메뉴 건너뛰기




Volumn 239, Issue 6, 2014, Pages 979-993

Impact of ultrasound on egg white proteins as a pretreatment for functional hydrolysates production

Author keywords

Antioxidant activity; Egg white hydrolysates; Functional properties; Proteases; Ultrasound pretreatment

Indexed keywords

ANTIOXIDANTS; PEPTIDES; THERMOACOUSTICS; ULTRASONICS;

EID: 84911986451     PISSN: 14382377     EISSN: 14382385     Source Type: Journal    
DOI: 10.1007/s00217-014-2295-8     Document Type: Article
Times cited : (69)

References (52)
  • 3
    • 1842535878 scopus 로고    scopus 로고
    • Applications and potential of ultrasonics in food processing
    • COI: 1:CAS:528:DC%2BD2cXis1Wns78%3D
    • Knorr D, Zenker M, Heinz V, Lee D-U (2004) Applications and potential of ultrasonics in food processing. Trends Food Sci Technol 15:261–266
    • (2004) Trends Food Sci Technol , vol.15 , pp. 261-266
    • Knorr, D.1    Zenker, M.2    Heinz, V.3    Lee, D.-U.4
  • 4
    • 32944482033 scopus 로고    scopus 로고
    • Interfacial properties and structural conformation of thermosonicated bovine serum albumin
    • Güzey D, Gülseren İ, Bruce B, Weiss J (2006) Interfacial properties and structural conformation of thermosonicated bovine serum albumin. Food Hydrocoll 20:669–677
    • (2006) Food Hydrocoll , vol.20 , pp. 669-677
    • Güzey, D.1    Gülseren, İ.2    Bruce, B.3    Weiss, J.4
  • 5
    • 70350751552 scopus 로고    scopus 로고
    • Ultrasonic effect on physicochemical and functional properties of α-lactalbumin
    • COI: 1:CAS:528:DC%2BD1MXhtlCntL7I
    • 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
    • (2010) LWT Food Sci Technol , vol.43 , pp. 254-262
    • Jambrak, A.R.1    Mason, T.J.2    Lelas, V.3    Krešić, G.4
  • 6
    • 33749386447 scopus 로고    scopus 로고
    • Structural and functional changes in ultrasonicated bovine serum albumin solutions
    • Gülseren İ, Güzey D, Bruce BD, Weiss J (2007) Structural and functional changes in ultrasonicated bovine serum albumin solutions. Ultrason Sonochem 14:173–183
    • (2007) Ultrason Sonochem , vol.14 , pp. 173-183
    • Gülseren, İ.1    Güzey, D.2    Bruce, B.D.3    Weiss, J.4
  • 7
    • 84864016547 scopus 로고    scopus 로고
    • Antioxidant, ACE inhibitory activities and functional properties of egg white protein hydrolysate
    • COI: 1:CAS:528:DC%2BC38XhtlGgu77F
    • Chen C, Chi Y-J (2012) Antioxidant, ACE inhibitory activities and functional properties of egg white protein hydrolysate. J Food Biochem 36:383–394
    • (2012) J Food Biochem , vol.36 , pp. 383-394
    • Chen, C.1    Chi, Y.-J.2
  • 8
    • 84878005615 scopus 로고    scopus 로고
    • Selective release of ACE-inhibiting tryptophan-containing dipeptides from food proteins by enzymatic hydrolysis
    • COI: 1:CAS:528:DC%2BC3sXpvVyis70%3D
    • Lunow D, Kaiser S, Bruckner S, Gotsch A, Henle T (2013) Selective release of ACE-inhibiting tryptophan-containing dipeptides from food proteins by enzymatic hydrolysis. Eur Food Res Technol 237:27–37
    • (2013) Eur Food Res Technol , vol.237 , pp. 27-37
