anal 23:234-242 (2015).
Wang Y, Zhang H, Zhang G, Tao W and Tang S, Interaction of the flavonoid hesperidin with bovine serum albumin: a fluorescence quenching study. J Lumin 126:211-218 (2007).
Bi S, Pang B, Wang T, Zhao T and Yu W, Investigation on the interactions of clenbuterol to bovine serum albumin and lysozyme by molecular fluorescence technique. Spectrochim Acta A 120:456-461 (2014).
Dickinson E, Milk protein interfacial layers and the relationship to emulsion stability and rheology. Colloid Surf 20:197-210 (2001).
Gantumur M, Sukhbaatar N, Shi R, Hu J, Bilawal A, Qayum A et al., Structural, functional, and physicochemical characterization of fermented whey protein concentrates recovered from various fermented-distilled whey. Food Hydrocolloids 135:108130 (2023).
de la Fuente MA, Hemar Y and Singh H, Influence of κ-carrageenan on the aggregation behaviour of proteins in heated whey protein isolate solutions. Food Chem 86:1-9 (2004).
Gantumur M, Hussain M, Li J, Hui M, Bai X, Sukhbaatar N et al., Modification of fermented whey protein concentrates: Impact of sequential ultrasound and TGase cross-linking. Food Res Int 163:112158 (2023).
Li X, Shi J, Scanlon M, Sophia J and Lu J, Effects of pretreatments on physicochemical and structural properties of proteins isolated from canola seeds after oil extraction by supercritical-CO2 process. LWT Food Sci Technol 137:110415 (2020).
Harnly JM, Bhagwat S and Lin L, Profiling methods for the determination of phenolic compounds in foods and dietary supplements. Anal Bioanal Chem 389:47-61 (2007).
Wang W, Wang M, Xu C, Liu Z, Gu L, Ma J et al., Effects of soybean oil body as a milk fat substitute on ice cream: physicochemical, sensory and digestive properties. Foods 11:1504 (2022).
Iijima K, Yoshizumi M, Hashimoto M, Kim S, Akishita M, Ako J et al., Inhibition of vascular smooth muscle cell proliferation by red wine polyphenols is associated with downregulation of cyclin A gene expression. Atherosclerosis 151:318 (2000).