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Volumn 54, Issue 1, 2011, Pages 20-28

Effects of enzymatic hydrolysis on molecular structure and antioxidant activity of barley hordein

Author keywords

Antioxidant activity; Barley hordein; Enzymatic hydrolysis; Molecular weight

Indexed keywords

HORDEUM; HORDEUM VULGARE SUBSP. VULGARE;

EID: 79960845541     PISSN: 07335210     EISSN: 10959963     Source Type: Journal    
DOI: 10.1016/j.jcs.2011.01.006     Document Type: Article
Times cited : (137)

References (43)
  • 1
    • 0018536145 scopus 로고
    • Determination of the degree of hydrolysis of food protein hydrolysates by trinitrobenzenesulfonic acid
    • Adler-Nissen J. Determination of the degree of hydrolysis of food protein hydrolysates by trinitrobenzenesulfonic acid. Journal of the Agricultural and Food Chemistry 1979, 27(6):1256-1262.
    • (1979) Journal of the Agricultural and Food Chemistry , vol.27 , Issue.6 , pp. 1256-1262
    • Adler-Nissen, J.1
  • 2
    • 77955599296 scopus 로고    scopus 로고
    • Enzymatic production of bioactive protein hydrolysates from tuna liver: effects of enzymes and molecular weight on bioactivity
    • Ahn C.-B., Lee K.-H., Je J.-Y. Enzymatic production of bioactive protein hydrolysates from tuna liver: effects of enzymes and molecular weight on bioactivity. International Journal of Food Science and Technology 2010, 45:562-568.
    • (2010) International Journal of Food Science and Technology , vol.45 , pp. 562-568
    • Ahn, C.-B.1    Lee, K.-H.2    Je, J.-Y.3
  • 3
    • 84987261103 scopus 로고
    • Lipophilization of β-lactoglobulin: effect on hydrophobicity, conformation and surface functional properties
    • Akita E.M., Nakai S. Lipophilization of β-lactoglobulin: effect on hydrophobicity, conformation and surface functional properties. Journal of Food Science 1990, 55(3):711-717.
    • (1990) Journal of Food Science , vol.55 , Issue.3 , pp. 711-717
    • Akita, E.M.1    Nakai, S.2
  • 4
    • 33746725357 scopus 로고    scopus 로고
    • Antioxidant properties and protein compositions of porcine haemoglobin hydrolysates
    • Chang C.-Y., Wu K.-C., Chiang S.-H. Antioxidant properties and protein compositions of porcine haemoglobin hydrolysates. Food Chemistry 2007, 100:1537-1543.
    • (2007) Food Chemistry , vol.100 , pp. 1537-1543
    • Chang, C.-Y.1    Wu, K.-C.2    Chiang, S.-H.3
  • 5
    • 67349160258 scopus 로고    scopus 로고
    • Antioxidative properties of partially purified barley hordein, rice bran protein fractions and their hydrolysates
    • Chanput W., Theerakulkait C., Nakai S. Antioxidative properties of partially purified barley hordein, rice bran protein fractions and their hydrolysates. Journal of Cereal Science 2009, 49:422-428.
    • (2009) Journal of Cereal Science , vol.49 , pp. 422-428
    • Chanput, W.1    Theerakulkait, C.2    Nakai, S.3
  • 7
    • 77954953719 scopus 로고    scopus 로고
    • Antioxidant activity of yoghurt peptides: part 2 - characterization of peptide fractions
    • Farvin K.H.S., Baron C.P., Nielsen N.S., Otte J., Jacobsen C. Antioxidant activity of yoghurt peptides: part 2 - characterization of peptide fractions. Food Chemistry 2010, 123:1090-1097.
    • (2010) Food Chemistry , vol.123 , pp. 1090-1097
    • Farvin, K.H.S.1    Baron, C.P.2    Nielsen, N.S.3    Otte, J.4    Jacobsen, C.5
  • 8
    • 0033805608 scopus 로고    scopus 로고
    • The problems of using one-dimensional methods to evaluate multifunctional food and biological antioxidants
    • Frankel E.N., Meyer A.S. The problems of using one-dimensional methods to evaluate multifunctional food and biological antioxidants. Journal of the Science of Food and Agriculture 2000, 80:1925-1941.
