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Volumn 55, Issue , 2014, Pages 418-425

Effects of partial hydrolysis on structure and gelling properties of oat globular proteins

Author keywords

Mechanical properties; Oat protein; Partial hydrolysis; Thermal gelation; Water holding capacity

Indexed keywords

ALKALINE CONDITIONS; AMINO ACID ANALYSIS; EGG WHITE PROTEINS; ENVIRONMENTAL CONDITIONS; PARTIAL HYDROLYSIS; TEXTURAL PROFILE ANALYSIS; THERMAL GELATION; WATER HOLDING CAPACITY;

EID: 84890359526     PISSN: 09639969     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodres.2013.11.038     Document Type: Article
Times cited : (99)

References (52)
  • 1
    • 0018536145 scopus 로고
    • Determination of degree of hydrolysis of food protein hydrolysates by trinitrobenzenesulfonic acid
    • Adler-Nissen J. Determination of degree of hydrolysis of food protein hydrolysates by trinitrobenzenesulfonic acid. Journal of Agricultural and Food Chemistry 1979, 6:1256-1262.
    • (1979) Journal of Agricultural and Food Chemistry , vol.6 , pp. 1256-1262
    • Adler-Nissen, J.1
  • 3
    • 79952674994 scopus 로고    scopus 로고
    • Influence of carbon dioxide on the activity of chicken egg with lysozyme
    • Banerjee P., Keener K.M., Lukito V.D. Influence of carbon dioxide on the activity of chicken egg with lysozyme. Poultry Science 2011, 90(4):889-895.
    • (2011) Poultry Science , vol.90 , Issue.4 , pp. 889-895
    • Banerjee, P.1    Keener, K.M.2    Lukito, V.D.3
  • 5
    • 0028180088 scopus 로고
    • Oat beta-glucan reduces blood cholesterol concentration in hypercholesterolemic subjects
    • Braaten J.T., Wood P.J., Scott F.W. Oat beta-glucan reduces blood cholesterol concentration in hypercholesterolemic subjects. European Journal of Clinical Nutrition 1994, 48(7):465-474.
    • (1994) European Journal of Clinical Nutrition , vol.48 , Issue.7 , pp. 465-474
    • Braaten, J.T.1    Wood, P.J.2    Scott, F.W.3
  • 7
    • 0034009150 scopus 로고    scopus 로고
    • Optimizing preparation conditions for heat-denatured whey protein solutions to be used as cold-gelling ingredients
    • Bryant C.M., McClements D.J. Optimizing preparation conditions for heat-denatured whey protein solutions to be used as cold-gelling ingredients. Journal of Food Science 2000, 65:259-263.
    • (2000) Journal of Food Science , vol.65 , pp. 259-263
    • Bryant, C.M.1    McClements, D.J.2
  • 9
    • 0036328703 scopus 로고    scopus 로고
    • Influence of NaCl on optical properties, large-strain rheology and water holding capacity of heat induced whey protein isolate gels
    • Chantrapornchai W., McClements D.J. Influence of NaCl on optical properties, large-strain rheology and water holding capacity of heat induced whey protein isolate gels. Food Hydrocolloids 2002, 16:467-476.
    • (2002) Food Hydrocolloids , vol.16 , pp. 467-476
    • Chantrapornchai, W.1    McClements, D.J.2
  • 10
    • 84863655277 scopus 로고    scopus 로고
    • Effects of protein hydrolysis on pasting properties of wheat flour
    • Chen J., Tian J., Zheng F., Li X., Zhao Y., Gao X., et al. Effects of protein hydrolysis on pasting properties of wheat flour. Starch-Starke 2012, 64:524-530.
    • (2012) Starch-Starke , vol.64 , pp. 524-530
    • Chen, J.1    Tian, J.2    Zheng, F.3    Li, X.4    Zhao, Y.5    Gao, X.6
  • 11
    • 79961031305 scopus 로고    scopus 로고
    • Food protein functionality: A comprehensive approach
    • Foegeding E.A., Davis J.P. Food protein functionality: A comprehensive approach. Food Hydrocolloids 2011, 25:1853-1864.