    • Lunow, D.1    Kaiser, S.2    Bruckner, S.3    Gotsch, A.4    Henle, T.5
  • 9
    • 19644374855 scopus 로고    scopus 로고
    • Combined effect of high pressure and temperature on selected properties of egg white proteins
    • Van Der Plancken I, Van Loey A, Hendrickx ME (2005) Combined effect of high pressure and temperature on selected properties of egg white proteins. Innov Food Sci Emerg Technol 6:11–20
    • (2005) Innov Food Sci Emerg Technol , vol.6 , pp. 11-20
    • Van Der Plancken, I.1    Van Loey, A.2    Hendrickx, M.E.3
  • 10
    • 84982522314 scopus 로고
    • Enzymatic modification of egg-white protein and some of its functional properties
    • COI: 1:CAS:528:DyaL28XltlagtLo%3D
    • Behnke U, Kiss E, Nádudvari V, Rutiloff H (1986) Enzymatic modification of egg-white protein and some of its functional properties. Nahrung 30:319–326
    • (1986) Nahrung , vol.30 , pp. 319-326
    • Behnke, U.1    Kiss, E.2    Nádudvari, V.3    Rutiloff, H.4
  • 12
    • 84890348094 scopus 로고    scopus 로고
    • Effect of high-pressure treatment on trypsin hydrolysis and antioxidant activity of egg white proteins
    • COI: 1:CAS:528:DC%2BC3sXhvFegsLfI
    • Singh A, Ramaswamy HS (2014) Effect of high-pressure treatment on trypsin hydrolysis and antioxidant activity of egg white proteins. Int J Food Sci Technol 49:269–279
    • (2014) Int J Food Sci Technol , vol.49 , pp. 269-279
    • Singh, A.1    Ramaswamy, H.S.2
  • 13
    • 0028873168 scopus 로고
    • Advances in the understanding of egg white protein functionalities
    • COI: 1:CAS:528:DyaK2MXntlals7c%3D
    • Mine Y (1995) Advances in the understanding of egg white protein functionalities. Trends Food Sci Technol 6:225–232
    • (1995) Trends Food Sci Technol , vol.6 , pp. 225-232
    • Mine, Y.1
  • 15
    • 33244487664 scopus 로고    scopus 로고
    • Effect of simulated gastrointestinal digestion on the antihypertensive properties of ACE-inhibitory peptides derived from ovalbumin
    • COI: 1:CAS:528:DC%2BD28XksFSgtQ%3D%3D
    • Miguel M, Ramos M, Aleixandre MA, Lopez-Fandino R (2006) Effect of simulated gastrointestinal digestion on the antihypertensive properties of ACE-inhibitory peptides derived from ovalbumin. J Agric Food Chem 54:726–731
    • (2006) J Agric Food Chem , vol.54 , pp. 726-731
    • Miguel, M.1    Ramos, M.2    Aleixandre, M.A.3    Lopez-Fandino, R.4
  • 16
    • 79551543469 scopus 로고    scopus 로고
    • Purification and characterization of angiotensin I converting enzyme (ACE) inhibitory peptides derived from enzymatic hydrolysate of ovotransferrin
    • COI: 1:CAS:528:DC%2BC3MXht1Wlsb4%3D
    • Majumder K, Wu J (2011) Purification and characterization of angiotensin I converting enzyme (ACE) inhibitory peptides derived from enzymatic hydrolysate of ovotransferrin. Food Chem 126:1614–1619
    • (2011) Food Chem , vol.126 , pp. 1614-1619
    • Majumder, K.1    Wu, J.2
  • 17
    • 84875925590 scopus 로고    scopus 로고
    • Research on the preparation of antioxidant peptides derived from egg white with assisting of high-intensity pulsed electric field
