메뉴 건너뛰기




Volumn 55, Issue 15, 2007, Pages 6357-6365

Elucidating the mechanism of laccase and tyrosinase in wheat bread making

Author keywords

Bread; Cross linking; Dough; Laccase; Tyrosinase; Wheat

Indexed keywords

GLIADIN; LACCASE; MONOPHENOL MONOOXYGENASE;

EID: 34547799272     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf0703349     Document Type: Article
Times cited : (107)

References (50)
  • 1
    • 77956491350 scopus 로고
    • Baking quality of wheat flours
    • MacRitchie, F. Baking quality of wheat flours. Adv. Food Res. 1984, 29, 201-277.
    • (1984) Adv. Food Res , vol.29 , pp. 201-277
    • MacRitchie, F.1
  • 2
    • 0002894280 scopus 로고
    • Non-starch polysaccharides
    • Blanshard, J. M. V, Frazier, P. J, Galliard, T, Eds, The Royal Society of Chemistry: London
    • Meuser, F.; Suckow, P. Non-starch polysaccharides. In Chemistry and Physics of Baking; Blanshard, J. M. V., Frazier, P. J., Galliard, T., Eds.; The Royal Society of Chemistry: London, 1986; pp 42-61.
    • (1986) Chemistry and Physics of Baking , pp. 42-61
    • Meuser, F.1    Suckow, P.2
  • 3
    • 0012406209 scopus 로고
    • Wheat starch properties and their effect on bread quality
    • Medcalf, D. G. Wheat starch properties and their effect on bread quality. Baker's Digest 1968, 42, 48-51.
    • (1968) Baker's Digest , vol.42 , pp. 48-51
    • Medcalf, D.G.1
  • 4
    • 34547768990 scopus 로고    scopus 로고
    • Medcalf, D. G.; Gilles, K. A. Wheat Starches. I. Comparison of physiochemical properties. Cereal Chem. 1965, 42, 157-162.
    • Medcalf, D. G.; Gilles, K. A. Wheat Starches. I. Comparison of physiochemical properties. Cereal Chem. 1965, 42, 157-162.
  • 5
    • 0032749840 scopus 로고    scopus 로고
    • Role of Starch Granules in Controlling Expansion of Dough During Baking
    • Kusunose, C.; Fujii, T.; Matsumoto, H. Role of Starch Granules in Controlling Expansion of Dough During Baking. Cereal Chem. 1999, 76, 920-924.
    • (1999) Cereal Chem , vol.76 , pp. 920-924
    • Kusunose, C.1    Fujii, T.2    Matsumoto, H.3
  • 6
    • 0037401954 scopus 로고    scopus 로고
    • Impact of Starch Properties on Hearth Bread Characteristics. I. Starch in Wheat Flour
    • Sahlstrøm, S.; Bævre, A. B.; Bråthen, E. Impact of Starch Properties on Hearth Bread Characteristics. I. Starch in Wheat Flour. J. Cereal Sci. 2003, 37, 275-284.
    • (2003) J. Cereal Sci , vol.37 , pp. 275-284
    • Sahlstrøm, S.1    Bævre, A.B.2    Bråthen, E.3
  • 7
    • 0003961160 scopus 로고
    • Carnegie Institute of Washington Publication No. 84; Washington, DC
    • Osborne, T. B. The proteins of the wheat kernel; Carnegie Institute of Washington Publication No. 84; Washington, DC, 1907.
    • (1907) The proteins of the wheat kernel
    • Osborne, T.B.1
  • 8
    • 0001415836 scopus 로고
    • Proteins and amino acids
    • Pomeranz, Y, Ed, American Association of Cereal Chemists, Inc, St. Paul, MN
    • Wrigley, C. W.; Bietz, J. A. Proteins and amino acids. In Wheat Chemistry and Technology; Pomeranz, Y., Ed.; American Association of Cereal Chemists, Inc.: St. Paul, MN, 1988; Vol. I, pp 159-200.
    • (1988) Wheat Chemistry and Technology , vol.1 , pp. 159-200
    • Wrigley, C.W.1    Bietz, J.A.2
  • 9
    • 0002877710 scopus 로고
    • Relation of polar lipid content to mixing requirement and loaf volume potential of hard red winter wheat flour
    • Chung, O. K.; Pomeranz, Y.; Finney, K. F. Relation of polar lipid content to mixing requirement and loaf volume potential of hard red winter wheat flour. Cereal Chem. 1982, 59, 14-20.