    • (2011) Food Hydrocolloids , vol.25 , pp. 1853-1864
    • Foegeding, E.A.1    Davis, J.P.2
  • 13
    • 0000081134 scopus 로고    scopus 로고
    • Effect of hen egg production and protein composition on textural properties of egg albumen gels
    • Hammershøj M., Larsen L.B. Effect of hen egg production and protein composition on textural properties of egg albumen gels. Journal of Texture Studies 2001, 32(2):105-129.
    • (2001) Journal of Texture Studies , vol.32 , Issue.2 , pp. 105-129
    • Hammershøj, M.1    Larsen, L.B.2
  • 15
    • 79957974656 scopus 로고    scopus 로고
    • Limited hydrolysis of two soybean protein products with trypsin and neutrase and the impacts on their solubility, gelation and fat absorption capacity
    • Hou Y., Zhao X.-H. Limited hydrolysis of two soybean protein products with trypsin and neutrase and the impacts on their solubility, gelation and fat absorption capacity. Biotechnology 2011, 10(2):190-196.
    • (2011) Biotechnology , vol.10 , Issue.2 , pp. 190-196
    • Hou, Y.1    Zhao, X.-H.2
  • 16
    • 84890424548 scopus 로고    scopus 로고
    • Converting oats to high-fiber products for use in functional foods
    • CRC, Woodhead, Cambridge, B.R. Hamaker (Ed.)
    • Inglett G.E., Lee S., Stevenson D.G. Converting oats to high-fiber products for use in functional foods. Technology of functional cereal products 2008, 476-494. CRC, Woodhead, Cambridge. B.R. Hamaker (Ed.).
    • (2008) Technology of functional cereal products , pp. 476-494
    • Inglett, G.E.1    Lee, S.2    Stevenson, D.G.3
  • 17
    • 84861424424 scopus 로고    scopus 로고
    • Proteins in Oats; their synthesis and changes during germination: A review
    • Klose C., Arendt E.K. Proteins in Oats; their synthesis and changes during germination: A review. Critical Reviews in Food Science and Nutrition 2012, 52:629-639.
    • (2012) Critical Reviews in Food Science and Nutrition , vol.52 , pp. 629-639
    • Klose, C.1    Arendt, E.K.2
  • 18
    • 45549103755 scopus 로고    scopus 로고
    • Identification of strong aggregating regions in soy glycinin upon enzymatic hydrolysis
    • Kuipers B.J., Gruppen H. Identification of strong aggregating regions in soy glycinin upon enzymatic hydrolysis. Journal of Agricultural and Food Chemistry 2008, 56:3818-3827.
    • (2008) Journal of Agricultural and Food Chemistry , vol.56 , pp. 3818-3827
    • Kuipers, B.J.1    Gruppen, H.2
  • 19
    • 34247184100 scopus 로고    scopus 로고
    • Rheological properties of soy hydrolysates obtained from limited enzymatic hydrolysis
    • Lamsal B.P., Jung S., Johnson L. Rheological properties of soy hydrolysates obtained from limited enzymatic hydrolysis. LWT -Food Science and Technology 2007, 40:1215-1223.
    • (2007) LWT -Food Science and Technology , vol.40 , pp. 1215-1223
    • Lamsal, B.P.1    Jung, S.2    Johnson, L.3
  • 20
    • 0034578634 scopus 로고    scopus 로고
    • Molecular difference in the formation and structure of fine-stranded and particulate beta lactoglobulin gels
    • Lefèvre T., Subirade M. Molecular difference in the formation and structure of fine-stranded and particulate beta lactoglobulin gels. Biopolymers 2000, 54:578-586.
    • (2000) Biopolymers , vol.54 , pp. 578-586
    • Lefèvre, T.1    Subirade, M.2
  • 22
    • 0000267995 scopus 로고
    • Functional properties of acylated oat protein
    • Ma C.-Y. Functional properties of acylated oat protein. Journal of Food Science 1984, 49:1128-1131.
    • (1984) Journal of Food Science , vol.49 , pp. 1128-1131
    • Ma, C.-Y.1
  • 23
    • 0039801807 scopus 로고
    • Functional properties of oat concentrate treated with linoleate or trypsin
    • Ma C.-Y. Functional properties of oat concentrate treated with linoleate or trypsin. Journal Canadian Institute of Food Science and Technology 1985, 18:79-84.