    • COI: 1:CAS:528:DC%2BC3sXltFOktro%3D
    • Lin S, Jin Y, Liu M, Yang Y, Zhang M, Guo Y, Jones G, Liu J, Yin Y (2013) Research on the preparation of antioxidant peptides derived from egg white with assisting of high-intensity pulsed electric field. Food Chem 139:300–306
    • (2013) Food Chem , vol.139 , pp. 300-306
    • Lin, S.1    Jin, Y.2    Liu, M.3    Yang, Y.4    Zhang, M.5    Guo, Y.6    Jones, G.7    Liu, J.8    Yin, Y.9
  • 18
    • 1542347593 scopus 로고    scopus 로고
    • Antimicrobial peptides released by enzymatic hydrolysis of hen egg white lysozyme
    • COI: 1:CAS:528:DC%2BD2cXht1Whs7s%3D
    • Mine Y, Ma F, Lauriau S (2004) Antimicrobial peptides released by enzymatic hydrolysis of hen egg white lysozyme. J Agric Food Chem 52:1088–1094
    • (2004) J Agric Food Chem , vol.52 , pp. 1088-1094
    • Mine, Y.1    Ma, F.2    Lauriau, S.3
  • 19
    • 4444238114 scopus 로고    scopus 로고
    • Antioxidant activity of peptides derived from egg white proteins by enzymatic hydrolysis
    • COI: 1:CAS:528:DC%2BD2cXot1Gmsro%3D
    • Davalos A, Miguel M, Bartolome B, Lopez-Fandino R (2004) Antioxidant activity of peptides derived from egg white proteins by enzymatic hydrolysis. J Food Prot 67:1939–1944
    • (2004) J Food Prot , vol.67 , pp. 1939-1944
    • Davalos, A.1    Miguel, M.2    Bartolome, B.3    Lopez-Fandino, R.4
  • 20
    • 84873727878 scopus 로고    scopus 로고
    • Protein hydrolysis using proteases: an important tool for food biotechnology
    • COI: 1:CAS:528:DC%2BC3sXjvFCktbw%3D
    • Tavano OL (2013) Protein hydrolysis using proteases: an important tool for food biotechnology. J Mol Catal B Enzym 90:1–11
    • (2013) J Mol Catal B Enzym , vol.90 , pp. 1-11
    • Tavano, O.L.1
  • 21
    • 84861226863 scopus 로고    scopus 로고
    • Purification and characterization of a novel serine protease compositain from compositae (Scorzonera hispanica L.)
    • COI: 1:CAS:528:DC%2BC38XntVSms7g%3D
    • Nadaroglu H, Demir N (2012) Purification and characterization of a novel serine protease compositain from compositae (Scorzonera hispanica L.). Eur Food Res Technol 234:945–953
    • (2012) Eur Food Res Technol , vol.234 , pp. 945-953
    • Nadaroglu, H.1    Demir, N.2
  • 22
    • 0030586806 scopus 로고    scopus 로고
    • Characterization of casein phosphopeptides prepared alcalase: determination of enzyme specificity
    • COI: 1:CAS:528:DyaK28XksFCjsrw%3D
    • Adamson NJ, Reynolds EC (1996) Characterization of casein phosphopeptides prepared alcalase: determination of enzyme specificity. Enzym Microb Technol 19:202–207
    • (1996) Enzym Microb Technol , vol.19 , pp. 202-207
    • Adamson, N.J.1    Reynolds, E.C.2
  • 23
    • 84894385275 scopus 로고    scopus 로고
    • Effects of sweeping frequency ultrasound treatment on enzymatic preparations of ACE-inhibitory peptides from zein
    • COI: 1:CAS:528:DC%2BC3sXhslGjsb7P
    • Ren X, Ma H, Mao S, Zhou H (2014) Effects of sweeping frequency ultrasound treatment on enzymatic preparations of ACE-inhibitory peptides from zein. Eur Food Res Technol 238:435–442
