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Volumn 85, Issue 1, 2008, Pages 59-64

Effect of transglutaminase on protein electrophoretic pattern of rice, soybean, and rice-soybean blends

Author keywords

[No Author keywords available]

Indexed keywords

AGGREGATES; ENZYME ACTIVITY; SULFUR COMPOUNDS;

EID: 38549170946     PISSN: 00090352     EISSN: None     Source Type: Journal    
DOI: 10.1094/CCHEM-85-1-0059     Document Type: Article
Times cited : (29)

References (36)
  • 1
    • 85153545437 scopus 로고    scopus 로고
    • AACC International. 2000. Approved Methods of the American Association of Cereal Chemists, 10th Ed. Methods 08-01, 30-25, 44-19, and 46-13. The Association: St. Paul, MN.
    • AACC International. 2000. Approved Methods of the American Association of Cereal Chemists, 10th Ed. Methods 08-01, 30-25, 44-19, and 46-13. The Association: St. Paul, MN.
  • 2
    • 84907421537 scopus 로고
    • Electrophoretic, solubility, and functional-properties of commercial soy protein isolates
    • Arrese, E. L., Sorgentini, D. A., Wagner, J. R., and Añon, M. C. 1991. Electrophoretic, solubility, and functional-properties of commercial soy protein isolates. J. Agric. Food Chem. 39:1029-1032.
    • (1991) J. Agric. Food Chem , vol.39 , pp. 1029-1032
    • Arrese, E.L.1    Sorgentini, D.A.2    Wagner, J.R.3    Añon, M.C.4
  • 3
    • 0034255689 scopus 로고    scopus 로고
    • Effect of transglutaminase treatment on the functional properties of native and chymotrypsin-digested soy protein
    • Babiker, E. E. 2000. Effect of transglutaminase treatment on the functional properties of native and chymotrypsin-digested soy protein. Food Chem. 70:139-145.
    • (2000) Food Chem , vol.70 , pp. 139-145
    • Babiker, E.E.1
  • 4
    • 0036751964 scopus 로고    scopus 로고
    • Effects of transglutaminase on SDS-PAGE patterns of wheat, soy, and barley proteins and their blends
    • Basman, A., Koksel, H., and Ng, P. K. W. 2002. Effects of transglutaminase on SDS-PAGE patterns of wheat, soy, and barley proteins and their blends. J. Food Sci. 67:2654-2658.
    • (2002) J. Food Sci , vol.67 , pp. 2654-2658
    • Basman, A.1    Koksel, H.2    Ng, P.K.W.3
  • 5
    • 22144442069 scopus 로고    scopus 로고
    • Microbial transglutaminase as a tool to restore the functionality of gluten from insect-damaged wheat
    • Bonet, A., Caballero, P. A., Gómez, M., and Rosell, C. M. 2005. Microbial transglutaminase as a tool to restore the functionality of gluten from insect-damaged wheat. Cereal Chem. 82:425-430.
    • (2005) Cereal Chem , vol.82 , pp. 425-430
    • Bonet, A.1    Caballero, P.A.2    Gómez, M.3    Rosell, C.M.4
  • 6
    • 33845188023 scopus 로고    scopus 로고
    • Formation of homopolymers and heteropolymers between wheat flour and several protein sources by transglutaminase catalyzed crosslinking
    • Bonet, A., Blaszczak, W., and Rosell, C. M. 2006. Formation of homopolymers and heteropolymers between wheat flour and several protein sources by transglutaminase catalyzed crosslinking. Cereal Chem. 83:655-662.
    • (2006) Cereal Chem , vol.83 , pp. 655-662
    • Bonet, A.1    Blaszczak, W.2    Rosell, C.M.3
  • 7
    • 19344375877 scopus 로고    scopus 로고
    • Effect of microbial transglutaminase on the rheological and thermal properties of insect damaged wheat flour
    • Caballero, P. A., Bonet, A., Rosell, C. M., and Gómez, M. 2005. Effect of microbial transglutaminase on the rheological and thermal properties of insect damaged wheat flour. J. Cereal Sci. 42:93-100.
    • (2005) J. Cereal Sci , vol.42 , pp. 93-100