    • (1985) Journal Canadian Institute of Food Science and Technology , vol.18 , pp. 79-84
    • Ma, C.-Y.1
  • 24
    • 0000299937 scopus 로고
    • Thermal coagulation of oat globulin
    • Ma C.-Y., Harwalkar V.R. Thermal coagulation of oat globulin. Cereal Chemistry 1987, 64:212-218.
    • (1987) Cereal Chemistry , vol.64 , pp. 212-218
    • Ma, C.-Y.1    Harwalkar, V.R.2
  • 26
    • 0037882040 scopus 로고    scopus 로고
    • Study of thermal aggregation and gelation of oat globulin by Raman spectroscopy
    • Ma C.-Y., Rout M.K., Phillips D.L. Study of thermal aggregation and gelation of oat globulin by Raman spectroscopy. Spectroscopy 2003, 17:417-428.
    • (2003) Spectroscopy , vol.17 , pp. 417-428
    • Ma, C.-Y.1    Rout, M.K.2    Phillips, D.L.3
  • 27
    • 84890388777 scopus 로고
    • Functional properties of oat proteins modified by acylation, trypsin hydrolysis or linoleate treatment
    • Ma C.-Y., Wood D.F. Functional properties of oat proteins modified by acylation, trypsin hydrolysis or linoleate treatment. Journal of the American Oil Chemists Society 1986, 63:447-447.
    • (1986) Journal of the American Oil Chemists Society , vol.63 , pp. 447-447
    • Ma, C.-Y.1    Wood, D.F.2
  • 28
    • 0023597146 scopus 로고
    • Functional properties of oat protein modified by acylation, trypsin hydrolysis or linoleate treatment
    • Ma C.-Y., Wood D.F. Functional properties of oat protein modified by acylation, trypsin hydrolysis or linoleate treatment. Journal of the American Oil Chemists Society 1987, 64:1726-1731.
    • (1987) Journal of the American Oil Chemists Society , vol.64 , pp. 1726-1731
    • Ma, C.-Y.1    Wood, D.F.2
  • 29
    • 84951665692 scopus 로고
    • Enzyme-modified proteins from corn gluten meal: Preparation and functional properties
    • Mannheim A., Cheryan M. Enzyme-modified proteins from corn gluten meal: Preparation and functional properties. Journal of the American Oil Chemists Society 1992, 69:1163-1169.
    • (1992) Journal of the American Oil Chemists Society , vol.69 , pp. 1163-1169
    • Mannheim, A.1    Cheryan, M.2
  • 30
    • 0035546753 scopus 로고    scopus 로고
    • Water holding capacity and microstucture of gellan gels
    • Mao R., Tang J., Swanson B. Water holding capacity and microstucture of gellan gels. Carbohydrate Polymers 2001, 46(4):356-371.
    • (2001) Carbohydrate Polymers , vol.46 , Issue.4 , pp. 356-371
    • Mao, R.1    Tang, J.2    Swanson, B.3
  • 31
    • 57249089073 scopus 로고    scopus 로고
    • An in-vitro investigation of selected biological activities of hydrolysed flaxseed (Linum usitatissimum L.) proteins
    • Marambe P., Shand P., Wanasundara J. An in-vitro investigation of selected biological activities of hydrolysed flaxseed (Linum usitatissimum L.) proteins. Journal of the American Oil Chemists Society 2008, 85:1155-1164.
    • (2008) Journal of the American Oil Chemists Society , vol.85 , pp. 1155-1164
    • Marambe, P.1    Shand, P.2    Wanasundara, J.3
  • 34
    • 0001419587 scopus 로고
    • Mercaptoethanol, N-ethylmaleimide, propylene glycol and urea effects on rheological properties of thermally induced β-lactoglobulin gels at alkaline pH
    • Mulvihill D.M., Rector D., Kinsella J.E. Mercaptoethanol, N-ethylmaleimide, propylene glycol and urea effects on rheological properties of thermally induced β-lactoglobulin gels at alkaline pH. Journal of Food Science 1991, 56(5):1338-1341.
    • (1991) Journal of Food Science , vol.56 , Issue.5 , pp. 1338-1341
    • Mulvihill, D.M.1    Rector, D.2    Kinsella, J.E.3
  • 35
    • 33846570491 scopus 로고    scopus 로고
    • The effect of limited proteolysis on canola protein gelation
    • Pinterits A., Arntfield S.D. The effect of limited proteolysis on canola protein gelation. Food Chemistry 2007, 102:1337-1343.