    • (2014) Eur Food Res Technol , vol.238 , pp. 435-442
    • Ren, X.1    Ma, H.2    Mao, S.3    Zhou, H.4
  • 24
    • 0038115456 scopus 로고    scopus 로고
    • Heat-induced changes in the susceptibility of egg white proteins to enzymatic hydrolysis: a kinetic study
    • Van Der Plancken I, Van Remoortere M, Indrawati Van Loey A, Hendrickx ME (2003) Heat-induced changes in the susceptibility of egg white proteins to enzymatic hydrolysis: a kinetic study. J Agric Food Chem 51:3819–3823
    • (2003) J Agric Food Chem , vol.51 , pp. 3819-3823
    • Van Der Plancken, I.1    Van Remoortere, M.2    Indrawati Van Loey, A.3    Hendrickx, M.E.4
  • 25
    • 84879018339 scopus 로고    scopus 로고
    • Enzymolysis reaction kinetics and thermodynamics of defatted wheat germ protein with ultrasonic pretreatment
    • COI: 1:CAS:528:DC%2BC3sXosVCisL8%3D
    • Qu W, Ma H, Liu B, He R, Pan Z, Abano EE (2013) Enzymolysis reaction kinetics and thermodynamics of defatted wheat germ protein with ultrasonic pretreatment. Ultrason Sonochem 20:1408–1413
    • (2013) Ultrason Sonochem , vol.20 , pp. 1408-1413
    • Qu, W.1    Ma, H.2    Liu, B.3    He, R.4    Pan, Z.5    Abano, E.E.6
  • 26
    • 84885475990 scopus 로고    scopus 로고
    • Effects of microwave and ultrasound pretreatments on enzymolysis of milk protein concentrate with different enzymes
    • COI: 1:CAS:528:DC%2BC3sXhsF2htrfK
    • Uluko H, Zhang S, Liu L, Chen J, Sun Y, Su Y, Li H, Cui W, Lv J (2013) Effects of microwave and ultrasound pretreatments on enzymolysis of milk protein concentrate with different enzymes. Int J Food Sci Technol 48:2250–2257
    • (2013) Int J Food Sci Technol , vol.48 , pp. 2250-2257
    • Uluko, H.1    Zhang, S.2    Liu, L.3    Chen, J.4    Sun, Y.5    Su, Y.6    Li, H.7    Cui, W.8    Lv, J.9
  • 27
    • 77956615199 scopus 로고    scopus 로고
    • Effect of sonication on thermolysin hydrolysis of ovotransferrin
    • COI: 1:CAS:528:DC%2BC3cXhtFOitbrE
    • Lei B, Majumder K, Shen S, Wu J (2011) Effect of sonication on thermolysin hydrolysis of ovotransferrin. Food Chem 124:808–815
    • (2011) Food Chem , vol.124 , pp. 808-815
    • Lei, B.1    Majumder, K.2    Shen, S.3    Wu, J.4
  • 29
    • 84879030357 scopus 로고    scopus 로고
    • Pretreatment of defatted wheat germ proteins (by-products of flour mill industry) using ultrasonic horn and bath reactors: effect on structure and preparation of ACE-inhibitory peptides
    • COI: 1:CAS:528:DC%2BC3sXmvV2nsbY%3D
    • Zhou C, Ma H, Yu X, Liu B, Yagoub El-Gasim A, Pan Z (2013) Pretreatment of defatted wheat germ proteins (by-products of flour mill industry) using ultrasonic horn and bath reactors: effect on structure and preparation of ACE-inhibitory peptides. Ultrason Sonochem 20:1390–1400
    • (2013) Ultrason Sonochem , vol.20 , pp. 1390-1400
    • Zhou, C.1    Ma, H.2    Yu, X.3    Liu, B.4    Yagoub El-Gasim, A.5    Pan, Z.6
  • 31
    • 0036302694 scopus 로고    scopus 로고
