메뉴 건너뛰기




Volumn 548, Issue , 2019, Pages 88-99

Water-in-oil Pickering emulsions stabilized by an interfacial complex of water-insoluble polyphenol crystals and protein

Author keywords

Biocompatible particles; Curcumin; Interfacial complexation; Interfacial shear viscosity; Pickering stabilizers; Quercetin; Water in oil emulsions; Whey protein

Indexed keywords

ALKALINITY; BIOCOMPATIBILITY; COMPLEXATION; DROPS; EMULSIONS; FLAVONOIDS; HYDROGEN BONDS; IONIC STRENGTH; PHENOLS; PROTEINS; SHEAR VISCOSITY; STABILIZATION; VISCOSITY MEASUREMENT;

EID: 85064259860     PISSN: 00219797     EISSN: 10957103     Source Type: Journal    
DOI: 10.1016/j.jcis.2019.04.010     Document Type: Article
Times cited : (128)

References (41)
  • 1
    • 80052829110 scopus 로고    scopus 로고
    • Fat crystals and water-in-oil emulsion stability
    • Ghosh, S., Rousseau, D., Fat crystals and water-in-oil emulsion stability. Curr. Opin. Colloid Interface Sci. 16 (2011), 421–431.
    • (2011) Curr. Opin. Colloid Interface Sci. , vol.16 , pp. 421-431
    • Ghosh, S.1    Rousseau, D.2
  • 2
    • 75849137203 scopus 로고    scopus 로고
    • Food emulsions and foams: stabilization by particles
    • Dickinson, E., Food emulsions and foams: stabilization by particles. Curr. Opin. Colloid Interface Sci. 15 (2010), 40–49.
    • (2010) Curr. Opin. Colloid Interface Sci. , vol.15 , pp. 40-49
    • Dickinson, E.1
  • 3
    • 85052320701 scopus 로고    scopus 로고
    • Water-in-oil Pickering emulsions stabilized by water-insoluble polyphenol crystals
    • Zembyla, M., Murray, B.S., Sarkar, A., Water-in-oil Pickering emulsions stabilized by water-insoluble polyphenol crystals. Langmuir 34 (2018), 10001–10011.
    • (2018) Langmuir , vol.34 , pp. 10001-10011
    • Zembyla, M.1    Murray, B.S.2    Sarkar, A.3
  • 4
    • 0033562179 scopus 로고    scopus 로고
    • Effect of aqueous phase composition on the properties of a silica-stabilized W/O emulsion
    • Midmore, B.R., Effect of aqueous phase composition on the properties of a silica-stabilized W/O emulsion. J. Colloid Interface Sci. 213 (1999), 352–359.
    • (1999) J. Colloid Interface Sci. , vol.213 , pp. 352-359
    • Midmore, B.R.1
  • 5
    • 84865211594 scopus 로고    scopus 로고
    • Quiescent water-in-oil Pickering emulsions as a route toward healthier fruit juice infused chocolate confectionary
    • Skelhon, T.S., Grossiord, N., Morgan, A.R., Bon, S.A.F., Quiescent water-in-oil Pickering emulsions as a route toward healthier fruit juice infused chocolate confectionary. J. Mater. Chem. 22 (2012), 19289–19295.
    • (2012) J. Mater. Chem. , vol.22 , pp. 19289-19295
    • Skelhon, T.S.1    Grossiord, N.2    Morgan, A.R.3    Bon, S.A.F.4
  • 6
    • 85047388921 scopus 로고    scopus 로고
    • Stabilization of oil continuous emulsions with colloidal particles from water-insoluble plant proteins
    • Rutkevičius, M., Allred, S., Velev, O.D., Velikov, K.P., Stabilization of oil continuous emulsions with colloidal particles from water-insoluble plant proteins. Food Hydrocolloids 82 (2018), 89–95.
    • (2018) Food Hydrocolloids , vol.82 , pp. 89-95
    • Rutkevičius, M.1    Allred, S.2    Velev, O.D.3    Velikov, K.P.4
  • 7
    • 84961864618 scopus 로고    scopus 로고
    • A comparative study on the capacity of a range of food-grade particles to form stable O/W and W/O Pickering emulsions
    • Duffus, L.J., Norton, J.E., Smith, P., Norton, I.T., Spyropoulos, F., A comparative study on the capacity of a range of food-grade particles to form stable O/W and W/O Pickering emulsions. J. Colloid Interface Sci. 473 (2016), 9–21.
    • (2016) J. Colloid Interface Sci. , vol.473 , pp. 9-21
