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Volumn 70, Issue 1, 2005, Pages

Gel-forming ability and radical-scavenging activity of soy protein hydrolysate treated with transglutaminase

Author keywords

Gel forming ability; Peptide; Radical scavenging activity; Transglutaminase

Indexed keywords

GLYCINE MAX;

EID: 13844266970     PISSN: 00221147     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1365-2621.2005.tb09027.x     Document Type: Article
Times cited : (34)

References (43)
  • 1
    • 0018536145 scopus 로고
    • Determination of the degree of hydrolysis of food protein hydrolysates by trinitrobenzenesulfonic acid
    • Adler-Nissen J. 1979. Determination of the degree of hydrolysis of food protein hydrolysates by trinitrobenzenesulfonic acid. J Agric Food Chem 27:1256-62.
    • (1979) J Agric Food Chem , vol.27 , pp. 1256-1262
    • Adler-Nissen, J.1
  • 2
    • 0000186865 scopus 로고
    • Some fundamental aspects of food protein hydrolysis. A review of food protein hydrolysis. Methods in food protein hydrolysis
    • Adler-Nissen J, editor. London: Elsevier Applied Science Publishers
    • Adler-Nissen J. 1986. Some fundamental aspects of food protein hydrolysis. A review of food protein hydrolysis. Methods in food protein hydrolysis. In: Adler-Nissen J, editor. Enzymic hydrolysis of food proteins. London: Elsevier Applied Science Publishers. p 9-24, 110-31.
    • (1986) Enzymic Hydrolysis of Food Proteins , pp. 9-24
    • Adler-Nissen, J.1
  • 3
    • 0031805573 scopus 로고    scopus 로고
    • Heat-induced egg white gels as affected by pH
    • Akihiro H, Keiko T, Namio K, Glenn WF. 1998. Heat-induced egg white gels as affected by pH. J Food Sci 63(3):403-7.
    • (1998) J Food Sci , vol.63 , Issue.3 , pp. 403-407
    • Akihiro, H.1    Keiko, T.2    Namio, K.3    Glenn, W.F.4
  • 4
    • 0029056306 scopus 로고
    • Meta-analysis of the effects of soy protein intake on serum lipids
    • Anderson J, Johnston B, Cook-Newell M. 1995. Meta-analysis of the effects of soy protein intake on serum lipids. N Engl J Med 333(5):276-82.
    • (1995) N Engl J Med , vol.333 , Issue.5 , pp. 276-282
    • Anderson, J.1    Johnston, B.2    Cook-Newell, M.3
  • 5
    • 0034255689 scopus 로고    scopus 로고
    • Effect of transglutaminase treatment on the functional properties of native and chymotrypsin-digested soy protein
    • Babiker EE. 2000. Effect of transglutaminase treatment on the functional properties of native and chymotrypsin-digested soy protein. Food Chem 70:139-45.
    • (2000) Food Chem , vol.70 , pp. 139-145
    • Babiker, E.E.1
  • 6
    • 0030265397 scopus 로고    scopus 로고
    • Polymerisation of soy protein digests by microbial transglutaminase for improvement of the functional properties
    • Babiker EE, Khan MAS, Matsudomi N, Kato A. 1996a. Polymerisation of soy protein digests by microbial transglutaminase for improvement of the functional properties. Food Res Int 29(7):627-34.
    • (1996) Food Res Int , vol.29 , Issue.7 , pp. 627-634
    • Babiker, E.E.1    Khan, M.A.S.2    Matsudomi, N.3    Kato, A.4
  • 7
    • 0001286679 scopus 로고    scopus 로고
    • Improvement in the functional properties of gluten by protease digestion or acid hydrolysis followed by microbial transglutaminase treatment
    • Babiker EE, Naotoshi M, Akio K. 1996b. Improvement in the functional properties of gluten by protease digestion or acid hydrolysis followed by microbial transglutaminase treatment. J Agric Food Chem 44:3746-50.
    • (1996) J Agric Food Chem , vol.44 , pp. 3746-3750
    • Babiker, E.E.1    Naotoshi, M.2    Akio, K.3
  • 8
    • 0004880564 scopus 로고    scopus 로고
    • Antioxidant activity of tea and common vegetables
    • Cao G, Sofic E, Prior RL. 1996. Antioxidant activity of tea and common vegetables. J Agric Food Chem 44:3426-31.