    • (2007) Food Chemistry , vol.102 , pp. 1337-1343
    • Pinterits, A.1    Arntfield, S.D.2
  • 36
    • 0021774163 scopus 로고
    • Shape, symmetry, hydration and secondary structure of the legumin from Vicia faba in solution
    • Plietz P., Zirwer D., Schlesier B., Gast K., Damaschun G. Shape, symmetry, hydration and secondary structure of the legumin from Vicia faba in solution. Biochimica et Biophysica Acta 1984, 784:140-146.
    • (1984) Biochimica et Biophysica Acta , vol.784 , pp. 140-146
    • Plietz, P.1    Zirwer, D.2    Schlesier, B.3    Gast, K.4    Damaschun, G.5
  • 37
    • 0030342874 scopus 로고    scopus 로고
    • Instrumental texture profile analysis with particular reference to gelled systems
    • Pons M., Fiszman S.M. Instrumental texture profile analysis with particular reference to gelled systems. Journal of Texture Studies 1996, 27:597-624.
    • (1996) Journal of Texture Studies , vol.27 , pp. 597-624
    • Pons, M.1    Fiszman, S.M.2
  • 38
    • 0343252706 scopus 로고
    • Total solubilization of groat proteins in high protein oat (Avena sativa L. cv. Hinoat): Evidence that glutelins are a minor component
    • Robert L.S., Nozzolillo C., Cudjoe A., Altosaar I. Total solubilization of groat proteins in high protein oat (Avena sativa L. cv. Hinoat): Evidence that glutelins are a minor component. Journal Canadian Institute of Food Science and Technology 1983, 16(3):196-200.
    • (1983) Journal Canadian Institute of Food Science and Technology , vol.16 , Issue.3 , pp. 196-200
    • Robert, L.S.1    Nozzolillo, C.2    Cudjoe, A.3    Altosaar, I.4
  • 39
    • 0030950745 scopus 로고    scopus 로고
    • Factors affecting the gelation properties of hydrolyzed sunflower proteins
    • Sanchez A.C., Burgos J. Factors affecting the gelation properties of hydrolyzed sunflower proteins. Journal of Food Science 1997, 62(2):284-288.
    • (1997) Journal of Food Science , vol.62 , Issue.2 , pp. 284-288
    • Sanchez, A.C.1    Burgos, J.2
  • 41
    • 84974224136 scopus 로고
    • Application of the plastein reaction to caseins and skim milk powder. I. Protein hydrolysis and plastein formation
    • Sukan G., Andrews A.T. Application of the plastein reaction to caseins and skim milk powder. I. Protein hydrolysis and plastein formation. Journal of Dairy Research 1982, 49:265-278.
    • (1982) Journal of Dairy Research , vol.49 , pp. 265-278
    • Sukan, G.1    Andrews, A.T.2
  • 42
    • 79955466817 scopus 로고    scopus 로고
    • Dynamic oscillatory rheological measurements and thermal properties of pea protein extracted by salt: Effect of pH and NaCl
    • Sun X.D., Arntfield S.D. Dynamic oscillatory rheological measurements and thermal properties of pea protein extracted by salt: Effect of pH and NaCl. Journal of Food Engineering 2011, 105:577-582.
    • (2011) Journal of Food Engineering , vol.105 , pp. 577-582
    • Sun, X.D.1    Arntfield, S.D.2
  • 43
    • 0026601661 scopus 로고
    • Isolation and amino acid sequence of a glutamic acid specific endopeptidase from Bacillus licheniformis
    • Svendsen I., Breddam K. Isolation and amino acid sequence of a glutamic acid specific endopeptidase from Bacillus licheniformis. European Journal of Biochemistry 1992, 204:164-171.
    • (1992) European Journal of Biochemistry , vol.204 , pp. 164-171
    • Svendsen, I.1    Breddam, K.2
  • 45
    • 0028073116 scopus 로고
    • Effect of dose and modification of viscous properties of oat gum on plasma glucose and insulin following an oral glucose load
    • Wood P.J., Scott J.T., Riedel K.D., Wolynetz M.S., Collins M.W. Effect of dose and modification of viscous properties of oat gum on plasma glucose and insulin following an oral glucose load. The British Journal of Nutrition 1994, 72(5):731-743.
