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Volumn 87, Issue 14, 2007, Pages 2576-2582

Effect of microbial transglutaminase on the protein fractions of rice, pea and their blends

Author keywords

Electrophoresis; Pea; Proteins; Rice; Transglutaminase

Indexed keywords

PISUM SATIVUM;

EID: 35648946769     PISSN: 00225142     EISSN: 10970010     Source Type: Journal    
DOI: 10.1002/jsfa.3006     Document Type: Article
Times cited : (45)

References (35)
  • 1
    • 0038792398 scopus 로고    scopus 로고
    • Effect of cyclodextrin glycoxyl transferase on dough rheology and bread quality from rice flour
    • Gujral HS, Guardiola I, Carbonell JV and Rosell CM, Effect of cyclodextrin glycoxyl transferase on dough rheology and bread quality from rice flour. J Agric Food Chem 51:3814-3818 (2003).
    • (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
  • 2
    • 0242525766 scopus 로고    scopus 로고
    • Starch hydrolyzing enzymes for retarding the staling of rice bread
    • Gujral HS, Haros M and Rosell CM, Starch hydrolyzing enzymes for retarding the staling of rice bread. Cereal Chem 80:750-754 (2003).
    • (2003) Cereal Chem , vol.80 , pp. 750-754
    • Gujral, H.S.1    Haros, M.2    Rosell, C.M.3
  • 3
    • 19944398492 scopus 로고    scopus 로고
    • Flour mixture of rice flour, corn and cassava starch in the production of gluten-free white bread
    • Lopez ACB, Pereira AJG and Junqueira RG, Flour mixture of rice flour, corn and cassava starch in the production of gluten-free white bread. Braz Arch Biol Technol 47:63-70 (2004).
    • (2004) Braz Arch Biol Technol , vol.47 , pp. 63-70
    • Lopez, A.C.B.1    Pereira, A.J.G.2    Junqueira, R.G.3
  • 4
    • 1642271550 scopus 로고    scopus 로고
    • Functionality of rice flour modified with a microbial transglutaminase
    • Gujral HS and Rosell CM, Functionality of rice flour modified with a microbial transglutaminase. J Cereal Sci 39:225-230 (2004).
    • (2004) J Cereal Sci , vol.39 , pp. 225-230
    • Gujral, H.S.1    Rosell, C.M.2
  • 5
    • 0030919552 scopus 로고    scopus 로고
    • Biopolymers produced by cross-linking soybean HS globulin with whey proteins using transglutaminase
    • Yildirim M and Hettiarachchy NS, Biopolymers produced by cross-linking soybean HS globulin with whey proteins using transglutaminase. J Food Sci 62:270-275 (1997).
    • (1997) J Food Sci , vol.62 , pp. 270-275
    • Yildirim, M.1    Hettiarachchy, N.S.2
  • 6
    • 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 PKW, Effects of transglutaminase on SDS-PAGE patterns of wheat, soy, and barley proteins and their blends. J Food Sci 67:2654-2658 (2002).
    • (2002) J Food Sci , vol.67 , pp. 2654-2658
    • Basman, A.1    Koksel, H.2    Ng, P.K.W.3
  • 7
    • 0029608871 scopus 로고
    • Microbial transglutaminase: A review of its production and application in food processing
    • Zhu Y, Rinzema A, Tramper J and Bol J, Microbial transglutaminase: a review of its production and application in food processing. Appl Microbiol Biotechnol 44:277-282 (1995).
    • (1995) Appl Microbiol Biotechnol , vol.44 , pp. 277-282
    • Zhu, Y.1    Rinzema, A.2    Tramper, J.3    Bol, J.4
  • 8
    • 22144442069 scopus 로고    scopus 로고
    • Microbial transglutaminase as a tool to restore the functionality of gluten from insect-damaged wheat
    • Bonet A, Caballero PA, Gómez M and Rosell CM, Microbial transglutaminase as a tool to restore the functionality of gluten from insect-damaged wheat. Cereal Chem 82:425-430 (2005).