    • (1996) J Agric Food Chem , vol.44 , pp. 3426-3431
    • Cao, G.1    Sofic, E.2    Prior, R.L.3
  • 9
    • 33751154733 scopus 로고
    • Structural analysis of antioxidative peptides from soybean b-conglycinin
    • Chen HM, Muramoto K, Yamauchi F. 1995. Structural analysis of antioxidative peptides from soybean b-conglycinin. J Agric Food Chem 43:574-8.
    • (1995) J Agric Food Chem , vol.43 , pp. 574-578
    • Chen, H.M.1    Muramoto, K.2    Yamauchi, F.3
  • 10
    • 2542545209 scopus 로고    scopus 로고
    • Antioxidant activity of designed peptides based on the antioxidative peptide isolated from digests of a soybean protein
    • Chen HM, Muramoto K, Yamauchi F, Fujimoto K, Nokihara K. 1996. Antioxidant activity of designed peptides based on the antioxidative peptide isolated from digests of a soybean protein. J Agric Food Chem 44:2619-23.
    • (1996) J Agric Food Chem , vol.44 , pp. 2619-2623
    • Chen, H.M.1    Muramoto, K.2    Yamauchi, F.3    Fujimoto, K.4    Nokihara, K.5
  • 11
    • 0002384554 scopus 로고    scopus 로고
    • Antioxidative properties of histidine-containing peptides designed from peptide fragments found in the digests of a soybean protein
    • Chen HM, Muramoto K, Yamauchi F, Fujimoto K, Nokihara K. 1998. Antioxidative properties of histidine-containing peptides designed from peptide fragments found in the digests of a soybean protein. J Agric Food Chem 46:49-53.
    • (1998) J Agric Food Chem , vol.46 , pp. 49-53
    • Chen, H.M.1    Muramoto, K.2    Yamauchi, F.3    Fujimoto, K.4    Nokihara, K.5
  • 12
    • 0002634895 scopus 로고
    • Proteins in solution and in membranes
    • Creighton TE, editor. New York: W.H. Freeman and Co.
    • Creighton TE. 1993. Proteins in solution and in membranes. In: Creighton TE, editor. Proteins. 2nd ed. New York: W.H. Freeman and Co. p 261-328.
    • (1993) Proteins. 2nd Ed. , pp. 261-328
    • Creighton, T.E.1
  • 13
    • 33748618420 scopus 로고    scopus 로고
    • Antioxidant chemistry: Reactivity and oxidation of dl-cysteine by some common oxidants
    • Darkwa J, Mundoma C, Simoyi RH. 1998. Antioxidant chemistry: reactivity and oxidation of dl-cysteine by some common oxidants. J Chem Soc Faraday Trans 94:1971-8.
    • (1998) J Chem Soc Faraday Trans , vol.94 , pp. 1971-1978
    • Darkwa, J.1    Mundoma, C.2    Simoyi, R.H.3
  • 14
    • 0001781763 scopus 로고
    • Texture and microstructure of soybean curd (tofu) as affected by different coagulants
    • DeMan JM, deMan L, Gupta S. 1986. Texture and microstructure of soybean curd (tofu) as affected by different coagulants. Food Microstruct 5:83-9.
    • (1986) Food Microstruct , vol.5 , pp. 83-89
    • DeMan, J.M.1    DeMan, L.2    Gupta, S.3
  • 15
    • 0141698725 scopus 로고    scopus 로고
    • Preparation of angiotensin I-converting enzyme inhibitory peptides from soybean protein by enzymatic hydrolysis
    • Fan JF, Saito M, Tatsumi E, Li LT. 2003. Preparation of angiotensin I-converting enzyme inhibitory peptides from soybean protein by enzymatic hydrolysis. Food Sci Technol Res 9 (3):254-6.
    • (2003) Food Sci Technol Res , vol.9 , Issue.3 , pp. 254-256
    • Fan, J.F.1    Saito, M.2    Tatsumi, E.3    Li, L.T.4
  • 16
    • 0001357362 scopus 로고
    • Influence of heating temperature on conformational changes of soybean proteins
    • Hashizume K, Watanabe T. 1979. Influence of heating temperature on conformational changes of soybean proteins. Agric Biol Chem 43:683-90.
