메뉴 건너뛰기




Volumn 83, Issue 8, 2018, Pages 2092-2100

Covalent Whey Protein–Rosmarinic Acid Interactions: A Comparison of Alkaline and Enzymatic Modifications on Physicochemical, Antioxidative, and Antibacterial Properties

Author keywords

antioxidant activity; covalent interactions; enzymatic modification; rosmarinic acid; whey protein isolate

Indexed keywords

ANTIINFECTIVE AGENT; ANTIOXIDANT; CINNAMIC ACID DERIVATIVE; DEPSIDE; MONOPHENOL MONOOXYGENASE; PHENOL DERIVATIVE; ROSMARINIC ACID; WHEY PROTEIN;

EID: 85050641217     PISSN: 00221147     EISSN: 17503841     Source Type: Journal    
DOI: 10.1111/1750-3841.14222     Document Type: Article
Times cited : (64)

References (58)
  • 1
    • 0017024705 scopus 로고
    • Enzymic hydrolysis of proteins for increased solubility
    • Adler-Nissen, J. (1976). Enzymic hydrolysis of proteins for increased solubility. Journal of Agricultural and Food Chemistry, 24, 1090–1093
    • (1976) Journal of Agricultural and Food Chemistry , vol.24 , pp. 1090-1093
    • Adler-Nissen, J.1
  • 2
    • 84874117816 scopus 로고    scopus 로고
    • Enhancement of emulsifying properties of cuttlefish skin Gelatin by modification with N-hydroxysuccinimide esters of fatty acids
    • Aewsiri, T., Benjakul, S., Visessanguan, W., Encarnacion, A., Wierenga, P., & Gruppen, H. (2013). Enhancement of emulsifying properties of cuttlefish skin Gelatin by modification with N-hydroxysuccinimide esters of fatty acids. Food and Bioprocess Technology, 6, 671–681
    • (2013) Food and Bioprocess Technology , vol.6 , pp. 671-681
    • Aewsiri, T.1    Benjakul, S.2    Visessanguan, W.3    Encarnacion, A.4    Wierenga, P.5    Gruppen, H.6
  • 3
    • 67349254662 scopus 로고    scopus 로고
    • Antioxidative activity and emulsifying properties of cuttlefish skin gelatin modified by oxidized phenolic compounds
    • Aewsiri, T., Benjakul, S., Visessanguan, W., Eun, J.-B., Wierenga, P. A., & Gruppen, H. (2009). Antioxidative activity and emulsifying properties of cuttlefish skin gelatin modified by oxidized phenolic compounds. Food Chemistry, 117, 160–168
    • (2009) Food Chemistry , vol.117 , pp. 160-168
    • Aewsiri, T.1    Benjakul, S.2    Visessanguan, W.3    Eun, J.-B.4    Wierenga, P.A.5    Gruppen, H.6
  • 4
    • 84880348207 scopus 로고    scopus 로고
    • Milk whey protein modification by coffee-specific phenolics: Effect on structural and functional properties
    • Ali, M., Homann, T., Khalil, M., Kruse, H.-P., & Rawel, H. (2013). Milk whey protein modification by coffee-specific phenolics: Effect on structural and functional properties. Journal of Agricultural and Food Chemistry, 61, 6911–6920
    • (2013) Journal of Agricultural and Food Chemistry , vol.61 , pp. 6911-6920
    • Ali, M.1    Homann, T.2    Khalil, M.3    Kruse, H.-P.4    Rawel, H.5
  • 5
    • 0034001548 scopus 로고    scopus 로고
    • Comparison of protein surface hydrophobicity measured at various pH values using three different fluorescent probes
    • Alizadeh-Pasdar, N., & Li-Chan, E. C. Y. (2000). Comparison of protein surface hydrophobicity measured at various pH values using three different fluorescent probes. Journal of Agricultural and Food Chemistry, 48(2), 328–334
    • (2000) Journal of Agricultural and Food Chemistry , vol.48 , Issue.2 , pp. 328-334
    • Alizadeh-Pasdar, N.1    Li-Chan, E.C.Y.2
  • 6
    • 84930399538 scopus 로고    scopus 로고
    • Characterization and biological activities of extracellular melanin produced by Schizophyllum commune (Fries)
    • Arun, G., Eyini, M., & Gunasekaran, P. (2015). Characterization and biological activities of extracellular melanin produced by Schizophyllum commune (Fries). Indian Journal of Experimental Biology, 53, 380–387