    • (1982) Cereal Chem , vol.59 , pp. 14-20
    • Chung, O.K.1    Pomeranz, Y.2    Finney, K.F.3
  • 10
    • 0001237811 scopus 로고
    • Mini review: Gas Cell Stabilisation and Gas Retention in Wheat Bread Dough
    • Gan, Z.; Ellis, P. R.; Schofield, J. D. Mini review: Gas Cell Stabilisation and Gas Retention in Wheat Bread Dough. J. Cereal Sci. 1995, 21, 215-230.
    • (1995) J. Cereal Sci , vol.21 , pp. 215-230
    • Gan, Z.1    Ellis, P.R.2    Schofield, J.D.3
  • 11
    • 0001407324 scopus 로고
    • Water-unextractable cell-wall material from wheat flour. 3. A structural model for arabinoxylans
    • Gruppen, H.; Kormelink, F. J. M.; Voragen, A. G. J. Water-unextractable cell-wall material from wheat flour. 3. A structural model for arabinoxylans. J. Cereal Sci. 1993, 18, 111-128.
    • (1993) J. Cereal Sci , vol.18 , pp. 111-128
    • Gruppen, H.1    Kormelink, F.J.M.2    Voragen, A.G.J.3
  • 12
    • 0001917552 scopus 로고
    • Occurrence and nature of ferulic acid substitution of cell wall polysaccharides in graminaceous plants
    • Smith, M. M.; Harley, R. D. Occurrence and nature of ferulic acid substitution of cell wall polysaccharides in graminaceous plants. Carbohydr. Res. 1983, 11, 65-80.
    • (1983) Carbohydr. Res , vol.11 , pp. 65-80
    • Smith, M.M.1    Harley, R.D.2
  • 13
    • 3042558142 scopus 로고    scopus 로고
    • Doctoral Thesis, Department of Agrotechnology and Food Sciences, Wageningen University, The Netherlands
    • Wang, M. Effect of Pentosans on Gluten Formation and Properties. Doctoral Thesis, Department of Agrotechnology and Food Sciences, Wageningen University, The Netherlands, 2003.
    • (2003) Effect of Pentosans on Gluten Formation and Properties
    • Wang, M.1
  • 15
    • 0001665049 scopus 로고
    • Effect of an Enzyme Preparation Containing Pentosanases on the Bread-making Quality of Flours in Relation to Changes in Pentosan Properties
    • Rouau, X.; Ei-Hayek, M. L.; Moreau, D. Effect of an Enzyme Preparation Containing Pentosanases on the Bread-making Quality of Flours in Relation to Changes in Pentosan Properties. J. Cereal Sci. 1994, 19, 259-272.
    • (1994) J. Cereal Sci , vol.19 , pp. 259-272
    • Rouau, X.1    Ei-Hayek, M.L.2    Moreau, D.3
  • 16
    • 0032726014 scopus 로고    scopus 로고
    • Baking performance, rheology and chemical composition of wheat dough and gluten affected by xylanase and oxidative enzymes
    • Hilhorst, R.; Dunnewind, B.; Orsel, R.; Stegeman, T.; Vliet, T. van Gruppen, H.; Schols, H. A. Baking performance, rheology and chemical composition of wheat dough and gluten affected by xylanase and oxidative enzymes. J. Food Sci. 1999, 64, 808-813.
    • (1999) J. Food Sci , vol.64 , pp. 808-813
    • Hilhorst, R.1    Dunnewind, B.2    Orsel, R.3    Stegeman, T.4    Vliet, T.5    van Gruppen, H.6    Schols, H.A.7
  • 17
    • 0002962296 scopus 로고    scopus 로고
    • Physical properties of enzyme-supplemented doughs and relationship with bread quality parameters
    • Martínez-Anaya, M. A.; Jiménez, T. Physical properties of enzyme-supplemented doughs and relationship with bread quality parameters. Eur. Food Res. Technol. 1998, 206, 134-142.