    • (1994) The British Journal of Nutrition , vol.72 , Issue.5 , pp. 731-743
    • Wood, P.J.1    Scott, J.T.2    Riedel, K.D.3    Wolynetz, M.S.4    Collins, M.W.5
  • 46
    • 79960699367 scopus 로고    scopus 로고
    • Effects of oxidative modification on thermal aggregation and gel properties of soy protein by peroxyl radicals
    • Wu W., Hua Y., Lin O., Xiao H. Effects of oxidative modification on thermal aggregation and gel properties of soy protein by peroxyl radicals. International Journal of Food Science and Technology 2011, 46:1891-1897.
    • (2011) International Journal of Food Science and Technology , vol.46 , pp. 1891-1897
    • Wu, W.1    Hua, Y.2    Lin, O.3    Xiao, H.4
  • 47
    • 0542391532 scopus 로고
    • Protein isolate from high-protein oats: Preparation composition and properties
    • Wu V., Sexson K.R., Cluskey J.E., Inglett G.E. Protein isolate from high-protein oats: Preparation composition and properties. Journal of Food Science 1977, 42(5):1383-1386.
    • (1977) Journal of Food Science , vol.42 , Issue.5 , pp. 1383-1386
    • Wu, V.1    Sexson, K.R.2    Cluskey, J.E.3    Inglett, G.E.4
  • 48
    • 0037226332 scopus 로고    scopus 로고
    • Properties of gels from whey protein concentrate and honey at different pH
    • Yamul D.K., Lupano C.E. Properties of gels from whey protein concentrate and honey at different pH. Food Research International 2003, 36:25-33.
    • (2003) Food Research International , vol.36 , pp. 25-33
    • Yamul, D.K.1    Lupano, C.E.2
  • 49
    • 79957540693 scopus 로고    scopus 로고
    • Production of physicochemical properties of rice bran protein isolates prepared with autoclaving and enzymatic hydrolysis
    • Yeom H.-J., Lee E.-H., Ha M.-S., Ha S.-D., Bae D.-H. Production of physicochemical properties of rice bran protein isolates prepared with autoclaving and enzymatic hydrolysis. Journal of Korean Society for Applied Biological Chemistry 2010, 53(1):62-70.
    • (2010) Journal of Korean Society for Applied Biological Chemistry , vol.53 , Issue.1 , pp. 62-70
    • Yeom, H.-J.1    Lee, E.-H.2    Ha, M.-S.3    Ha, S.-D.4    Bae, D.-H.5
  • 50
    • 34548487814 scopus 로고    scopus 로고
    • Effects of limited enzymatic hydrolysis with trypsin on the functional properties of hemp (Cannabis sativa L.) protein isolate
    • Yin S.-W., Tang C.-H., Cao J.-S., Hu E.-K., Wen Q.-B., Yang X.-Q. Effects of limited enzymatic hydrolysis with trypsin on the functional properties of hemp (Cannabis sativa L.) protein isolate. Food Chemistry 2008, 106:1004-1013.
    • (2008) Food Chemistry , vol.106 , pp. 1004-1013
    • Yin, S.-W.1    Tang, C.-H.2    Cao, J.-S.3    Hu, E.-K.4    Wen, Q.-B.5    Yang, X.-Q.6
  • 51
    • 33847788038 scopus 로고    scopus 로고
    • Texture profile of Tufu as affected by Instron parameters and sample preparation, and correlations of Instron hardness and springines with sensory scores
    • Yuan S., Chang S. Texture profile of Tufu as affected by Instron parameters and sample preparation, and correlations of Instron hardness and springines with sensory scores. Journal of Food Science 2007, 72(2):136-144.
    • (2007) Journal of Food Science , vol.72 , Issue.2 , pp. 136-144
    • Yuan, S.1    Chang, S.2
  • 52
    • 79953203868 scopus 로고    scopus 로고
    • Enzymatic hydrolysis and their effects on conformational and functional properties of peanut protein isolate
    • Zhao G., Liu Y., Zhao M., Ren J., Yang B. Enzymatic hydrolysis and their effects on conformational and functional properties of peanut protein isolate. Food Chemistry 2011, 127:1438-1443.
    • (2011) Food Chemistry , vol.127 , pp. 1438-1443
    • Zhao, G.1    Liu, Y.2    Zhao, M.3    Ren, J.4    Yang, B.5


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