    • Caballero, P.A.1    Bonet, A.2    Rosell, C.M.3    Gómez, M.4
  • 8
    • 6644220102 scopus 로고
    • Changes in salt-soluble proteins of rice during grain development
    • Cagampang, G. B., Perdon, A. A., and Juliano, B. O. 1976. Changes in salt-soluble proteins of rice during grain development. Phytochemistry 15:1425-1430.
    • (1976) Phytochemistry , vol.15 , pp. 1425-1430
    • Cagampang, G.B.1    Perdon, A.A.2    Juliano, B.O.3
  • 9
    • 0342615061 scopus 로고    scopus 로고
    • Effect of frying various legumes under optimum conditions on amino acids, in vitro protein digestibility, phytate and oligosaccharides
    • El-Moniem, G. M. A., Honke, J., and Bednarska, A. 2000. Effect of frying various legumes under optimum conditions on amino acids, in vitro protein digestibility, phytate and oligosaccharides. J. Sci. Food Agric. 80:57-62.
    • (2000) J. Sci. Food Agric , vol.80 , pp. 57-62
    • El-Moniem, G.M.A.1    Honke, J.2    Bednarska, A.3
  • 10
    • 13844266970 scopus 로고    scopus 로고
    • Gel-forming ability and radical-scavenging activity of soy protein hydrolysate treated with transglutaminase
    • Fan, J., Saito, M., Yanyan, Z., Szesze, T., Wang, L., Tatsumi, E., and Li, L. 2005. Gel-forming ability and radical-scavenging activity of soy protein hydrolysate treated with transglutaminase. J. Food Sci. 70:C87-C92.
    • (2005) J. Food Sci , vol.70
    • Fan, J.1    Saito, M.2    Yanyan, Z.3    Szesze, T.4    Wang, L.5    Tatsumi, E.6    Li, L.7
  • 12
    • 1642271550 scopus 로고    scopus 로고
    • Functionality of rice flour modified with a microbial transglutaminase
    • Gujral, H. S., and Rosell, C. M. 2004. Functionality of rice flour modified with a microbial transglutaminase. J. Cereal Sci. 39:225-230.
    • (2004) J. Cereal Sci , vol.39 , pp. 225-230
    • Gujral, H.S.1    Rosell, C.M.2
  • 13
    • 0038792398 scopus 로고    scopus 로고
    • Effect of cyclodextrin glycoxyl transferase on dough rheology and bread quality from rice flour
    • Gujral, H. S., Guardiola, I., Carbonell, J. V., and Rosell, C. M. 2003a. Effect of cyclodextrin glycoxyl transferase on dough rheology and bread quality from rice flour. J. Agric. Food Chem. 51:3814-3818.
    • (2003) J. Agric. Food Chem , vol.51 , pp. 3814-3818
    • Gujral, H.S.1    Guardiola, I.2    Carbonell, J.V.3    Rosell, C.M.4
  • 14
    • 0242525766 scopus 로고    scopus 로고
    • Starch hydrolyzing enzymes for retarding the staling of rice bread
    • Gujral, H. S., Haros, M., and Rosell, C. M. 2003b. Starch hydrolyzing enzymes for retarding the staling of rice bread. Cereal Chem. 80:750-754.
    • (2003) Cereal Chem , vol.80 , pp. 750-754
    • Gujral, H.S.1    Haros, M.2    Rosell, C.M.3
  • 15
    • 0005629170 scopus 로고
    • Rice cultivar identification by high-performance liquid chromatography of endosperm proteins
    • Huebner, F. R., Bietz, J. A., Webb, B. D., and Juliano, B. O. 1990. Rice cultivar identification by high-performance liquid chromatography of endosperm proteins. Cereal Chem. 67:129-135.
    • (1990) Cereal Chem , vol.67 , pp. 129-135
    • Huebner, F.R.1    Bietz, J.A.2    Webb, B.D.3    Juliano, B.O.4
  • 16
    • 84954936295 scopus 로고
    • Crosslinking of soybean 7S and 11S proteins by transglutaminase
    • Ikura, K., Kometani, T., Sasaki, R., and Chiba, H. 1980. Crosslinking of soybean 7S and 11S proteins by transglutaminase. Agric. Biol. Chem. 44:2979-2984.
    • (1980) Agric. Biol. Chem , vol.44 , pp. 2979-2984
    • Ikura, K.1    Kometani, T.2    Sasaki, R.3    Chiba, H.4
  • 17
    • 28944431636 scopus 로고    scopus 로고