    • (1998) Eur. Food Res. Technol , vol.206 , pp. 134-142
    • Martínez-Anaya, M.A.1    Jiménez, T.2
  • 19
    • 0033020839 scopus 로고    scopus 로고
    • Oxidative Cross-Linking of Wheat Arabinoxylans by Maganese Peroxidase. Comparison with Laccase and Horseradish Peroxidase. Effect of Cysteine and Tyrosine Gelation
    • Figueroa-Espinoza, M. C.; Morel, M. H.; Surget, A.; Rouau, X. Oxidative Cross-Linking of Wheat Arabinoxylans by Maganese Peroxidase. Comparison with Laccase and Horseradish Peroxidase. Effect of Cysteine and Tyrosine Gelation. J. Sci. Food Agric. 1999, 79, 460-463.
    • (1999) J. Sci. Food Agric , vol.79 , pp. 460-463
    • Figueroa-Espinoza, M.C.1    Morel, M.H.2    Surget, A.3    Rouau, X.4
  • 20
    • 0031805157 scopus 로고    scopus 로고
    • Oxidative Cross-Linking of Pentosans by a Fungal Laccase and Horseradish Peroxidase: Mechanism of Linkage Between Feruloylated Arabinoxylans
    • Figueroa-Espinoza, M. C.; Rouau, X. Oxidative Cross-Linking of Pentosans by a Fungal Laccase and Horseradish Peroxidase: Mechanism of Linkage Between Feruloylated Arabinoxylans. Cereal Chem. 1998, 75, 259-265.
    • (1998) Cereal Chem , vol.75 , pp. 259-265
    • Figueroa-Espinoza, M.C.1    Rouau, X.2
  • 21
    • 0035113941 scopus 로고    scopus 로고
    • Effect of Laccase and Maganase Peroxidase on Wheat Gluten and Pentosans during Mixing
    • Labat, E.; Morel, M. H.; Rouau, X. Effect of Laccase and Maganase Peroxidase on Wheat Gluten and Pentosans during Mixing. Food Hydrocolloids 2001, 15, 47-52.
    • (2001) Food Hydrocolloids , vol.15 , pp. 47-52
    • Labat, E.1    Morel, M.H.2    Rouau, X.3
  • 22
    • 0033748390 scopus 로고    scopus 로고
    • Effect of laccase and Ferulic Acid on Wheat Flour Dough during Mixing
    • Labat, E.; Morel, M. H.; Rouau, X. Effect of laccase and Ferulic Acid on Wheat Flour Dough during Mixing. Cereal Chem. 2000, 77, 823-828.
    • (2000) Cereal Chem , vol.77 , pp. 823-828
    • Labat, E.1    Morel, M.H.2    Rouau, X.3
  • 23
    • 0031690193 scopus 로고    scopus 로고
    • Review: Transglutaminase and its use for food processing
    • Motoki, M.; Seguro, K. Review: Transglutaminase and its use for food processing. Trends Food Sci. Technol. 1998, 9, 204-210.
    • (1998) Trends Food Sci. Technol , vol.9 , pp. 204-210
    • Motoki, M.1    Seguro, K.2
  • 24
    • 23944470680 scopus 로고    scopus 로고
    • Impact of microbial transglutaminase on the staling behaviour of enzyme supplemented pan breads
    • Collar, C.; Bollaín, C. Impact of microbial transglutaminase on the staling behaviour of enzyme supplemented pan breads. Eur. Food Res. Technol. 2005, 221, 298-304.
    • (2005) Eur. Food Res. Technol , vol.221 , pp. 298-304
    • Collar, C.1    Bollaín, C.2
  • 25
    • 20644440389 scopus 로고    scopus 로고
    • Glucose oxidase effects on gluten and water solubles
    • Vemulapalli, V.; Hoseney, R. C. Glucose oxidase effects on gluten and water solubles. Cereal Chem. 1998, 75, 859-862.
    • (1998) Cereal Chem , vol.75 , pp. 859-862
    • Vemulapalli, V.1    Hoseney, R.C.2
  • 27
    • 33646564345 scopus 로고    scopus 로고
    • When quinones meet amino acids: Chemical, physical and biological consequences
    • Bittner, S. When quinones meet amino acids: chemical, physical and biological consequences. Amino Acids 2006, 30, 205-224.
    • (2006) Amino Acids , vol.30 , pp. 205-224
    • Bittner, S.1
  • 28
    • 0033575234 scopus 로고    scopus 로고
    • Rotational echo double resonance detection of cross-links formed in mussel byssus under high-flow stress
    • McDowell, L. M.; Burzio, L. A.; Waite, J. H.; Schaefer, J. Rotational echo double resonance detection of cross-links formed in mussel byssus under high-flow stress. J. Biol. Chem. 1999, 274, 20293-20295.