    • Utilisation of chickpea protein isolates for production of peptides with angiotensin I-converting enzyme (ACE)-inhibitory activity
    • COI: 1:CAS:528:DC%2BD38XlsFShtr8%3D
    • Pedroche J, Yust MM, Giron-Calle J, Alaiz M, Millan F, Vioque J (2002) Utilisation of chickpea protein isolates for production of peptides with angiotensin I-converting enzyme (ACE)-inhibitory activity. J Sci Food Agric 82:960–965
    • (2002) J Sci Food Agric , vol.82 , pp. 960-965
    • Pedroche, J.1    Yust, M.M.2    Giron-Calle, J.3    Alaiz, M.4    Millan, F.5    Vioque, J.6
  • 33
    • 0000209774 scopus 로고
    • Studies on products of browning reaction. Antioxidative activities of products of browning reaction prepared from glucosamine
    • COI: 1:CAS:528:DyaL2sXktlyiu7g%3D
    • Oyaizu M (1986) Studies on products of browning reaction. Antioxidative activities of products of browning reaction prepared from glucosamine. Jpn J Nutr Diet 44:307–315
    • (1986) Jpn J Nutr Diet , vol.44 , pp. 307-315
    • Oyaizu, M.1
  • 34
    • 37349053019 scopus 로고    scopus 로고
    • Antioxidant and radical scavenging properties of Iris germanica
    • COI: 1:CAS:528:DC%2BD2sXhsVGgtbzE
    • Nadaroglu H, Demir Y, Demir N (2007) Antioxidant and radical scavenging properties of Iris germanica. Pharm Chem J 41:409–415
    • (2007) Pharm Chem J , vol.41 , pp. 409-415
    • Nadaroglu, H.1    Demir, Y.2    Demir, N.3
  • 35
    • 69949109819 scopus 로고    scopus 로고
    • Antioxidant and radical scavenging activities of capsules of caper (Capparis spinosa)
    • COI: 1:CAS:528:DC%2BD1MXhtVGht7bI
    • Nadaroglu H, Demır N, Demır Y (2009) Antioxidant and radical scavenging activities of capsules of caper (Capparis spinosa). Asian J Chem 21:5123–5134
    • (2009) Asian J Chem , vol.21 , pp. 5123-5134
    • Nadaroglu, H.1    Demır, N.2    Demır, Y.3
  • 37
    • 71849104860 scopus 로고
    • Protein measurement with the Folin phenol reagent
    • COI: 1:CAS:528:DyaG38XhsVyrsw%3D%3D
    • Lowry OH, Rosebrough NJ, Farr AL, Randall RJ (1951) Protein measurement with the Folin phenol reagent. J Biol Chem 193:265–275
    • (1951) J Biol Chem , vol.193 , pp. 265-275
    • Lowry, O.H.1    Rosebrough, N.J.2    Farr, A.L.3    Randall, R.J.4
  • 38
    • 0032982508 scopus 로고    scopus 로고
    • Antioxidant activity applying an improved ABTS radical cation decolorization assay
    • COI: 1:CAS:528:DyaK1MXjvVakt7o%3D
    • Re R, Pellegrini N, Proteggente A, Pannala A, Yang M, Rice-Evans C (1999) Antioxidant activity applying an improved ABTS radical cation decolorization assay. Free Radic Biol Med 26:1231–1237
    • (1999) Free Radic Biol Med , vol.26 , pp. 1231-1237
    • Re, R.1    Pellegrini, N.2    Proteggente, A.3    Pannala, A.4    Yang, M.5    Rice-Evans, C.6
  • 39
    • 0035238923 scopus 로고    scopus 로고
    • Effect of malt pretreatment on phytic acid and in vitro protein digestibility of sorghum flour
    • COI: 1:CAS:528:DC%2BD3cXovFSlu7g%3D
    • Elkhalil EAI, El Tinay AH, Mohamed BE, Elsheikh EAE (2001) Effect of malt pretreatment on phytic acid and in vitro protein digestibility of sorghum flour. Food Chem 72:29–32