    • (2000) Journal of the Science of Food and Agriculture , vol.80 , pp. 1925-1941
    • Frankel, E.N.1    Meyer, A.S.2
  • 9
    • 29244486210 scopus 로고    scopus 로고
    • Food-derived antioxidants: how to evaluate their importance in food and in vivo
    • Marcel Dekker, Inc., New York, E. Cadenas, L. Packer (Eds.)
    • Halliwell B. Food-derived antioxidants: how to evaluate their importance in food and in vivo. Handbook of Antioxidants 2002, 1-45. Marcel Dekker, Inc., New York. E. Cadenas, L. Packer (Eds.).
    • (2002) Handbook of Antioxidants , pp. 1-45
    • Halliwell, B.1
  • 10
    • 0032818805 scopus 로고    scopus 로고
    • FTIR spectroscopic characterization of protein structure in aqueous and non-aqueous media
    • Haris P.I., Severcan F. FTIR spectroscopic characterization of protein structure in aqueous and non-aqueous media. Journal of Molecular Catalysis B: Enzymatic 1999, 7:207-221.
    • (1999) Journal of Molecular Catalysis B: Enzymatic , vol.7 , pp. 207-221
    • Haris, P.I.1    Severcan, F.2
  • 13
    • 0012395825 scopus 로고    scopus 로고
    • Comparison of antioxidative activity among three types of prolamin subunits
    • Kawase S.I., Matsumura Y., Murakami H., Mori T. Comparison of antioxidative activity among three types of prolamin subunits. Journal of Cereal Science 1998, 28:33-41.
    • (1998) Journal of Cereal Science , vol.28 , pp. 33-41
    • Kawase, S.I.1    Matsumura, Y.2    Murakami, H.3    Mori, T.4
  • 14
    • 33846610587 scopus 로고    scopus 로고
    • Antioxidative activity and functional properties of protein hydrolysate of yellow stripe trevally (Selaroides leptolepis) as influenced by the degree of hydrolysis and enzyme type
    • Klompong V., Benjakul S., Kantachote D., Shahidi F. Antioxidative activity and functional properties of protein hydrolysate of yellow stripe trevally (Selaroides leptolepis) as influenced by the degree of hydrolysis and enzyme type. Food Chemistry 2007, 102:1317-1327.
    • (2007) Food Chemistry , vol.102 , pp. 1317-1327
    • Klompong, V.1    Benjakul, S.2    Kantachote, D.3    Shahidi, F.4
  • 15
    • 43449129718 scopus 로고    scopus 로고
    • Comparative study on antioxidative activity of yellow stripe trevally protein hydrolysate produced from alcalase and flavourzyme
    • Klompong V., Benjakul S., Kantachote D., Hayes K.D., Shahidi F. Comparative study on antioxidative activity of yellow stripe trevally protein hydrolysate produced from alcalase and flavourzyme. International Journal of Food Science & Technology 2008, 43:1019-1026.
    • (2008) International Journal of Food Science & Technology , vol.43 , pp. 1019-1026
    • Klompong, V.1    Benjakul, S.2    Kantachote, D.3    Hayes, K.D.4    Shahidi, F.5
  • 16
    • 33748431810 scopus 로고    scopus 로고
    • Antioxidant activity of zein hydrolysates in a liposome system and the possible mode of action
    • Kong B., Xiong Y.L. Antioxidant activity of zein hydrolysates in a liposome system and the possible mode of action. Journal of Agricultural and Food Chemistry 2006, 54:6059-6068.
    • (2006) Journal of Agricultural and Food Chemistry , vol.54 , pp. 6059-6068
    • Kong, B.1    Xiong, Y.L.2
  • 17
    • 0001589422 scopus 로고    scopus 로고
    • Some physicochemical and interfacial properties of native and acetylated legumin from faba beans (Vicia faba L)
    • Krause J.-P., Mothes R., Schwenke K.D. Some physicochemical and interfacial properties of native and acetylated legumin from faba beans (Vicia faba L). Journal of Agricultural and Food Chemistry 1996, 44:429-437.