    • (1979) Agric Biol Chem , vol.43 , pp. 683-690
    • Hashizume, K.1    Watanabe, T.2
  • 17
    • 22844454897 scopus 로고    scopus 로고
    • Inhibitory effect of proteins and their hydrolysates on the oxidation of triacylglycerols containing docosahexaenoic acids in emulsion
    • Hirose A, Miyashita K. 1999. Inhibitory effect of proteins and their hydrolysates on the oxidation of triacylglycerols containing docosahexaenoic acids in emulsion. J Jpn Soc Food Sci Technol 46:799-805.
    • (1999) J Jpn Soc Food Sci Technol , vol.46 , pp. 799-805
    • Hirose, A.1    Miyashita, K.2
  • 18
    • 13844250766 scopus 로고    scopus 로고
    • Properties of soybean 7S globulin and myosin polymerized by transglutaminase
    • in Chinese
    • Jiang B, Zhou HX. 2001. Properties of soybean 7S globulin and myosin polymerized by transglutaminase. J Wuxi Univ Light Indust 20(2):122-7 (in Chinese).
    • (2001) J Wuxi Univ Light Indust , vol.20 , Issue.2 , pp. 122-127
    • Jiang, B.1    Zhou, H.X.2
  • 19
    • 3743108414 scopus 로고
    • Gelation properties of lipid reduced, and calcium-reduced whey protein concentrates
    • Karleskind D, Laye I, Mei FI, Morr CV. 1995. Gelation properties of lipid reduced, and calcium-reduced whey protein concentrates. J Food Sci 60:731-7, 741.
    • (1995) J Food Sci , vol.60 , pp. 731-737
    • Karleskind, D.1    Laye, I.2    Mei, F.I.3    Morr, C.V.4
  • 21
    • 0000403060 scopus 로고
    • Rheological characteristics and gelation mechanism of tofu
    • Kohyama K, Sano Y, Doi E. 1995. Rheological characteristics and gelation mechanism of tofu. J Agric Food Chem 43:1808-12.
    • (1995) J Agric Food Chem , vol.43 , pp. 1808-1812
    • Kohyama, K.1    Sano, Y.2    Doi, E.3
  • 22
    • 0038397146 scopus 로고    scopus 로고
    • Food-derived bioactive peptides - Opportunities for designing future foods
    • Korhonen H, Pihlanto A. 2003. Food-derived bioactive peptides - opportunities for designing future foods. Curr Pharm Des 9(16):1297-308.
    • (2003) Curr Pharm des , vol.9 , Issue.16 , pp. 1297-1308
    • Korhonen, H.1    Pihlanto, A.2
  • 23
    • 0035531318 scopus 로고    scopus 로고
    • Transglutaminase: Its utilization in the food industry
    • Kuraishi C, Yamazaki K, Susa Y. 2001. Transglutaminase: its utilization in the food industry. Food Rev Int 17(2):221-46.
    • (2001) Food Rev Int , vol.17 , Issue.2 , pp. 221-246
    • Kuraishi, C.1    Yamazaki, K.2    Susa, Y.3
  • 24
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-5.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 25
    • 13844292925 scopus 로고    scopus 로고
    • Effects of heat denaturation of soybean protein on tofu-gel
    • in Chinese
    • Li LT, Wang LJ, Li ZG, Tatsumi E. 2002. Effects of heat denaturation of soybean protein on tofu-gel. J Chinese Cereals Oils Assn 17(1):1-4 (in Chinese).
    • (2002) J Chinese Cereals Oils Assn , vol.17 , Issue.1 , pp. 1-4
    • Li, L.T.1    Wang, L.J.2    Li, Z.G.3    Tatsumi, E.4
  • 26
    • 0000881255 scopus 로고
    • Enzymatic hydrolysis of casein: Effect of degree of hydrolysis on antigenicity and physical properties
    • Mahmoud MI, Malone WT, Cordle CT. 1992. Enzymatic hydrolysis of casein: effect of degree of hydrolysis on antigenicity and physical properties. J Food Sci 33:51-65.
    • (1992) J Food Sci , vol.33 , pp. 51-65
    • Mahmoud, M.I.1    Malone, W.T.2    Cordle, C.T.3
  • 27
    • 0000266715 scopus 로고
    • Network structure formation in thermally induced gelation of glycinin
    • Nakamura T, Utsumi S, Mori T. 1984. Network structure formation in thermally induced gelation of glycinin. J Agric Food Chem 32:349-52.