    • (2001) Food Chem , vol.72 , pp. 29-32
    • Elkhalil, E.A.I.1    El Tinay, A.H.2    Mohamed, B.E.3    Elsheikh, E.A.E.4
  • 40
    • 33748533149 scopus 로고    scopus 로고
    • Foaming properties of egg white proteins affected by heat or high pressure treatment
    • Van der Plancken I, Van Loey A, Hendrickx ME (2007) Foaming properties of egg white proteins affected by heat or high pressure treatment. J Food Eng 78:1410–1426
    • (2007) J Food Eng , vol.78 , pp. 1410-1426
    • Van der Plancken, I.1    Van Loey, A.2    Hendrickx, M.E.3
  • 41
    • 84883480405 scopus 로고    scopus 로고
    • Effect of ultrasound treatment on particle size and molecular weight of whey proteins
    • COI: 1:CAS:528:DC%2BC3sXhsVylsbrM
    • Jambrak AR, Mason TJ, Lelas V, Paniwnyk L, Herceg Z (2014) Effect of ultrasound treatment on particle size and molecular weight of whey proteins. J Food Eng 121:15–23
    • (2014) J Food Eng , vol.121 , pp. 15-23
    • Jambrak, A.R.1    Mason, T.J.2    Lelas, V.3    Paniwnyk, L.4    Herceg, Z.5
  • 42
    • 77951569210 scopus 로고    scopus 로고
    • Ultrasonic parameters of hen’s egg
    • Opielinski KJ (2007) Ultrasonic parameters of hen’s egg. Mol Quant Acoust 28:203–216
    • (2007) Mol Quant Acoust , vol.28 , pp. 203-216
    • Opielinski, K.J.1
  • 43
    • 35349029007 scopus 로고    scopus 로고
    • Protein digestibility of selected legumes treated with ultrasound and high hydrostatic pressure during soaking
    • COI: 1:CAS:528:DC%2BD2sXhtFGmsLnE
    • Han IH, Swanson BG, Baik BK (2007) Protein digestibility of selected legumes treated with ultrasound and high hydrostatic pressure during soaking. Cereal Chem 84:518–521
    • (2007) Cereal Chem , vol.84 , pp. 518-521
    • Han, I.H.1    Swanson, B.G.2    Baik, B.K.3
  • 44
    • 84888642304 scopus 로고    scopus 로고
    • Ultrasonic pretreatment of corn gluten meal proteins and neutrase: effect on protein conformation and preparation of ACE (angiotensin converting enzyme) inhibitory peptides
    • COI: 1:CAS:528:DC%2BC3sXhtVOjsbjK
    • Zhou C, Ma H, Ding Q, Lin L, Yu X, Luo L, Dai C, Yagoub AE-GA (2013) Ultrasonic pretreatment of corn gluten meal proteins and neutrase: effect on protein conformation and preparation of ACE (angiotensin converting enzyme) inhibitory peptides. Food Bioprod Process 91:665–671
    • (2013) Food Bioprod Process , vol.91 , pp. 665-671
    • Zhou, C.1    Ma, H.2    Ding, Q.3    Lin, L.4    Yu, X.5    Luo, L.6    Dai, C.7    Yagoub, A.E.-G.A.8
  • 45
    • 85012401662 scopus 로고
    • Increase in the pH of the white and yolk of hens’ eggs
    • COI: 1:CAS:528:DyaA3MXhsVCitQ%3D%3D
    • Sharp PF, Powell CK (1931) Increase in the pH of the white and yolk of hens’ eggs. Ind Eng Chem 23:196–199
    • (1931) Ind Eng Chem , vol.23 , pp. 196-199
    • Sharp, P.F.1    Powell, C.K.2
  • 46
    • 84887580420 scopus 로고    scopus 로고
    • Free radical scavenging activity of peptide fractions from defatted soybean meal hydrolysates evaluated by electron spin resonance