    • (2015) Indian Journal of Experimental Biology , vol.53 , pp. 380-387
    • Arun, G.1    Eyini, M.2    Gunasekaran, P.3
  • 7
    • 34548317269 scopus 로고    scopus 로고
    • Antioxidative activity of Mungoong, an extract paste, from the cephalothorax of white shrimp (Litopenaeus vannamei)
    • Binsan, W., Benjakul, S., Visessanguan, W., Roytrakul, S., Tanaka, M., & Kishimura, H. (2008). Antioxidative activity of Mungoong, an extract paste, from the cephalothorax of white shrimp (Litopenaeus vannamei). Food Chemistry, 106, 185–193
    • (2008) Food Chemistry , vol.106 , pp. 185-193
    • Binsan, W.1    Benjakul, S.2    Visessanguan, W.3    Roytrakul, S.4    Tanaka, M.5    Kishimura, H.6
  • 8
    • 85000789435 scopus 로고    scopus 로고
    • Evidence for the formation of Benzacridine derivatives in slkaline-treated sunflower meal and model solutions
    • Bongartz, V., Brandt, L., Gehrmann, M., Zimmermann, B., Schulze-Kaysers, N., & Schieber, A. (2016). Evidence for the formation of Benzacridine derivatives in slkaline-treated sunflower meal and model solutions. Molecules, 21, 91–100
    • (2016) Molecules , vol.21 , pp. 91-100
    • Bongartz, V.1    Brandt, L.2    Gehrmann, M.3    Zimmermann, B.4    Schulze-Kaysers, N.5    Schieber, A.6
  • 10
    • 85010911748 scopus 로고    scopus 로고
    • Interaction of whey proteins with phenolic derivatives under neutral and acidic pH conditions
    • Cao, Y., & Xiong, Y. L. (2017). Interaction of whey proteins with phenolic derivatives under neutral and acidic pH conditions. Journal of Food Science, 82(2), 409–419
    • (2017) Journal of Food Science , vol.82 , Issue.2 , pp. 409-419
    • Cao, Y.1    Xiong, Y.L.2
  • 11
    • 85047392286 scopus 로고    scopus 로고
    • Interfacial properties of whey protein foams as influenced by preheating and phenolic binding at neutral pH
    • Cao, Y., Xiong, Y. L., Cao, Y., & True, A. D. (2018). Interfacial properties of whey protein foams as influenced by preheating and phenolic binding at neutral pH. Food Hydrocolloids, 82, 379–387
    • (2018) Food Hydrocolloids , vol.82 , pp. 379-387
    • Cao, Y.1    Xiong, Y.L.2    Cao, Y.3    True, A.D.4
  • 12
    • 78650329054 scopus 로고    scopus 로고
    • Antimicrobial activity of bovine β-lactoglobulin against mastitis-causing bacteria
    • Chaneton, L., Perez Saez, J. M., & Bussmann, L. E. (2011). Antimicrobial activity of bovine β-lactoglobulin against mastitis-causing bacteria. Journal of Dairy Science, 94(1), 138e–e145
    • (2011) Journal of Dairy Science , vol.94 , Issue.1 , pp. 138e-e145
    • Chaneton, L.1    Perez Saez, J.M.2    Bussmann, L.E.3
  • 13
    • 33748449287 scopus 로고    scopus 로고
    • Bioactivity of β-lactoglobulin and β-lactalbumin—Technological implications for processing
    • Chatterton, D. E. W., Smithers, G., Roupas, P., & Brodkorb, A. (2006). Bioactivity of β-lactoglobulin and β-lactalbumin—Technological implications for processing. International Dairy Journal, 16, 1229–1240
    • (2006) International Dairy Journal , vol.16 , pp. 1229-1240
    • Chatterton, D.E.W.1    Smithers, G.2    Roupas, P.3    Brodkorb, A.4
  • 15
    • 1942441014 scopus 로고    scopus 로고
    • Spectroscopic characterization of heat-induced nonnative β–Lactoglobulin monomers
    • Croguennec, T., Molle, D., Mehra, R., & Bouhallab, S. (2004). Spectroscopic characterization of heat-induced nonnative β–Lactoglobulin monomers. Protein Science, 13, 1340–1346
    • (2004) Protein Science , vol.13 , pp. 1340-1346
    • Croguennec, T.1    Molle, D.2    Mehra, R.3    Bouhallab, S.4
  • 16
    • 0038528396 scopus 로고    scopus 로고