    • (1996) Journal of Agricultural and Food Chemistry , vol.44 , pp. 429-437
    • Krause, J.-P.1    Mothes, R.2    Schwenke, K.D.3
  • 18
    • 0038761793 scopus 로고    scopus 로고
    • Structural and interaction properties of β-lactoglobulin as studied by FTIR spectroscopy
    • Lefevre T., Subirade M. Structural and interaction properties of β-lactoglobulin as studied by FTIR spectroscopy. International Journal of Food Science and Technology 1999, 34:419-428.
    • (1999) International Journal of Food Science and Technology , vol.34 , pp. 419-428
    • Lefevre, T.1    Subirade, M.2
  • 19
    • 46049116527 scopus 로고    scopus 로고
    • In vitro antioxidant activity of protein hydrolysates prepared from corn gluten meal
    • Li X.-X., Han L.-J., Chen L.-J. In vitro antioxidant activity of protein hydrolysates prepared from corn gluten meal. Journal of the Science of Food and Agriculture 2008, 88:1660-1666.
    • (2008) Journal of the Science of Food and Agriculture , vol.88 , pp. 1660-1666
    • Li, X.-X.1    Han, L.-J.2    Chen, L.-J.3
  • 20
    • 69249206712 scopus 로고    scopus 로고
    • Antioxidant activity and functional properties of porcine plasma protein hydrolysate as influenced by the degree of hydrolysis
    • Liu Q., Kong B., Xiong Y.L., Xia X. Antioxidant activity and functional properties of porcine plasma protein hydrolysate as influenced by the degree of hydrolysis. Food Chemistry 2010, 118:403-410.
    • (2010) Food Chemistry , vol.118 , pp. 403-410
    • Liu, Q.1    Kong, B.2    Xiong, Y.L.3    Xia, X.4
  • 21
    • 57249089073 scopus 로고    scopus 로고
    • An in-vitro investigation of selected biological activities of hydrolysed flaxseed (Linum usitatissimum L.) proteins
    • Marambe P.W.M.L.H.K., Shand P.J., Wanasundara J.P.D. An in-vitro investigation of selected biological activities of hydrolysed flaxseed (Linum usitatissimum L.) proteins. Journal of American Oil Chemists Society 2008, 85:1155-1164.
    • (2008) Journal of American Oil Chemists Society , vol.85 , pp. 1155-1164
    • Marambe, P.W.M.L.H.K.1    Shand, P.J.2    Wanasundara, J.P.D.3
  • 22
    • 0016272750 scopus 로고
    • Involvement of the superoxide anion radical in the autoxidation of pyrogallol and a convenient assay for superoxide dismutase
    • Marklund S., Marklund G. Involvement of the superoxide anion radical in the autoxidation of pyrogallol and a convenient assay for superoxide dismutase. European Journal of Biochemistry 1974, 47:469-474.
    • (1974) European Journal of Biochemistry , vol.47 , pp. 469-474
    • Marklund, S.1    Marklund, G.2
  • 23
    • 29244443998 scopus 로고    scopus 로고
    • Antioxidant properties of ultrafiltration-recovered soy protein fractions from industrial effluents and their hydrolysates
    • Moure A., Domínguez H., Parajo J.C. Antioxidant properties of ultrafiltration-recovered soy protein fractions from industrial effluents and their hydrolysates. Process Biochemistry 2006, 41:447-456.
    • (2006) Process Biochemistry , vol.41 , pp. 447-456
    • Moure, A.1    Domínguez, H.2    Parajo, J.C.3
  • 24
    • 76449100730 scopus 로고    scopus 로고
    • Structural and functional properties of heat-processed soybean flour: effect of proteolytic modification
    • Radha C., Prakash V. Structural and functional properties of heat-processed soybean flour: effect of proteolytic modification. Food Science and Technology International 2009, 15:453-463.