    • (1999) J. Biol. Chem , vol.274 , pp. 20293-20295
    • McDowell, L.M.1    Burzio, L.A.2    Waite, J.H.3    Schaefer, J.4
  • 29
    • 0021213448 scopus 로고
    • Oxidation of tyrosine residues in proteins by tyrosinase
    • Ito, S.; Kato, T.; Shinpo, K.; Fujita, K. Oxidation of tyrosine residues in proteins by tyrosinase. Biochem. J. 1984, 222, 407-411.
    • (1984) Biochem. J , vol.222 , pp. 407-411
    • Ito, S.1    Kato, T.2    Shinpo, K.3    Fujita, K.4
  • 30
    • 0000038841 scopus 로고    scopus 로고
    • Cross-linking of whey proteins by enzymatic oxidation
    • Færgemand, M.; Otte, J.; Qvist, K. B. Cross-linking of whey proteins by enzymatic oxidation. J. Agric. Food Chem. 1998, 46, 1326-1333.
    • (1998) J. Agric. Food Chem , vol.46 , pp. 1326-1333
    • Færgemand, M.1    Otte, J.2    Qvist, K.B.3
  • 32
    • 22244437897 scopus 로고    scopus 로고
    • Identification of dehydro-ferulic acid-tyrosine in rye and wheat: Evidence for a covalent cross-link between arabinoxylans and proteins
    • Piber, M.; Koehler, P. Identification of dehydro-ferulic acid-tyrosine in rye and wheat: evidence for a covalent cross-link between arabinoxylans and proteins. J. Agric. Food Chem. 2005, 53, 5276-5284.
    • (2005) J. Agric. Food Chem , vol.53 , pp. 5276-5284
    • Piber, M.1    Koehler, P.2
  • 35
    • 0020688520 scopus 로고
    • Neurosopra tyrosinase: Structural, spectroscopic and catalytic properties
    • Lerch, K. Neurosopra tyrosinase: structural, spectroscopic and catalytic properties. Mol. Cell. Biochem. 1983, 52, 125-138.
    • (1983) Mol. Cell. Biochem , vol.52 , pp. 125-138
    • Lerch, K.1
  • 36
    • 0028013536 scopus 로고
    • The structure and function of fungal laccases
    • Thurston, C. The structure and function of fungal laccases. Microbiology 1994, 140, 19-26.
    • (1994) Microbiology , vol.140 , pp. 19-26
    • Thurston, C.1
  • 37
    • 0037009169 scopus 로고    scopus 로고
    • Investigations on the laccase-catalyzed polymerization of lignin model compounds using size-exclusion HPLC
    • Rittstieg, K.; Suurnäkki, A.; Suortti, T.; Kruus, K.; Guebitz, G.; Buchert, J. Investigations on the laccase-catalyzed polymerization of lignin model compounds using size-exclusion HPLC. Enzyme Microb. Technol. 2002, 31, 403-410.
    • (2002) Enzyme Microb. Technol , vol.31 , pp. 403-410
    • Rittstieg, K.1    Suurnäkki, A.2    Suortti, T.3    Kruus, K.4    Guebitz, G.5    Buchert, J.6
  • 38
    • 0024288734 scopus 로고
    • Ligninolytic enzymes of the white-rot-fungus Phlebia ferulic
    • Niku-Paavola, M.-L.; Karhunen, E.; Salola, P.; Raunio, V. Ligninolytic enzymes of the white-rot-fungus Phlebia ferulic. Biochem. J. 1988, 254, 877-884.
    • (1988) Biochem. J , vol.254 , pp. 877-884
    • Niku-Paavola, M.-L.1    Karhunen, E.2    Salola, P.3    Raunio, V.4
  • 39
    • 33748327047 scopus 로고    scopus 로고
    • Production and characterization of a secreted, C-terminally processed tyrosinase from the filamentous fungus Trichoderma reesei
    • Selinheimo, E.; Saloheimo, M.; Ahola, E.; Westerholm-Parvinen, A.; Kalkkinen, N.; Buchert, J.; Kruus, K. Production and characterization of a secreted, C-terminally processed tyrosinase from the filamentous fungus Trichoderma reesei. FEBS J. 2006, 273, 4322-4335.