    • Whey protein isolate and glyco-macropeptide recovery from whey using ion exchange chromatography
    • Doultani, S., Turhan, K. N., & Etzel, M. R. (2003). Whey protein isolate and glyco-macropeptide recovery from whey using ion exchange chromatography. Journal of Food Science, 68, 1389–1395
    • (2003) Journal of Food Science , vol.68 , pp. 1389-1395
    • Doultani, S.1    Turhan, K.N.2    Etzel, M.R.3
  • 17
    • 84855682808 scopus 로고    scopus 로고
    • Antioxidation mechanism of rosmarinic acid, identification of an unstable quinone derivative by the addition of odorless thiol
    • Fujimoto, A., & Masuda, T. (2012). Antioxidation mechanism of rosmarinic acid, identification of an unstable quinone derivative by the addition of odorless thiol. Food Chemistry, 132(2), 901–906
    • (2012) Food Chemistry , vol.132 , Issue.2 , pp. 901-906
    • Fujimoto, A.1    Masuda, T.2
  • 19
    • 84991316046 scopus 로고    scopus 로고
    • Interactions of β–conglycinin (7S) with different phenolic acids: impact on structural characteristics and proteolytic degradation of proteins
    • Gan, J., Chen, H., Liu, J., Wang, Y., Nirasawa, S., & Cheng, Y. (2016). Interactions of β–conglycinin (7S) with different phenolic acids: impact on structural characteristics and proteolytic degradation of proteins. International Journal of Molecular Sciences, 17(10), 1671–1684
    • (2016) International Journal of Molecular Sciences , vol.17 , Issue.10 , pp. 1671-1684
    • Gan, J.1    Chen, H.2    Liu, J.3    Wang, Y.4    Nirasawa, S.5    Cheng, Y.6
  • 21
    • 84937605198 scopus 로고    scopus 로고
    • Intrinsic tryptophan fluorescence in the detection and analysis of proteins: A focus on forster resonance energy transfer techniques
    • Ghisaidoobe, A. B. T., & Chung, S. J. (2014). Intrinsic tryptophan fluorescence in the detection and analysis of proteins: A focus on forster resonance energy transfer techniques. International Journal of Molecular Sciences, 15, 22518–22538
    • (2014) International Journal of Molecular Sciences , vol.15 , pp. 22518-22538
    • Ghisaidoobe, A.B.T.1    Chung, S.J.2
  • 22
    • 73549106551 scopus 로고    scopus 로고
    • Phenolic compounds prevent Alzheimer's pathology through different effects on the amyloid- beta aggregation pathway
    • Hamaguchi, T., Ono, K., Murase, A., & Yamada, M. (2009). Phenolic compounds prevent Alzheimer's pathology through different effects on the amyloid- beta aggregation pathway. The American Journal of Pathology, 175(6), 2557–2565
    • (2009) The American Journal of Pathology , vol.175 , Issue.6 , pp. 2557-2565
    • Hamaguchi, T.1    Ono, K.2    Murase, A.3    Yamada, M.4
  • 23
    • 84985200365 scopus 로고
    • Relationships of hydrophobicity and net charge to the solubility of milk and soy proteins
    • Hayakawa, S., & Nakai, S. (1985). Relationships of hydrophobicity and net charge to the solubility of milk and soy proteins. Journal of Food Science, 50, 486–491
    • (1985) Journal of Food Science , vol.50 , pp. 486-491
    • Hayakawa, S.1    Nakai, S.2
  • 24
    • 0018163373 scopus 로고
    • Sulfhydryl and disulfide groups in meats
    • &
    • Hofmann, K. & Hamm, R. (1978). Sulfhydryl and disulfide groups in meats. Advances in Food Research, 24, 1–111
    • (1978) Advances in Food Research , vol.24 , pp. 1-111
    • Hofmann, K.1    Hamm, R.2
  • 25
    • 72449169400 scopus 로고    scopus 로고
    • Rosmarinic acid in Prunella vulgaris ethanol extract inhibits lipopolysaccharide-induced prostaglandin E2 and nitric oxide in RAW 264.7 mouse macrophages