    • COI: 1:CAS:528:DC%2BC2cXhs1OgtbrN
    • Xu J, Zhao Q, Qu Y, Ye F (2013) Free radical scavenging activity of peptide fractions from defatted soybean meal hydrolysates evaluated by electron spin resonance. Food Sci Technol Int 19:557–566
    • (2013) Food Sci Technol Int , vol.19 , pp. 557-566
    • Xu, J.1    Zhao, Q.2    Qu, Y.3    Ye, F.4
  • 48
    • 84872374073 scopus 로고    scopus 로고
    • Determination of reaction kinetics of hydrolysis of tilapia (Oreochromis niloticus) protein for manipulating production of bioactive peptides with antioxidant activity, angiotensin-I-converting enzyme inhibitory activity and Ca-binding properties
    • COI: 1:CAS:528:DC%2BC3sXns1yjug%3D%3D
    • Charoenphun N, Youravong W, Cheirsilp B (2013) Determination of reaction kinetics of hydrolysis of tilapia (Oreochromis niloticus) protein for manipulating production of bioactive peptides with antioxidant activity, angiotensin-I-converting enzyme inhibitory activity and Ca-binding properties. Int J Food Sci Technol 48:419–428
    • (2013) Int J Food Sci Technol , vol.48 , pp. 419-428
    • Charoenphun, N.1    Youravong, W.2    Cheirsilp, B.3
  • 49
    • 77950545854 scopus 로고    scopus 로고
    • Antioxidant properties of whey protein hydrolysates as measured by three methods
    • COI: 1:CAS:528:DC%2BC3cXjtFKktr0%3D
    • Dryakova A, Pihlanto A, Marnila P, Curda L, Korhonen HJT (2010) Antioxidant properties of whey protein hydrolysates as measured by three methods. Eur Food Res Technol 230:865–874
    • (2010) Eur Food Res Technol , vol.230 , pp. 865-874
    • Dryakova, A.1    Pihlanto, A.2    Marnila, P.3    Curda, L.4    Korhonen, H.J.T.5
  • 50
    • 84880330485 scopus 로고    scopus 로고
    • Antioxidant peptides obtained from goose egg white proteins by enzymatic hydrolysis
    • COI: 1:CAS:528:DC%2BC3sXhtV2mt7nE
    • Baratzadeh MH, Asoodeh A, Chamani J (2013) Antioxidant peptides obtained from goose egg white proteins by enzymatic hydrolysis. Int J Food Sci Technol 48:1603–1609
    • (2013) Int J Food Sci Technol , vol.48 , pp. 1603-1609
    • Baratzadeh, M.H.1    Asoodeh, A.2    Chamani, J.3
  • 51
    • 80051545037 scopus 로고    scopus 로고
    • Antioxidant activities of rapeseed protein hydrolysates
    • COI: 1:CAS:528:DC%2BC3MXht1ShtL7M
    • Pan M, Jiang T, Pan J (2011) Antioxidant activities of rapeseed protein hydrolysates. Food Bioprocess Technol 4:1144–1152
    • (2011) Food Bioprocess Technol , vol.4 , pp. 1144-1152
    • Pan, M.1    Jiang, T.2    Pan, J.3
  • 52
    • 70349835623 scopus 로고    scopus 로고
    • The use of ultrasound for enzymatic preparation of ACE-inhibitory peptides from wheat germ protein
    • COI: 1:CAS:528:DC%2BD1MXht1Oiu7jN
    • Jia J, Ma H, Zhao W, Wang Z, Tian W, Luo L, He R (2010) The use of ultrasound for enzymatic preparation of ACE-inhibitory peptides from wheat germ protein. Food Chem 119:336–342
    • (2010) Food Chem , vol.119 , pp. 336-342
    • Jia, J.1    Ma, H.2    Zhao, W.3    Wang, Z.4    Tian, W.5    Luo, L.6    He, R.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.