    • Genetic variation of glutclin acidic subunit polypeptides in Bangladesh rice genetic resources
    • Jahan, M. S., Uemura, Y., Kumamaru, T., Hamid, A., and Satoh, H. 2005. Genetic variation of glutclin acidic subunit polypeptides in Bangladesh rice genetic resources. Genetic Res. Crop Evol. 52:977-987.
    • (2005) Genetic Res. Crop Evol , vol.52 , pp. 977-987
    • Jahan, M.S.1    Uemura, Y.2    Kumamaru, T.3    Hamid, A.4    Satoh, H.5
  • 18
    • 0034997960 scopus 로고    scopus 로고
    • Extraction, denaturation and hydrophobic properties of rice flour proteins
    • Ju, Z. Y., Hettiarachchy, N. S., and Rath, N. 2001. Extraction, denaturation and hydrophobic properties of rice flour proteins. J. Food Sci. 66:229-232.
    • (2001) J. Food Sci , vol.66 , pp. 229-232
    • Ju, Z.Y.1    Hettiarachchy, N.S.2    Rath, N.3
  • 19
    • 0001736464 scopus 로고
    • Use of multistacking gels in sodium dodecyl sulfate-polyacrylamide gel-electrophoresis to reveal polydispersity, aggregation, and disaggregation of the glutenin protein-fraction
    • Khan, K., and Huckle, L. 1992. Use of multistacking gels in sodium dodecyl sulfate-polyacrylamide gel-electrophoresis to reveal polydispersity, aggregation, and disaggregation of the glutenin protein-fraction. Cereal Chem. 69:686-688.
    • (1992) Cereal Chem , vol.69 , pp. 686-688
    • Khan, K.1    Huckle, L.2
  • 20
    • 0000414415 scopus 로고
    • Structural relationships among the rice glutelin polypeptides
    • Krishnan, H. B., and Okita, T. W. 1986. Structural relationships among the rice glutelin polypeptides. Plant Physiol. 81:748-753.
    • (1986) Plant Physiol , vol.81 , pp. 748-753
    • Krishnan, H.B.1    Okita, T.W.2
  • 21
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of head of bacteriophage-T4
    • Luemmli, U. K. 1970. Cleavage of structural proteins during assembly of head of bacteriophage-T4. Nature. 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Luemmli, U.K.1
  • 22
    • 31844438599 scopus 로고    scopus 로고
    • Improved functional properties for soy-wheat doughs due to modification of the size distribution of polymeric proteins
    • Maforimbo, E., Skurray, G., Uthayakumaran, S., and Wrigley, C. W. 2006. Improved functional properties for soy-wheat doughs due to modification of the size distribution of polymeric proteins. J. Cereal Sci. 43:223-229.
    • (2006) J. Cereal Sci , vol.43 , pp. 223-229
    • Maforimbo, E.1    Skurray, G.2    Uthayakumaran, S.3    Wrigley, C.W.4
  • 23
    • 34547511151 scopus 로고    scopus 로고
    • Effect of different protein isolates and transglutaminase on rice Hour properties
    • Marco, C., and Rosell, C. M. 2008. Effect of different protein isolates and transglutaminase on rice Hour properties. J. Food Eng. 84:132-139
    • (2008) J. Food Eng , vol.84 , pp. 132-139
    • Marco, C.1    Rosell, C.M.2
  • 24
    • 85153549399 scopus 로고    scopus 로고
    • Marco, C. Pérez, G., Ribotta, P., and Rosell, C. M. 2007. Effect of microbial transglutaminase on the protein fractions of rice, pea and their blends. J. Sci. Food Agric. DOI: 10.1002/jsfa.3006.
    • Marco, C. Pérez, G., Ribotta, P., and Rosell, C. M. 2007. Effect of microbial transglutaminase on the protein fractions of rice, pea and their blends. J. Sci. Food Agric. DOI: 10.1002/jsfa.3006.
  • 25
    • 0242525781 scopus 로고    scopus 로고
    • Identification of wheat protein components involved in polymer formation on incubation with transglutaminase
    • Mujoo, R., and Ng, P. K. W. 2003. Identification of wheat protein components involved in polymer formation on incubation with transglutaminase. Cereal Chem. 80:703-706.