    • Huang, N., Hauck, C., Yum, M-Y., Rizshsky, L., Widrlechner, M. P., Mccoy, J-A., … Birt, D. F. (2009). Rosmarinic acid in Prunella vulgaris ethanol extract inhibits lipopolysaccharide-induced prostaglandin E2 and nitric oxide in RAW 264.7 mouse macrophages. Journal of Agriculture and Food Chemistry, 57(22), 10579–10589
    • (2009) Journal of Agriculture and Food Chemistry , vol.57 , Issue.22 , pp. 10579-10589
    • Huang, N.1    Hauck, C.2    Yum, M.-Y.3    Rizshsky, L.4    Widrlechner, M.P.5    Mccoy, J.-A.6    Birt, D.F.7
  • 26
    • 84950143102 scopus 로고    scopus 로고
    • Effect of covalent modification by (-)-epigallocatechin-3-gallate on physicochemical and functional properties of whey protein isolate
    • Jia, Z., Zheng, M., Tao, F., Chen, W., Huang, G., & Jiang, J. (2016). Effect of covalent modification by (-)-epigallocatechin-3-gallate on physicochemical and functional properties of whey protein isolate. LWT-Food Science and Technology, 66, 305–310
    • (2016) LWT-Food Science and Technology , vol.66 , pp. 305-310
    • Jia, Z.1    Zheng, M.2    Tao, F.3    Chen, W.4    Huang, G.5    Jiang, J.6
  • 27
    • 67650465074 scopus 로고    scopus 로고
    • Whey proteins-properties and possibility of application
    • Jovanović, S., Barać, M., & Maćej, O. (2005). Whey proteins-properties and possibility of application. Mljekarstvo, 55, 215–233
    • (2005) Mljekarstvo , vol.55 , pp. 215-233
    • Jovanović, S.1    Barać, M.2    Maćej, O.3
  • 28
    • 85041009838 scopus 로고    scopus 로고
    • Covalent bonding of chlorogenic acid induces structural modifications on sunflower proteins
    • Karefyllakis, D., Salakou, S., Bitter, J. H., Van Der Goot, A. J., & Nikifordidis, C.V. (2018). Covalent bonding of chlorogenic acid induces structural modifications on sunflower proteins. ChemPhysChem, 19, 459–468
    • (2018) ChemPhysChem , vol.19 , pp. 459-468
    • Karefyllakis, D.1    Salakou, S.2    Bitter, J.H.3    Van Der Goot, A.J.4    Nikifordidis, C.V.5
  • 29
    • 85027952807 scopus 로고    scopus 로고
    • Functionality of whey proteins covalently modified by allyl isothiocyanate. Part 1 physicochemical and antibacterial properties of native and modified whey proteins at pH 2 to 7
    • Keppler, J. K., Martin, D., Garamus, V. M., Berton-Carabin, C., Nipoti, E., Coenye, T., & Schwarz, K. (2017). Functionality of whey proteins covalently modified by allyl isothiocyanate. Part 1 physicochemical and antibacterial properties of native and modified whey proteins at pH 2 to 7. Food Hydrocolloid, 65, 130–143
    • (2017) Food Hydrocolloid , vol.65 , pp. 130-143
    • Keppler, J.K.1    Martin, D.2    Garamus, V.M.3    Berton-Carabin, C.4    Nipoti, E.5    Coenye, T.6    Schwarz, K.7
  • 30
    • 84943819441 scopus 로고    scopus 로고
    • Differences in binding behavior of (-)-epigallocatechin gallate to β-lactoglobulin heterodimers (AB) compared to homodimers (A) and (B)
    • Keppler, J. K., Martin, D., Garamus, V. M., & Schwarz, K. (2015). Differences in binding behavior of (-)-epigallocatechin gallate to β-lactoglobulin heterodimers (AB) compared to homodimers (A) and (B). Journal of Molecular Recognition, 28, 656–666
    • (2015) Journal of Molecular Recognition , vol.28 , pp. 656-666
    • Keppler, J.K.1    Martin, D.2    Garamus, V.M.3    Schwarz, K.4
  • 31
    • 85016509968 scopus 로고    scopus 로고
    • Increasing the emulsifying capacity of whey proteins at acidic pH values through covalent modification with allyl isothiocyanate
    • Keppler, J. K., & Schwarz, K. (2017). Increasing the emulsifying capacity of whey proteins at acidic pH values through covalent modification with allyl isothiocyanate. Colloids and Surfaces A: Physicochemical and Engineering Aspects, 522, 514–524