    • (2006) FEBS J , vol.273 , pp. 4322-4335
    • Selinheimo, E.1    Saloheimo, M.2    Ahola, E.3    Westerholm-Parvinen, A.4    Kalkkinen, N.5    Buchert, J.6    Kruus, K.7
  • 40
    • 85053591293 scopus 로고
    • Tyrosinase
    • Lontie, R, Ed, CRC Press Inc, Boca Raton, FL
    • Robb, D. A. Tyrosinase. In Copperproteins and copper enzymes; Lontie, R., Ed.; CRC Press Inc.: Boca Raton, FL, 1984; Vol. 2, pp 207-240.
    • (1984) Copperproteins and copper enzymes , vol.2 , pp. 207-240
    • Robb, D.A.1
  • 41
    • 0026537453 scopus 로고
    • Interlaboratory testing methods for assay of xylanase activity
    • Bailey, M. J.; Biely, P.; Poutanen, K. Interlaboratory testing methods for assay of xylanase activity. J. Biotechnol. 1992, 23, 257-270.
    • (1992) J. Biotechnol , vol.23 , pp. 257-270
    • Bailey, M.J.1    Biely, P.2    Poutanen, K.3
  • 42
  • 44
    • 0344267735 scopus 로고    scopus 로고
    • Barley spent grain: Release of hydroxycinnamic acids (ferulic and p-coumaric acids) by commercial enzyme preparations
    • Bartolomé, B.; Gómez-Cordovés, C. Barley spent grain: release of hydroxycinnamic acids (ferulic and p-coumaric acids) by commercial enzyme preparations. J. Sci. Food Agric. 1999, 79, 435-439.
    • (1999) J. Sci. Food Agric , vol.79 , pp. 435-439
    • Bartolomé, B.1    Gómez-Cordovés, C.2
  • 45
    • 34547758965 scopus 로고
    • Concerning the identity of the proteins extracted from wheat flour by the usual solvents
    • Bailey, C. H.; Blish, M. J. Concerning the identity of the proteins extracted from wheat flour by the usual solvents. J. Biol. Chem. 1915, 23, 345-357.
    • (1915) J. Biol. Chem , vol.23 , pp. 345-357
    • Bailey, C.H.1    Blish, M.J.2
  • 46
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 47
    • 0002217586 scopus 로고    scopus 로고
    • Correlations of the breadmaking performance of wheat flour with Theological measurements on a micro-scale
    • Kieffer, R.; Wieser, H.; Henderson, M. H.; Graveland, A. Correlations of the breadmaking performance of wheat flour with Theological measurements on a micro-scale. J. Cereal Sci. 1998, 27, 53-60.
    • (1998) J. Cereal Sci , vol.27 , pp. 53-60
    • Kieffer, R.1    Wieser, H.2    Henderson, M.H.3    Graveland, A.4
  • 48
    • 31844448219 scopus 로고    scopus 로고
    • Laccase
    • Whitaker, J. R, Voragen, A. G. J, Wong, D. W. S, Eds, Marcel Dekker, Inc, New York
    • Flurkey, W. H. Laccase. In Handbook of food enzymology; Whitaker, J. R., Voragen, A. G. J., Wong, D. W. S., Eds.; Marcel Dekker, Inc.: New York, 2003; pp 525-537.
    • (2003) Handbook of food enzymology , pp. 525-537
    • Flurkey, W.H.1
  • 49
    • 31844432538 scopus 로고    scopus 로고
    • Effects of laccase, xylanase and their combination on the rheological properties of wheat doughs
    • Selinheimo, E.; Kruus, K.; Buchert, J.; Hopia, A.; Autio, K. Effects of laccase, xylanase and their combination on the rheological properties of wheat doughs. J. Cereal Sci. 2006, 43, 152-159.
    • (2006) J. Cereal Sci , vol.43 , pp. 152-159
    • Selinheimo, E.1    Kruus, K.2    Buchert, J.3    Hopia, A.4    Autio, K.5
  • 50
    • 0000295882 scopus 로고
    • Effect of the outer bran layers on the loaf volume of wheat bread
    • Gan, Z.; Galliard, T.; Ellis, P. R.; Angold, R. E.; Vaughan, J. G. Effect of the outer bran layers on the loaf volume of wheat bread. J. Cereal Sci. 1992, 15, 151-163.
    • (1992) J. Cereal Sci , vol.15 , pp. 151-163
    • Gan, Z.1    Galliard, T.2    Ellis, P.R.3    Angold, R.E.4    Vaughan, J.G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.