    • Duffus, L.J.1    Norton, J.E.2    Smith, P.3    Norton, I.T.4    Spyropoulos, F.5
  • 8
    • 85065598647 scopus 로고    scopus 로고
    • Emulsions in foods
    • Murray, B.S., Zembyla, M., Sarkar, A., Emulsions in foods. WO, 2019/008059, 2019, Al.
    • (2019) WO , vol.2019/008059 , pp. Al
    • Murray, B.S.1    Zembyla, M.2    Sarkar, A.3
  • 10
    • 75849133338 scopus 로고    scopus 로고
    • Binding of curcumin and its long chain derivatives to the activator binding domain of novel protein kinase C
    • Majhi, A., Rahman, G.M., Panchal, S., Das, J., Binding of curcumin and its long chain derivatives to the activator binding domain of novel protein kinase C. Bioorg. Med. Chem. 18 (2010), 1591–1598.
    • (2010) Bioorg. Med. Chem. , vol.18 , pp. 1591-1598
    • Majhi, A.1    Rahman, G.M.2    Panchal, S.3    Das, J.4
  • 11
    • 85034650270 scopus 로고    scopus 로고
    • Recent advances in emulsion-based delivery approaches for curcumin: from encapsulation to bioaccessibility
    • Araiza-Calahorra, A., Akhtar, M., Sarkar, A., Recent advances in emulsion-based delivery approaches for curcumin: from encapsulation to bioaccessibility. Trends Food Sci. Technol. 71 (2018), 155–169.
    • (2018) Trends Food Sci. Technol. , vol.71 , pp. 155-169
    • Araiza-Calahorra, A.1    Akhtar, M.2    Sarkar, A.3
  • 12
    • 33745254486 scopus 로고    scopus 로고
    • Quercetin content in some food and herbal samples
    • Wach, A., Pyrzyńska, K., Biesaga, M., Quercetin content in some food and herbal samples. Food Chem. 100 (2007), 699–704.
    • (2007) Food Chem. , vol.100 , pp. 699-704
    • Wach, A.1    Pyrzyńska, K.2    Biesaga, M.3
  • 13
    • 0029610477 scopus 로고
    • Review of the biology of quercetin and related bioflavonoids
    • Formica, J., Regelson, W., Review of the biology of quercetin and related bioflavonoids. Food Chem. Toxicol. 33 (1995), 1061–1080.
    • (1995) Food Chem. Toxicol. , vol.33 , pp. 1061-1080
    • Formica, J.1    Regelson, W.2
  • 15
    • 0022637164 scopus 로고
    • The crystal and molecular structure of quercetin: a biologically active and naturally occurring flavonoid
    • Rossi, M., Rickles, L.F., Halpin, W.A., The crystal and molecular structure of quercetin: a biologically active and naturally occurring flavonoid. Bioorg. Chem. 14 (1986), 55–69.
    • (1986) Bioorg. Chem. , vol.14 , pp. 55-69
    • Rossi, M.1    Rickles, L.F.2    Halpin, W.A.3
  • 17
    • 84890940480 scopus 로고    scopus 로고
    • Nature and consequences of non-covalent interactions between flavonoids and macronutrients in foods
    • Bordenave, N., Hamaker, B.R., Ferruzzi, M.G., Nature and consequences of non-covalent interactions between flavonoids and macronutrients in foods. Food Funct. 5 (2014), 18–34.
    • (2014) Food Funct. , vol.5 , pp. 18-34
    • Bordenave, N.1    Hamaker, B.R.2    Ferruzzi, M.G.3
  • 19
    • 0242314936 scopus 로고    scopus 로고
    • Adsorption of whey protein isolate at the oil− water interface as a function of processing conditions: A rheokinetic study
    • Rodríguez-Patino, J.M., Rodríguez-Niño, M.R., Sánchez, C.C., Adsorption of whey protein isolate at the oil− water interface as a function of processing conditions: A rheokinetic study. J. Agric. Food Chem. 47 (1999), 2241–2248.
    • (1999) J. Agric. Food Chem. , vol.47 , pp. 2241-2248
    • Rodríguez-Patino, J.M.1    Rodríguez-Niño, M.R.2    Sánchez, C.C.3
  • 20
    • 0036867705 scopus 로고    scopus 로고
    • Interfacial rheology of food emulsifiers and proteins
    • Murray, B.S., Interfacial rheology of food emulsifiers and proteins. Curr. Opin. Colloid Interface Sci. 7 (2002), 426–431.
    • (2002) Curr. Opin. Colloid Interface Sci. , vol.7 , pp. 426-431