    • (2017) Colloids and Surfaces A: Physicochemical and Engineering Aspects , vol.522 , pp. 514-524
    • Keppler, J.K.1    Schwarz, K.2
  • 32
    • 84898606059 scopus 로고    scopus 로고
    • Differences in heat stability and ligand binding among β–lactoglobulin genetic variants A, B, and C using 1H NMR and fluorescence quenching
    • Keppler, J. K., Sonnichsen, F. D., Lorenzen, P.-C., & Schwarz, K. (2014a). Differences in heat stability and ligand binding among β–lactoglobulin genetic variants A, B, and C using 1H NMR and fluorescence quenching. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 1844, 1083–1093
    • (2014) Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics , vol.1844 , pp. 1083-1093
    • Keppler, J.K.1    Sonnichsen, F.D.2    Lorenzen, P.-C.3    Schwarz, K.4
  • 33
    • 84901038631 scopus 로고    scopus 로고
    • Influence of mathematical models and correction factors on binding results of polyphenols and retinol with β-Lactoglobulin measured with fluorescence quenching
    • Keppler, J. K., Stuhldreier, M. C., Temps, F., & Schwarz, K. (2014b). Influence of mathematical models and correction factors on binding results of polyphenols and retinol with β-Lactoglobulin measured with fluorescence quenching. Food Biophysics, 9, 158–168
    • (2014) Food Biophysics , vol.9 , pp. 158-168
    • Keppler, J.K.1    Stuhldreier, M.C.2    Temps, F.3    Schwarz, K.4
  • 34
    • 0242657803 scopus 로고    scopus 로고
    • Reactions of plant phenolics with food proteins and enzymes under special consideration of covalent bonds
    • Kroll, J., Rawel, H. M., & Rohn, A. S. (2003). Reactions of plant phenolics with food proteins and enzymes under special consideration of covalent bonds. Food Science and Technology Research, 9, 205–218
    • (2003) Food Science and Technology Research , vol.9 , pp. 205-218
    • Kroll, J.1    Rawel, H.M.2    Rohn, A.S.3
  • 35
    • 33751421851 scopus 로고    scopus 로고
    • Electrostatically driven protein aggregation: β-Lactoglobulin at low ionic strength
    • Majhi, P. R., Ganta, R. R., Vanam, R. P., Seyrek, E., Giger, K., & Dubin, P. L. (2006). Electrostatically driven protein aggregation: β-Lactoglobulin at low ionic strength. Langmuir, 22(22), 9150–9159
    • (2006) Langmuir , vol.22 , Issue.22 , pp. 9150-9159
    • Majhi, P.R.1    Ganta, R.R.2    Vanam, R.P.3    Seyrek, E.4    Giger, K.5    Dubin, P.L.6
  • 36
    • 34548550580 scopus 로고    scopus 로고
    • The molecular characterization and antimicrobial properties of amidated bovine β-lactoglobulin
    • Pan, Y., Shiell, B., Wan, J., Coventry, M. J., Michalski, W. P., Lee, A., & Et, A. L. (2007). The molecular characterization and antimicrobial properties of amidated bovine β-lactoglobulin. International Dairy Journal, 17(12), 1450–1459
    • (2007) International Dairy Journal , vol.17 , Issue.12 , pp. 1450-1459
    • Pan, Y.1    Shiell, B.2    Wan, J.3    Coventry, M.J.4    Michalski, W.P.5    Lee, A.6    Et, A.L.7
  • 37
    • 23244438736 scopus 로고    scopus 로고
    • The nonequilibrium phase and glass transition behavior of β-Lactoglobulin
    • Parker, R., Noel, T. R., Brownsey, G. J., Laos, K., & Ring, S. G. (2005). The nonequilibrium phase and glass transition behavior of β-Lactoglobulin. Biophysical Journal, 89, 1227–1236
    • (2005) Biophysical Journal , vol.89 , pp. 1227-1236
    • Parker, R.1    Noel, T.R.2    Brownsey, G.J.3    Laos, K.4    Ring, S.G.5
  • 41
    • 77949916503 scopus 로고    scopus 로고
    • Nature of hydroxycinnamate-protein interactions
    • Rawel, H. M., & Rohn, S. (2010). Nature of hydroxycinnamate-protein interactions. Phytochemistry Review, 9, 93–109