    • (2009) Food Science and Technology International , vol.15 , pp. 453-463
    • Radha, C.1    Prakash, V.2
  • 25
    • 23944469378 scopus 로고    scopus 로고
    • Purification and in vitro antioxidative effects of giant squid muscle peptides on free radical-mediated oxidative systems
    • Rajapakse N., Mendis E., Byun H.-G., Kim S.-K. Purification and in vitro antioxidative effects of giant squid muscle peptides on free radical-mediated oxidative systems. Journal of Nutritional Biochemistry 2005, 16:562-569.
    • (2005) Journal of Nutritional Biochemistry , vol.16 , pp. 562-569
    • Rajapakse, N.1    Mendis, E.2    Byun, H.-G.3    Kim, S.-K.4
  • 27
    • 0002427947 scopus 로고
    • Barley seed proteins
    • American Association of Cereal Chemists Inc., St. Paul, Minnesota, USA, A.W. MacGregor, R.S. Bhatty (Eds.)
    • Shewry P.R. Barley seed proteins. Barley: Chemistry and Technology 1993, 131-197. American Association of Cereal Chemists Inc., St. Paul, Minnesota, USA. A.W. MacGregor, R.S. Bhatty (Eds.).
    • (1993) Barley: Chemistry and Technology , pp. 131-197
    • Shewry, P.R.1
  • 28
    • 0034773313 scopus 로고    scopus 로고
    • Proteolytic degradation of cereal prolamins-the problem with proline
    • Simpson D.J. Proteolytic degradation of cereal prolamins-the problem with proline. Plant Science 2001, 161:825-838.
    • (2001) Plant Science , vol.161 , pp. 825-838
    • Simpson, D.J.1
  • 29
    • 0034121187 scopus 로고    scopus 로고
    • Molecular basis of celiac disease
    • Sollid L.M. Molecular basis of celiac disease. Annual Review of Immunology 2000, 18:53-81.
    • (2000) Annual Review of Immunology , vol.18 , pp. 53-81
    • Sollid, L.M.1
  • 30
    • 38849117102 scopus 로고    scopus 로고
    • Statistics Canada, Available at
    • Estimated production of field crops 2006, Statistics Canada, Available at. http://www.statcan.ca/daily/English/061005/d061005a.htm.
    • (2006) Estimated production of field crops
  • 31
    • 0027492164 scopus 로고
    • Determination of protein secondary structure by fourier transform infrared spectroscopy: a critical assessment
    • Surewicz W.K., Mantsch H.H., Chapman D. Determination of protein secondary structure by fourier transform infrared spectroscopy: a critical assessment. Biochemistry 1993, 32(2):389-394.
    • (1993) Biochemistry , vol.32 , Issue.2 , pp. 389-394
    • Surewicz, W.K.1    Mantsch, H.H.2    Chapman, D.3
  • 32
    • 55649086169 scopus 로고    scopus 로고
    • Transglutaminase-induced cross-linking of vicillin-rich kidney protein isolate: influence on functional properties and in vitro digestion
    • Tang C.-H., Sun X., Yin S.-W., Ma C.-Y. Transglutaminase-induced cross-linking of vicillin-rich kidney protein isolate: influence on functional properties and in vitro digestion. Food Research International 2008, 41:941-947.
    • (2008) Food Research International , vol.41 , pp. 941-947
    • Tang, C.-H.1    Sun, X.2    Yin, S.-W.3    Ma, C.-Y.4
  • 34
    • 77951275186 scopus 로고    scopus 로고
    • Antioxidant and angiotensin converting enzyme-inhibitory properties of a flaxseed protein-derived high fischer ratio peptide mixture
    • Udenigwe C.C., Aluko R.E. Antioxidant and angiotensin converting enzyme-inhibitory properties of a flaxseed protein-derived high fischer ratio peptide mixture. Journal of Agricultural and Food Chemistry 2010, 58:4762-4768.
    • (2010) Journal of Agricultural and Food Chemistry , vol.58 , pp. 4762-4768
    • Udenigwe, C.C.1    Aluko, R.E.2
  • 35
    • 54149118358 scopus 로고    scopus 로고
    • Grain fractionation technologies for cereal beta-glucan concentration
    • Vasanthan T., Temelli F. Grain fractionation technologies for cereal beta-glucan concentration. Food Research International 2008, 41:876-881.