    • (2005) Cereal Chem , vol.82 , pp. 425-430
    • Bonet, A.1    Caballero, P.A.2    Gómez, M.3    Rosell, C.M.4
  • 9
    • 19344375877 scopus 로고    scopus 로고
    • Effect of microbial transglutaminase on the rheological and thermal propenies of insect damaged wheat flour
    • Caballero PA, Bonet A, Rosell CM and Gómez M, Effect of microbial transglutaminase on the rheological and thermal propenies of insect damaged wheat flour. J Cereal Sci 42:93-100 (2005).
    • (2005) J Cereal Sci , vol.42 , pp. 93-100
    • Caballero, P.A.1    Bonet, A.2    Rosell, C.M.3    Gómez, M.4
  • 10
    • 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 CM, Formation of homopolymers and heteropolymers between wheat flour and several protein sources by transglutaminase catalyzed crosslinking. Cereal Chem 83:655-662 (2006).
    • (2006) Cereal Chem , vol.83 , pp. 655-662
    • Bonet, A.1    Blaszczak, W.2    Rosell, C.M.3
  • 11
    • 21144432257 scopus 로고    scopus 로고
    • The effect of dairy and rice powder addition on loaf and crumb characteristics, and on shelf life (intermediate and long-term) of gluten-free breads stored in a modified atmosphere
    • Gallagher E, Kunkel A, Gormley TR and Arendt EK, The effect of dairy and rice powder addition on loaf and crumb characteristics, and on shelf life (intermediate and long-term) of gluten-free breads stored in a modified atmosphere. Eur Food Res Technol 218:44-48 (2003).
    • (2003) Eur Food Res Technol , vol.218 , pp. 44-48
    • Gallagher, E.1    Kunkel, A.2    Gormley, T.R.3    Arendt, E.K.4
  • 13
    • 30844474169 scopus 로고    scopus 로고
    • Network formation in gluten-free bread with application of transglutaminase
    • Moore MM, Heinbockel M, Dockery P, Ulmer HM and Arendt EK, Network formation in gluten-free bread with application of transglutaminase. Cereal Chem 83:28-36 (2006).
    • (2006) Cereal Chem , vol.83 , pp. 28-36
    • Moore, M.M.1    Heinbockel, M.2    Dockery, P.3    Ulmer, H.M.4    Arendt, E.K.5
  • 14
    • 29244449013 scopus 로고    scopus 로고
    • Nutritional quality of important food legumes
    • Iqbal A, Khalil IA, Ateeq N and Khan MS, Nutritional quality of important food legumes. Food Chem 97:331-335 (2006).
    • (2006) Food Chem , vol.97 , pp. 331-335
    • Iqbal, A.1    Khalil, I.A.2    Ateeq, N.3    Khan, M.S.4
  • 15
    • 18044404858 scopus 로고    scopus 로고
    • Isolation and study of the functional properties of pea proteins
    • Tömösközi S, Lásztity R, Haraszi R and Baticz O, Isolation and study of the functional properties of pea proteins. Nahrung/Food 45:399-401 (2001).
    • (2001) Nahrung/Food , vol.45 , pp. 399-401
    • Tömösközi, S.1    Lásztity, R.2    Haraszi, R.3    Baticz, O.4
  • 16
    • 35648965762 scopus 로고    scopus 로고
    • Modification of rice proteins functionality by crosslinking with different protein isolates
    • DOI:10.1016/j.jfoodeng.2007.05.003
    • Marco C and Rosell CM, Modification of rice proteins functionality by crosslinking with different protein isolates. J Food Eng (2007). DOI:10.1016/j.jfoodeng.2007.05.003.
    • (2007) J Food Eng
    • Marco, C.1    Rosell, C.M.2
  • 17
    • 0034997960 scopus 로고    scopus 로고
    • Extraction, denaturation and hydrophobic properties of rice flour proteins
    • Ju ZY, Hettiarachchy NS and Rath N, Extraction, denaturation and hydrophobic properties of rice flour proteins. J Food Sci 66:229-232 (2001).