    • (2010) Phytochemistry Review , vol.9 , pp. 93-109
    • Rawel, H.M.1    Rohn, S.2
  • 42
    • 17444398561 scopus 로고    scopus 로고
    • Characterisation of 11S protein fractions and phenolic compounds from green coffee beans under special consideration of their interactions—a review
    • Rawel, H. M., Rohn, S., & Kroll, J. R. (2005a). Characterisation of 11S protein fractions and phenolic compounds from green coffee beans under special consideration of their interactions—a review. Deutsche Lebensmittelrundschau, 101, 148–159
    • (2005) Deutsche Lebensmittelrundschau , vol.101 , pp. 148-159
    • Rawel, H.M.1    Rohn, S.2    Kroll, J.R.3
  • 43
    • 0041524991 scopus 로고    scopus 로고
    • Model studies on reactions of plant phenols with whey proteins
    • Rawel, H. M., Kroll, J., & Hohl, U. C. (2001a). Model studies on reactions of plant phenols with whey proteins. Nahrung, 45, 72–81
    • (2001) Nahrung , vol.45 , pp. 72-81
    • Rawel, H.M.1    Kroll, J.2    Hohl, U.C.3
  • 44
    • 0035238955 scopus 로고    scopus 로고
    • Reactions of phenolic substances with lysozyme–physicochemical characterization and proteolytic digestion of the derivatives
    • Rawel, H. M., Kroll, J., & Rohn, S. (2001b). Reactions of phenolic substances with lysozyme–physicochemical characterization and proteolytic digestion of the derivatives. Food Chemistry, 72, 59–71
    • (2001) Food Chemistry , vol.72 , pp. 59-71
    • Rawel, H.M.1    Kroll, J.2    Rohn, S.3
  • 46
    • 0036768548 scopus 로고    scopus 로고
    • Structural changes induced in bovine serum albumin by covalent attachment of chlorogenic acid
    • Rawel, H. M., Rohn, S., Kruse, H.-P., & Kroll, J. R. (2002). Structural changes induced in bovine serum albumin by covalent attachment of chlorogenic acid. Food Chemistry, 78, 443–455
    • (2002) Food Chemistry , vol.78 , pp. 443-455
    • Rawel, H.M.1    Rohn, S.2    Kruse, H.-P.3    Kroll, J.R.4
  • 49
    • 23744477534 scopus 로고    scopus 로고
    • Reactions with phenolic substances can induce changes in some physico-chemical properties and activities of bromelain – the consequences for supplementary food products
    • Rohn, S., Rawel, H. M., Röber, M., & Kroll, J. (2005). Reactions with phenolic substances can induce changes in some physico-chemical properties and activities of bromelain – the consequences for supplementary food products. International Journal of Food Science and Technology, 40, 771–782
    • (2005) International Journal of Food Science and Technology , vol.40 , pp. 771-782
    • Rohn, S.1    Rawel, H.M.2    Röber, M.3    Kroll, J.4
  • 50
    • 39749104718 scopus 로고    scopus 로고
    • Characterization of covalent addition products of chlorogenic acid quinone with amino acid derivatives in model systems and apple juice by high-performance liquid chromatography/electrospray ionization tandem mass spectrometry
    • Schilling, S., Sigolotto, C.-I., Carle, R., & Schieber, A. (2008). Characterization of covalent addition products of chlorogenic acid quinone with amino acid derivatives in model systems and apple juice by high-performance liquid chromatography/electrospray ionization tandem mass spectrometry. Rapid Communications in Mass Spectrometry, 22, 441–448
    • (2008) Rapid Communications in Mass Spectrometry , vol.22 , pp. 441-448
    • Schilling, S.1    Sigolotto, C.-I.2    Carle, R.3    Schieber, A.4
  • 51
    • 84857766775 scopus 로고    scopus 로고
    • Thermally-induced β–lactoglobulin-EGCG nanovehicles: Loading, stability, sensory and digestive-release study
    • Shpigelman, A., Cohen, Y., & Livney, Y. D. (2012). Thermally-induced β–lactoglobulin-EGCG nanovehicles: Loading, stability, sensory and digestive-release study. Food Hydrocolloid, 29, 57–67