    • (2008) Food Research International , vol.41 , pp. 876-881
    • Vasanthan, T.1    Temelli, F.2
  • 36
    • 78149300292 scopus 로고    scopus 로고
    • Functionality of barley proteins extracted and fractionated by alkaline and alcohol methods
    • Wang C., Tian Z., Chen L., Temelli F., Liu H., Wang Y. Functionality of barley proteins extracted and fractionated by alkaline and alcohol methods. Cereal Chemistry 2010, 87(6):597-606.
    • (2010) Cereal Chemistry , vol.87 , Issue.6 , pp. 597-606
    • Wang, C.1    Tian, Z.2    Chen, L.3    Temelli, F.4    Liu, H.5    Wang, Y.6
  • 37
    • 33748885488 scopus 로고    scopus 로고
    • Chemistry of gluten proteins
    • Wieser H. Chemistry of gluten proteins. Food Microbiology 2007, 24:115-119.
    • (2007) Food Microbiology , vol.24 , pp. 115-119
    • Wieser, H.1
  • 38
    • 1942470493 scopus 로고    scopus 로고
    • Relationships between solution properties of cereal β-glucans and physiological effects - a review
    • Wood P.J. Relationships between solution properties of cereal β-glucans and physiological effects - a review. Trends in Food Science and Technology 2002, 15:313-320.
    • (2002) Trends in Food Science and Technology , vol.15 , pp. 313-320
    • Wood, P.J.1
  • 40
    • 60149090291 scopus 로고    scopus 로고
    • Effect of degree of hydrolysis on the antioxidant activity of loach (Misgurnus anguillicaudatus) protein hydrolysates
    • You L., Zhao M., Cui C., Zhao H., Yang B. Effect of degree of hydrolysis on the antioxidant activity of loach (Misgurnus anguillicaudatus) protein hydrolysates. Innovative Food Science and Emerging Technologies 2009, 10:235-240.
    • (2009) Innovative Food Science and Emerging Technologies , vol.10 , pp. 235-240
    • You, L.1    Zhao, M.2    Cui, C.3    Zhao, H.4    Yang, B.5
  • 41
    • 74149087241 scopus 로고    scopus 로고
    • Changes in the antioxidant activity of loach (Misgurnus anguillicaudatus) protein hydrolysates during a simulated gastrointestinal digestion
    • You L., Zhao M., Regenstein J.M., Ren J. Changes in the antioxidant activity of loach (Misgurnus anguillicaudatus) protein hydrolysates during a simulated gastrointestinal digestion. Food Chemistry 2010, 120:810-816.
    • (2010) Food Chemistry , vol.120 , pp. 810-816
    • You, L.1    Zhao, M.2    Regenstein, J.M.3    Ren, J.4
  • 42
    • 70349916047 scopus 로고    scopus 로고
    • Antioxidant activities of the rice endosperm protein hydrolysate: identification of the active peptide
    • Zhang J., Zhang H., Wang L., Guo X., Wang X., Yao H. Antioxidant activities of the rice endosperm protein hydrolysate: identification of the active peptide. European Food Research and Technology 2009, 229:709-719.
    • (2009) European Food Research and Technology , vol.229 , pp. 709-719
    • Zhang, J.1    Zhang, H.2    Wang, L.3    Guo, X.4    Wang, X.5    Yao, H.6
  • 43
    • 43649092437 scopus 로고    scopus 로고
    • Reducing, radical scavenging, and chelation properties of in vitro digests of alcalase-treated zein hydrolysate
    • Zhu L., Chen J., Tang T., Xiong Y.L. Reducing, radical scavenging, and chelation properties of in vitro digests of alcalase-treated zein hydrolysate. Journal of Agricultural and Food Chemistry 2008, 56:2714-2721.
    • (2008) Journal of Agricultural and Food Chemistry , vol.56 , pp. 2714-2721
    • Zhu, L.1    Chen, J.2    Tang, T.3    Xiong, Y.L.4


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