    • (2001) J Food Sci , vol.66 , pp. 229-232
    • Ju, Z.Y.1    Hettiarachchy, N.S.2    Rath, N.3
  • 18
    • 35649013833 scopus 로고
    • AACC, )9th edn, American Association of Cereal Chemists, St Paul, MN
    • AACC, Approved Methods of the AACC (no. 46-13)(9th edn). American Association of Cereal Chemists, St Paul, MN (1995).
    • (1995) Approved Methods of the AACC , Issue.46 -13
  • 19
    • 0002972547 scopus 로고
    • Polysaccharides, proteins, and lipids of rice
    • ed. by Juliano BO. American Association of Cereal Chemists, St Paul, MN, pp
    • Juliano BO, Polysaccharides, proteins, and lipids of rice, in Rice: Chemistry and Technology, ed. by Juliano BO. American Association of Cereal Chemists, St Paul, MN, pp. 98-141 (1994).
    • (1994) Rice: Chemistry and Technology , pp. 98-141
    • Juliano, B.O.1
  • 20
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of head of bacteriophage-T4
    • Laemmli UK, Cleavage of structural proteins during assembly of head of bacteriophage-T4. Nature 227:680-685 (1970).
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 21
    • 0022975847 scopus 로고
    • Gene structure, protein structure, and regulation of the synthesis of a sulfur-rich protein in pea seeds
    • Higgins TJV, Chandler PM, Randall PJ, Spencer D, Beach LR, Blagrove RJ, et al, Gene structure, protein structure, and regulation of the synthesis of a sulfur-rich protein in pea seeds. J Biol Chem 261:11124- 11130 (1986).
    • (1986) J Biol Chem , vol.261 , pp. 11124-11130
    • Higgins, T.J.V.1    Chandler, P.M.2    Randall, P.J.3    Spencer, D.4    Beach, L.R.5    Blagrove, R.J.6
  • 22
    • 84907421537 scopus 로고
    • Electrophoretic, solubility, and functional properties of commercial soy protein isolates
    • Arrese EL, Sorgentini DA, Wagner JR and Anon MC, Electrophoretic, solubility, and functional properties of commercial soy protein isolates. J Agric Food Chem 39:1029-1032 (1991).
    • (1991) J Agric Food Chem , vol.39 , pp. 1029-1032
    • Arrese, E.L.1    Sorgentini, D.A.2    Wagner, J.R.3    Anon, M.C.4
  • 23
    • 84907421519 scopus 로고
    • Relationship between the method of obtention and the structural and functional properties of soy protein isolates. 2. Surface properties
    • Petruccelli S and Añón MC, Relationship between the method of obtention and the structural and functional properties of soy protein isolates. 2. Surface properties. J Agric Food Chem 42:2170-2175 (1994).
    • (1994) J Agric Food Chem , vol.42 , pp. 2170-2175
    • Petruccelli, S.1    Añón, M.C.2
  • 24
    • 0029137458 scopus 로고
    • Characterization and digestibility of Basmati rice (Oryza sativa 1 var Dehraduni) storage proteins
    • Steenson DF and Sathe SK, Characterization and digestibility of Basmati rice (Oryza sativa 1 var Dehraduni) storage proteins. Cereal Chem 72:275-280 (1995).
    • (1995) Cereal Chem , vol.72 , pp. 275-280
    • Steenson, D.F.1    Sathe, S.K.2
  • 25
    • 0000911216 scopus 로고
    • Properties of glutelin from mature and developing rice grain
    • Villareal RM and Juliano BO, Properties of glutelin from mature and developing rice grain. Phytochemistry 17:177-182 (1978).
    • (1978) Phytochemistry , vol.17 , pp. 177-182
    • Villareal, R.M.1    Juliano, B.O.2
  • 26
    • 0005536606 scopus 로고
    • Action of transglutaminase on an 11S seed protein (pea legumin): Influence of the substrate conformation