    • (2012) Food Hydrocolloid , vol.29 , pp. 57-67
    • Shpigelman, A.1    Cohen, Y.2    Livney, Y.D.3
  • 52
    • 37549051646 scopus 로고    scopus 로고
    • Antioxidant potentials and rosmarinic acid levels of the methanolic extracts of Salvia virgata (Jacq), Salvia staminea (Montbret & Aucher ex Bentham) and Salvia verbenaca (L.) from Turkey
    • Tepe, B. (2008). Antioxidant potentials and rosmarinic acid levels of the methanolic extracts of Salvia virgata (Jacq), Salvia staminea (Montbret & Aucher ex Bentham) and Salvia verbenaca (L.) from Turkey. Bioresource Technology, 99(6), 1584–1588
    • (2008) Bioresource Technology , vol.99 , Issue.6 , pp. 1584-1588
    • Tepe, B.1
  • 53
    • 0036653591 scopus 로고    scopus 로고
    • Whey components: millennia of evolution create functionalities for mammalian nutrition: What we know and what we may be overlooking
    • Walzem, R. L., Dillard, C. J., & German, J. B. (2002). Whey components: millennia of evolution create functionalities for mammalian nutrition: What we know and what we may be overlooking. Critical Reviews in Food Science and Nutrition, 42, 353–375
    • (2002) Critical Reviews in Food Science and Nutrition , vol.42 , pp. 353-375
    • Walzem, R.L.1    Dillard, C.J.2    German, J.B.3
  • 54
    • 84951038650 scopus 로고    scopus 로고
    • β-Lactoglobulin as nanotransporter. Part II: Characterization of the covalent protein modification by allicin and diallyl disulfide
    • Wilde, S. C., Treitz, C., Keppler, J. K., Koudelka, T., Palanip, K., Tholey, A., … Schwarz, K. (2016). β-Lactoglobulin as nanotransporter. Part II: Characterization of the covalent protein modification by allicin and diallyl disulfide. Food Chemistry, 197, 1022–1029
    • (2016) Food Chemistry , vol.197 , pp. 1022-1029
    • Wilde, S.C.1    Treitz, C.2    Keppler, J.K.3    Koudelka, T.4    Palanip, K.5    Tholey, A.6    Schwarz, K.7
  • 55
    • 70449627783 scopus 로고    scopus 로고
    • Salvia fruticosa, Salvia officinalis, and rosmarinic acid induce apoptosis and inhibit proliferation of human colorectal cell lines: The role in MAPK/ERK pathway
    • Xavier, C. P., Lima, C. F., Fernandes-Ferreira, M., & Pereira-Wilson, C. (2009). Salvia fruticosa, Salvia officinalis, and rosmarinic acid induce apoptosis and inhibit proliferation of human colorectal cell lines: The role in MAPK/ERK pathway. Nutrition and Cancer, 61(4), 564–571
    • (2009) Nutrition and Cancer , vol.61 , Issue.4 , pp. 564-571
    • Xavier, C.P.1    Lima, C.F.2    Fernandes-Ferreira, M.3    Pereira-Wilson, C.4
  • 57
    • 84896974150 scopus 로고    scopus 로고
    • Conjugation of ovotransferrin with catechin shows improved antioxidant activity
    • You, J., Luo, Y., & Wu, J. (2012). Conjugation of ovotransferrin with catechin shows improved antioxidant activity. Journal of Agricultural and Food Chemistry, 62, 2581–2587
    • (2012) Journal of Agricultural and Food Chemistry , vol.62 , pp. 2581-2587
    • You, J.1    Luo, Y.2    Wu, J.3
  • 58
    • 34547539768 scopus 로고    scopus 로고
    • Broad-spectrum antimicrobial activity of the reactive compounds generated in vitro by Manduca sexta phenoloxidase
    • Zhao, P., Li, J., Wang, Y., & Jiang, H. (2007). Broad-spectrum antimicrobial activity of the reactive compounds generated in vitro by Manduca sexta phenoloxidase. Insect Biochemistry and Molecular Biology, 37, 952–959
    • (2007) Insect Biochemistry and Molecular Biology , vol.37 , pp. 952-959
    • Zhao, P.1    Li, J.2    Wang, Y.3    Jiang, H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.