    • Murray, B.S.1
  • 21
    • 85021754430 scopus 로고    scopus 로고
    • Modulating in vitro gastric digestion of emulsions using composite whey protein-cellulose nanocrystal interfaces
    • Sarkar, A., Zhang, S., Murray, B., Russell, J.A., Boxal, S., Modulating in vitro gastric digestion of emulsions using composite whey protein-cellulose nanocrystal interfaces. Colloids Surf. B Biointerf. 158 (2017), 137–146.
    • (2017) Colloids Surf. B Biointerf. , vol.158 , pp. 137-146
    • Sarkar, A.1    Zhang, S.2    Murray, B.3    Russell, J.A.4    Boxal, S.5
  • 22
    • 20844447710 scopus 로고    scopus 로고
    • Interactions of whey proteins during heat treatment of oil-in-water emulsions formed with whey protein isolate and hydroxylated lecithin
    • Jiménez-Flores, R., Ye, A., Singh, H., Interactions of whey proteins during heat treatment of oil-in-water emulsions formed with whey protein isolate and hydroxylated lecithin. J. Agric. Food. Chem. 53 (2005), 4213–4219.
    • (2005) J. Agric. Food. Chem. , vol.53 , pp. 4213-4219
    • Jiménez-Flores, R.1    Ye, A.2    Singh, H.3
  • 23
    • 84956731608 scopus 로고    scopus 로고
    • Emulsions and Foams Stabilised by Milk Proteins. Advanced Dairy Chemistry
    • Springer
    • Sarkar, A., Singh, H., Emulsions and Foams Stabilised by Milk Proteins. Advanced Dairy Chemistry. 2016, Springer.
    • (2016)
    • Sarkar, A.1    Singh, H.2
  • 24
    • 85027932498 scopus 로고    scopus 로고
    • The effect of pH and temperature pre-treatments on the physicochemical and emulsifying properties of whey protein isolate
    • Lam, R.S., Nickerson, M.T., The effect of pH and temperature pre-treatments on the physicochemical and emulsifying properties of whey protein isolate. LWT-Food Sci. Technol. 60 (2015), 427–434.
    • (2015) LWT-Food Sci. Technol. , vol.60 , pp. 427-434
    • Lam, R.S.1    Nickerson, M.T.2
  • 25
    • 84884418339 scopus 로고    scopus 로고
    • Interfacial rheology and stability of air bubbles stabilized by mixtures of hydrophobin and β-casein
    • Burke, J., Cox, A., Petkov, J., Murray, B.S., Interfacial rheology and stability of air bubbles stabilized by mixtures of hydrophobin and β-casein. Food Hydrocolloids 34 (2014), 119–127.
    • (2014) Food Hydrocolloids , vol.34 , pp. 119-127
    • Burke, J.1    Cox, A.2    Petkov, J.3    Murray, B.S.4
  • 26
    • 0001084450 scopus 로고    scopus 로고
    • Interfacial rheology and the dynamic properties of adsorbed films of food proteins and surfactants
    • Murray, B.S., Dickinson, E., Interfacial rheology and the dynamic properties of adsorbed films of food proteins and surfactants. Food Sci. Technol. Int., Tokyo 2 (1996), 131–145.
    • (1996) Food Sci. Technol. Int., Tokyo , vol.2 , pp. 131-145
    • Murray, B.S.1    Dickinson, E.2
  • 27
    • 85014248384 scopus 로고    scopus 로고
    • Physical and chemical stability of curcumin in aqueous solutions and emulsions: impact of pH, temperature, and molecular environment
    • Kharat, M., Du, Z., Zhang, G., McClements, D.J., Physical and chemical stability of curcumin in aqueous solutions and emulsions: impact of pH, temperature, and molecular environment. J. Agric. Food. Chem. 65 (2017), 1525–1532.
    • (2017) J. Agric. Food. Chem. , vol.65 , pp. 1525-1532
    • Kharat, M.1    Du, Z.2    Zhang, G.3    McClements, D.J.4
  • 28
    • 85064268053 scopus 로고    scopus 로고
    • Chemical and technical assessment curcumin, 61st jecfa.
    • I. Stankovic, Chemical and technical assessment curcumin, 61st jecfa, 2004.
    • (2004)
    • Stankovic, I.1
  • 29
    • 85041485191 scopus 로고    scopus 로고
    • Assessment of interaction of vanillin with barley, pea and whey proteins: Binding properties and sensory characteristics