    • Larré C, Kedzior ZM, Chenu MG, Viroben G and Gueguen J, Action of transglutaminase on an 11S seed protein (pea legumin): influence of the substrate conformation. J Agric Food Chem 40:1121-1126 (1992).
    • (1992) J Agric Food Chem , vol.40 , pp. 1121-1126
    • Larré, C.1    Kedzior, Z.M.2    Chenu, M.G.3    Viroben, G.4    Gueguen, J.5
  • 27
    • 0027142694 scopus 로고
    • Action of transglutaminase on the constitutive polypeptides of pea legumin
    • Larré C, Chiarello M, Dudek S, Chenu M and Gueguen J, Action of transglutaminase on the constitutive polypeptides of pea legumin. J Agric Food Chem 41:1816-1820 (1993).
    • (1993) J Agric Food Chem , vol.41 , pp. 1816-1820
    • Larré, C.1    Chiarello, M.2    Dudek, S.3    Chenu, M.4    Gueguen, J.5
  • 28
    • 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 and Damaschun G, Shape, symmetry, hydration and secondary structure of the legumin from Vicia faba in solution. Biochim Biophys Acta 784:140-146 (1984).
    • (1984) Biochim Biophys Acta , vol.784 , pp. 140-146
    • Plietz, P.1    Zirwer, D.2    Schlesier, B.3    Gast, K.4    Damaschun, G.5
  • 30
    • 0025422167 scopus 로고
    • Pea and lentil protein extraction and functionality
    • Swanson BG, Pea and lentil protein extraction and functionality. J Am Oil Chem Soc 67:276-280 (1990).
    • (1990) J Am Oil Chem Soc , vol.67 , pp. 276-280
    • Swanson, B.G.1
  • 31
    • 0346225805 scopus 로고
    • Homology among 3S and 7S globulins from cereals and pea
    • Robert LS, Adeli K and Altosaar I, Homology among 3S and 7S globulins from cereals and pea. Plant Physiol 78:812-816 (1985).
    • (1985) Plant Physiol , vol.78 , pp. 812-816
    • Robert, L.S.1    Adeli, K.2    Altosaar, I.3
  • 32
    • 0030265397 scopus 로고    scopus 로고
    • Polymerization of soy protein digests by microbial transglutaminase for improvement of the functional properties
    • Babiker EFE, Khan MAS, Matsudomi N and Kato A, Polymerization of soy protein digests by microbial transglutaminase for improvement of the functional properties. Food Res Int 29:627-634 (1996).
    • (1996) Food Res Int , vol.29 , pp. 627-634
    • Babiker, E.F.E.1    Khan, M.A.S.2    Matsudomi, N.3    Kato, A.4
  • 33
    • 0000668916 scopus 로고    scopus 로고
    • Properties of biopolymers from cross-linking whey protein isolate and soybean HS globulin
    • Yildirim M, Hettiarachchy NS and Kalapathy U, Properties of biopolymers from cross-linking whey protein isolate and soybean HS globulin. J Food Sci 61:1129-1131 (1996).
    • (1996) J Food Sci , vol.61 , pp. 1129-1131
    • Yildirim, M.1    Hettiarachchy, N.S.2    Kalapathy, U.3
  • 34
    • 0036348648 scopus 로고    scopus 로고
    • Spectrophotometric assay using o-phtaldialdehyde for the determination of transglutaminase activity on casein
    • Dinnella C, Gargaro MT, Rossano R and Monteleone E, Spectrophotometric assay using o-phtaldialdehyde for the determination of transglutaminase activity on casein. Food Chem 78(3):363-368 (2002).
    • (2002) Food Chem , vol.78 , Issue.3 , pp. 363-368
    • Dinnella, C.1    Gargaro, M.T.2    Rossano, R.3    Monteleone, E.4
  • 35
    • 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, et al, Gel-forming ability and radical-scavenging activity of soy protein hydrolysate treated with transglutaminase. J Food Sci 70:C87-C92 (2005).
    • (2005) J Food Sci , vol.70
    • Fan, J.1    Saito, M.2    Yanyan, Z.3    Szesze, T.4    Wang, L.5    Tatsumi, E.6


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