    • (1984) J Agric Food Chem , vol.32 , pp. 349-352
    • Nakamura, T.1    Utsumi, S.2    Mori, T.3
  • 28
    • 0001258097 scopus 로고
    • Interactions during heat-induced gelation in mixed system of soybean 7S and 11S globulins
    • Nakamura T, Utsumi S, Mori T. 1986. Interactions during heat-induced gelation in mixed system of soybean 7S and 11S globulins. Agric Biol Chem 50(10):2429-35.
    • (1986) Agric Biol Chem , vol.50 , Issue.10 , pp. 2429-2435
    • Nakamura, T.1    Utsumi, S.2    Mori, T.3
  • 29
    • 0024851912 scopus 로고
    • Polymerization of several proteins by Ca2+ - Independent transglutaminase derived from microorganisms
    • Nonaka M, Tanaka H, Okiyama A, Motoki M, Ando H, Unda K, Matsura A. 1989. Polymerization of several proteins by Ca2+ - independent transglutaminase derived from microorganisms. Agric Biol Chem 53:2619-23.
    • (1989) Agric Biol Chem , vol.53 , pp. 2619-2623
    • Nonaka, M.1    Tanaka, H.2    Okiyama, A.3    Motoki, M.4    Ando, H.5    Unda, K.6    Matsura, A.7
  • 30
    • 0013637299 scopus 로고
    • Spectrophotometric determination of sulfhydryl groups in soymilk using 2,29-dithiobis-(5-nitropyridine)
    • Obata A, Matsuura M, Fukushima D. 1989. Spectrophotometric determination of sulfhydryl groups in soymilk using 2,29-dithiobis-(5-nitropyridine). Nippon Shokuhin Kogyo Gakkaishi 36(9):707-11.
    • (1989) Nippon Shokuhin Kogyo Gakkaishi , vol.36 , Issue.9 , pp. 707-711
    • Obata, A.1    Matsuura, M.2    Fukushima, D.3
  • 31
    • 0036813306 scopus 로고    scopus 로고
    • Antioxidant activity of soy protein hydrolysates in liposomal system
    • Pena-Ramos EA, Xiong YL. 2002. Antioxidant activity of soy protein hydrolysates in liposomal system. J Food Sci 67:2952-6.
    • (2002) J Food Sci , vol.67 , pp. 2952-2956
    • Pena-Ramos, E.A.1    Xiong, Y.L.2
  • 32
    • 0028821534 scopus 로고    scopus 로고
    • Overview of proposed mechanisms for the hypocholesterolemic effect of soy
    • Potter SM. 1996. Overview of proposed mechanisms for the hypocholesterolemic effect of soy. J Nutr 125:606-11.
    • (1996) J Nutr , vol.125 , pp. 606-611
    • Potter, S.M.1
  • 33
    • 84987343068 scopus 로고
    • Conformational change in actomyosin from postspawned hake stored on ice
    • Roura S, Saavedra JP, Truco R, Crupkin M. 1992. Conformational change in actomyosin from postspawned hake stored on ice. J Food Sci 57:1109-11.
    • (1992) J Food Sci , vol.57 , pp. 1109-1111
    • Roura, S.1    Saavedra, J.P.2    Truco, R.3    Crupkin, M.4
  • 34
    • 0011543220 scopus 로고
    • Food processing characteristics of soybean proteins. Part II. Effect of sulfhydryl groups on physical properties of tofu-gel
    • Saio K, Kajiawa M, Watanabe T. 1971. Food processing characteristics of soybean proteins. Part II. Effect of sulfhydryl groups on physical properties of tofu-gel. Agric Biol Chem 35:890-8.
    • (1971) Agric Biol Chem , vol.35 , pp. 890-898
    • Saio, K.1    Kajiawa, M.2    Watanabe, T.3
  • 35
    • 0028139777 scopus 로고
    • Strength of protein gels prepared with microbiaal transglutaminase as related to reaction conditions
    • Sakamoto H, Kumazawa Y, Motoki M. 1994. Strength of protein gels prepared with microbiaal transglutaminase as related to reaction conditions. J Food Sci 59:866-71.