    • (2003) Cereal Chem , vol.80 , pp. 703-706
    • Mujoo, R.1    Ng, P.K.W.2
  • 26
    • 0022245052 scopus 로고
    • The structure and complexity of the 11S polypeptides in soybeans
    • Nielsen, N. C. 1985. The structure and complexity of the 11S polypeptides in soybeans. J. Am. Oil Chem. Soc. 62:1680-1686.
    • (1985) J. Am. Oil Chem. Soc , vol.62 , pp. 1680-1686
    • Nielsen, N.C.1
  • 27
    • 0000118081 scopus 로고
    • A comparative study of the proteins of wheats of diverse baking qualities
    • Orth, R. A., and Bushuk, W. 1972. A comparative study of the proteins of wheats of diverse baking qualities. Cereal Chem. 49:268-275.
    • (1972) Cereal Chem , vol.49 , pp. 268-275
    • Orth, R.A.1    Bushuk, W.2
  • 29
    • 84907421489 scopus 로고    scopus 로고
    • Effect of soybean addition on the rheological properties and breadmaking quality of wheat flour
    • Ribotta, P. D., Arnulphi, S. A., León, A. E., and Añón, M. C. 2005. Effect of soybean addition on the rheological properties and breadmaking quality of wheat flour. J. Sci. Food Agric. 85:1889-1896.
    • (2005) J. Sci. Food Agric , vol.85 , pp. 1889-1896
    • Ribotta, P.D.1    Arnulphi, S.A.2    León, A.E.3    Añón, M.C.4
  • 30
    • 0029137458 scopus 로고
    • Characterization and digestibility of Basmati rice (Oryza-sativa L. var Dehraduni) storage proteins
    • Steenson, D. F., and Sathe, S. K. 1995. Characterization and digestibility of Basmati rice (Oryza-sativa L. var Dehraduni) storage proteins. Cereal Chem. 72:275-280.
    • (1995) Cereal Chem , vol.72 , pp. 275-280
    • Steenson, D.F.1    Sathe, S.K.2
  • 32
    • 26844437327 scopus 로고    scopus 로고
    • Formation and properties of glycinin-rich and beta-conglycinin-rich soy protein isolate gels induced by microbial transglutaminase
    • Tang, C. H., Wu, H., Chen, Z., and Yang, X. Q. 2006. Formation and properties of glycinin-rich and beta-conglycinin-rich soy protein isolate gels induced by microbial transglutaminase. Food Res. Int. 39:87-97.
    • (2006) Food Res. Int , vol.39 , pp. 87-97
    • Tang, C.H.1    Wu, H.2    Chen, Z.3    Yang, X.Q.4
  • 33
    • 0026462509 scopus 로고
    • Plant food protein engineering
    • Utsumi, S. 1992. Plant food protein engineering. Adv. Food Nutr. Res. 36:89-208.
    • (1992) Adv. Food Nutr. Res , vol.36 , pp. 89-208
    • Utsumi, S.1
  • 34
    • 0000911216 scopus 로고
    • Properties of glutelin from mature and developing rice grain
    • Villareal, R. M., and Juliano, B. O. 1978. Properties of glutelin from mature and developing rice grain. Phytochemistry 17:177-182.
    • (1978) Phytochemistry , vol.17 , pp. 177-182
    • Villareal, R.M.1    Juliano, B.O.2
  • 35
    • 0009976813 scopus 로고
    • Soybean proteins - Their functional, chemical, and physical properties
    • Wolf, W. J. 1970. Soybean proteins - Their functional, chemical, and physical properties. J. Agric. Food Chem. 18:969-976.
    • (1970) J. Agric. Food Chem , vol.18 , pp. 969-976
    • Wolf, W.J.1
  • 36
    • 0000668916 scopus 로고    scopus 로고
    • Properties of biopolymers from cross-linking whey protein isolate and soybean 11S globulin
    • Yildirim, M., Hettiarachchy, N. S., and Kalapathy, U. 1996. Properties of biopolymers from cross-linking whey protein isolate and soybean 11S globulin. J. Food Sci. 61:1129-1131.
    • (1996) J. Food Sci , vol.61 , pp. 1129-1131
    • Yildirim, M.1    Hettiarachchy, N.S.2    Kalapathy, U.3


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