    • Houde, M., Khodaei, N., Karboune, S., Assessment of interaction of vanillin with barley, pea and whey proteins: Binding properties and sensory characteristics. LWT 91 (2018), 133–142.
    • (2018) LWT , vol.91 , pp. 133-142
    • Houde, M.1    Khodaei, N.2    Karboune, S.3
  • 30
    • 84888371883 scopus 로고    scopus 로고
    • Interaction of milk whey protein with common phenolic acids
    • Zhang, H., Yu, D., Sun, J., Guo, H., Ding, Q., Liu, R., Ren, F., Interaction of milk whey protein with common phenolic acids. J. Mol. Struct. 1058 (2014), 228–233.
    • (2014) J. Mol. Struct. , vol.1058 , pp. 228-233
    • Zhang, H.1    Yu, D.2    Sun, J.3    Guo, H.4    Ding, Q.5    Liu, R.6    Ren, F.7
  • 33
    • 0000453877 scopus 로고
    • Factors affecting molecular characteristics of whey protein gelation
    • Boye, J.I., Alli, I., Ismail, A.A., Gibbs, B.F., Konishi, Y., Factors affecting molecular characteristics of whey protein gelation. Int. Dairy J. 5 (1995), 337–353.
    • (1995) Int. Dairy J. , vol.5 , pp. 337-353
    • Boye, J.I.1    Alli, I.2    Ismail, A.A.3    Gibbs, B.F.4    Konishi, Y.5
  • 34
    • 84857382394 scopus 로고    scopus 로고
    • Interactions between polyphenols and macromolecules: quantification methods and mechanisms
    • le Bourvellec, C., Renard, C., Interactions between polyphenols and macromolecules: quantification methods and mechanisms. Crit. Rev. Food Sci. Nutr. 52 (2012), 213–248.
    • (2012) Crit. Rev. Food Sci. Nutr. , vol.52 , pp. 213-248
    • le Bourvellec, C.1    Renard, C.2
  • 35
    • 0000038821 scopus 로고
    • Characterization of haze-forming proteins of beer and their roles in chill haze formation
    • Asano, K., Shinagawa, K., Hashimoto, N., Characterization of haze-forming proteins of beer and their roles in chill haze formation. J. Am. Soc. Brew. Chem. 40 (1982), 147–154.
    • (1982) J. Am. Soc. Brew. Chem. , vol.40 , pp. 147-154
    • Asano, K.1    Shinagawa, K.2    Hashimoto, N.3
  • 37
    • 0019876875 scopus 로고
    • The specificity of proanthocyanidin-protein interactions
    • Hagerman, A.E., Butler, L.G., The specificity of proanthocyanidin-protein interactions. J. Biol. Chem. 256 (1981), 4494–4497.
    • (1981) J. Biol. Chem. , vol.256 , pp. 4494-4497
    • Hagerman, A.E.1    Butler, L.G.2
  • 38
    • 0030968136 scopus 로고    scopus 로고
    • Multiple interactions between polyphenols and a salivary proline-rich protein repeat result in complexation and precipitation
    • Baxter, N.J., Lilley, T.H., Haslam, E., Williamson, M.P., Multiple interactions between polyphenols and a salivary proline-rich protein repeat result in complexation and precipitation. Biochemistry 36 (1997), 5566–5577.
    • (1997) Biochemistry , vol.36 , pp. 5566-5577
    • Baxter, N.J.1    Lilley, T.H.2    Haslam, E.3    Williamson, M.P.4
  • 39
    • 0028069242 scopus 로고
    • Study of the interaction between salivary proline-rich proteins and a polyphenol by 1H-NMR spectroscopy
    • Murray, N.J., Williamson, M.P., Lilley, T.H., Haslam, E., Study of the interaction between salivary proline-rich proteins and a polyphenol by 1H-NMR spectroscopy. Eur. J. Biochem. 219 (1994), 923–935.
    • (1994) Eur. J. Biochem. , vol.219 , pp. 923-935
    • Murray, N.J.1    Williamson, M.P.2    Lilley, T.H.3    Haslam, E.4
  • 40
    • 0028097921 scopus 로고
    • The structure and function of proline-rich regions in proteins
    • Williamson, M.P., The structure and function of proline-rich regions in proteins. Biochem. J 297 (1994), 249–260.
    • (1994) Biochem. J , vol.297 , pp. 249-260
    • Williamson, M.P.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.