    • (1994) J Food Sci , vol.59 , pp. 866-871
    • Sakamoto, H.1    Kumazawa, Y.2    Motoki, M.3
  • 36
    • 84986465415 scopus 로고
    • Gel strength enhancement by addition of microbial transglutaminase during onshore surimi manufacture
    • Sakamoto H, Kumazawa Y, Toiguchi S, Serguro K, Soeda T, Motoki M. 1995. Gel strength enhancement by addition of microbial transglutaminase during onshore surimi manufacture. J Food Sci 60:300-4.
    • (1995) J Food Sci , vol.60 , pp. 300-304
    • Sakamoto, H.1    Kumazawa, Y.2    Toiguchi, S.3    Serguro, K.4    Soeda, T.5    Motoki, M.6
  • 37
    • 84986446950 scopus 로고
    • Microbial transglutaminase and ε-(Y-Glutamyl) lysine cross-links effects on elastic properties of kamaboko gels
    • Sergo K, Kumazawa Y, Ohtsuka T, Toiguchi S, Motoki M. 1995. Microbial transglutaminase and ε-(Y-Glutamyl) lysine cross-links effects on elastic properties of kamaboko gels. J Food Sci 60:305-11.
    • (1995) J Food Sci , vol.60 , pp. 305-311
    • Sergo, K.1    Kumazawa, Y.2    Ohtsuka, T.3    Toiguchi, S.4    Motoki, M.5
  • 38
    • 0141475387 scopus 로고    scopus 로고
    • Antioxidative activity
    • Shinohara K, Suzuki T, Kaminogaw S. editors. Tokyo, Japan: Korin
    • Suda I. 2000. Antioxidative activity. In: Shinohara K, Suzuki T, Kaminogaw S. editors. The methods of food functions analysis. Tokyo, Japan: Korin. p 218-20.
    • (2000) The Methods of Food Functions Analysis , pp. 218-220
    • Suda, I.1
  • 40
    • 0043128997 scopus 로고    scopus 로고
    • Reduction of paraquat-induced oxidative stress in rats by dietary soy peptide
    • Takenaka A, Annaka H, Kimura Y, Aoki H, Igarashi K. 2003. Reduction of paraquat-induced oxidative stress in rats by dietary soy peptide. Biosci Biotechnol Biochem 67(2):278-83.
    • (2003) Biosci Biotechnol Biochem , vol.67 , Issue.2 , pp. 278-283
    • Takenaka, A.1    Annaka, H.2    Kimura, Y.3    Aoki, H.4    Igarashi, K.5
  • 41
    • 33845471438 scopus 로고
    • Heat-induced interactions between soybean proteins: Preferential association of 11S basic subunits and bsubunits of 7S
    • Utsumi S, Damodaran S, Kinsella JE. 1984. Heat-induced interactions between soybean proteins: preferential association of 11S basic subunits and bsubunits of 7S. Agric. Food Chem 32:1406-12.
    • (1984) Agric Food Chem , vol.32 , pp. 1406-1412
    • Utsumi, S.1    Damodaran, S.2    Kinsella, J.E.3
  • 42
    • 85052678887 scopus 로고    scopus 로고
    • Structure-function relationships of soy proteins
    • Damodaran S, Paraf A, editors. New York: Marcel Dekker
    • Utsumi S, Matsumura Y, Mori T. 1997. Structure-function relationships of soy proteins. In: Damodaran S, Paraf A, editors. Food proteins and their applications. New York: Marcel Dekker. p 257-91.
    • (1997) Food Proteins and Their Applications , pp. 257-291
    • Utsumi, S.1    Matsumura, Y.2    Mori, T.3
  • 43
    • 0023662410 scopus 로고
    • The relative contributions of vitamin E, urate, ascorbate, and proteins to the total peroxyl radical-trapping antioxidant activity of human blood plasma
    • Wayner DDM, Burton GW, Ingold KU, Barclay LRC, Locke SL. 1987. The relative contributions of vitamin E, urate, ascorbate, and proteins to the total peroxyl radical-trapping antioxidant activity of human blood plasma. Biochim Biophys Acta 924:408-19.
    • (1987) Biochim Biophys Acta , vol.924 , pp. 408-419
    • Wayner, D.D.M.1    Burton, G.W.2    Ingold, K.U.3    Barclay, L.R.C.4    Locke, S.L.5


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