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Volumn 49, Issue 2, 2011, Pages 229-236

Characterisation of a Talaromyces emersonii thermostable enzyme cocktail with applications in wheat dough rheology

Author keywords

De novo sequence analysis; Enzymes; Rheology; Talaromyces emersonii; Thermophilic fungus; Wheat dough

Indexed keywords

ACID TREHALASE; ALTERING PROPERTIES; BAKING PROCESS; CELLOBIOHYDROLASES; CHARACTERISATION; ENDOGLUCANASES; ENZYME SEQUENCE; FILAMENTOUS FUNGI; FUNGAL ENZYMES; GLUCANASE; GLUCOSIDASE; IDENTITY-BASED; NANO-LC-ESI-MS/MS; NOVO PROTEINS; PEPTIDE SEQUENCES; PROTEOMIC APPROACHES; RHEOLOGICAL CHARACTERIZATION; RHEOLOGY TEST; SEQUENCE ANALYSIS; SEQUENCE DATA; STRUCTURAL ALTERATIONS; SWISS-PROT; TALAROMYCES EMERSONII; THERMOPHILIC FUNGUS; THERMOSTABLE ENZYMES; WHEAT DOUGH; WHEAT FLOURS; XYLANASES;

EID: 79959895933     PISSN: 01410229     EISSN: 18790909     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2011.04.006     Document Type: Article
Times cited : (17)

References (45)
  • 1
    • 0242634658 scopus 로고
    • Enzymes from thermophilic fungi: Proteases and lipases
    • Johri B., Jain S., Chouhan S. Enzymes from thermophilic fungi: Proteases and lipases. Proc Plant Sci 1985, 94:175-196.
    • (1985) Proc Plant Sci , vol.94 , pp. 175-196
    • Johri, B.1    Jain, S.2    Chouhan, S.3
  • 2
    • 8844286155 scopus 로고    scopus 로고
    • Expression in Trichoderma reesei and characterisation of a thermostable family 3 β-glucosidase from the moderately thermophilic fungus Talaromyces emersonii
    • Murray P.G., Aro N., Collins C., Grassick A., Penttilä M., Saloheimo M., et al. Expression in Trichoderma reesei and characterisation of a thermostable family 3 β-glucosidase from the moderately thermophilic fungus Talaromyces emersonii. Protein Exp Purif 2004, 38:248-257.
    • (2004) Protein Exp Purif , vol.38 , pp. 248-257
    • Murray, P.G.1    Aro, N.2    Collins, C.3    Grassick, A.4    Penttilä, M.5    Saloheimo, M.6
  • 4
    • 0028575479 scopus 로고
    • Characterization of the individual components of the xylanolytic enzyme system of Talaromyces emersonii
    • Tuohy M.G., Laffey C.D., Coughlan M.P. Characterization of the individual components of the xylanolytic enzyme system of Talaromyces emersonii. Bioresour Technol 1994, 50:37-42.
    • (1994) Bioresour Technol , vol.50 , pp. 37-42
    • Tuohy, M.G.1    Laffey, C.D.2    Coughlan, M.P.3
  • 5
    • 0027526567 scopus 로고
    • The xylan-degrading enzyme system of Talaromyces emersonii: novel enzymes with activity against aryl β-d-xylosides and unsubstituted xylans
    • Tuohy M.G., Puls J., Claeyssens M., Vrsanská M., Coughlan M.P. The xylan-degrading enzyme system of Talaromyces emersonii: novel enzymes with activity against aryl β-d-xylosides and unsubstituted xylans. Biochem J 1993, 290:515-523.
    • (1993) Biochem J , vol.290 , pp. 515-523
    • Tuohy, M.G.1    Puls, J.2    Claeyssens, M.3    Vrsanská, M.4    Coughlan, M.P.5
  • 6
    • 84981976048 scopus 로고
    • β-1,4-d-xylan-degrading enzyme systems: Biochemistry, molecular biology and applications
    • Coughlan M.P., Hazlewood G.P. β-1,4-d-xylan-degrading enzyme systems: Biochemistry, molecular biology and applications. Biotechnol Appl Biochem 1993, 17:259-289.
    • (1993) Biotechnol Appl Biochem , vol.17 , pp. 259-289
    • Coughlan, M.P.1    Hazlewood, G.P.2
  • 7
    • 0015449530 scopus 로고
    • Thermostable acid protease produced by Penicillium duponti K1014, a true thermophilic fungus newly isolated from compost
    • Hashimoto H., Iwaasa T., Yokotsuka T. Thermostable acid protease produced by Penicillium duponti K1014, a true thermophilic fungus newly isolated from compost. Appl Microbiol 1972, 24:986-992.
    • (1972) Appl Microbiol , vol.24 , pp. 986-992
    • Hashimoto, H.1    Iwaasa, T.2    Yokotsuka, T.3
  • 8
    • 77953628358 scopus 로고    scopus 로고
    • Talaromyces emersonii thermostable enzyme systems and their applications in wheat baking systems
    • Waters D.M., Murray P.G., Ryan L.A., Arendt E.K., Tuohy M.G. Talaromyces emersonii thermostable enzyme systems and their applications in wheat baking systems. J Agric Food Chem 2010, 58:7415-7422.
    • (2010) J Agric Food Chem , vol.58 , pp. 7415-7422
    • Waters, D.M.1    Murray, P.G.2    Ryan, L.A.3    Arendt, E.K.4    Tuohy, M.G.5
  • 9
    • 13844298129 scopus 로고    scopus 로고
    • Evaluation of the potential of three thermostable fungal endo-β-glucanases for brewing and food applications using viscometric analysis and Dionex HPAEC
    • McCarthy T., Hanniffy O., Lalor E., Savage A.V., Tuohy M.G. Evaluation of the potential of three thermostable fungal endo-β-glucanases for brewing and food applications using viscometric analysis and Dionex HPAEC. Process Biochem 2005, 40:1741-1748.
    • (2005) Process Biochem , vol.40 , pp. 1741-1748
    • McCarthy, T.1    Hanniffy, O.2    Lalor, E.3    Savage, A.V.4    Tuohy, M.G.5
  • 10
    • 0242383940 scopus 로고    scopus 로고
    • Catalytic properties and mode of action of three endo-β-glucanases from Talaromyces emersonii on soluble β-1,4- and β-1,3;1,4-linked glucans
    • McCarthy T., Hanniffy O., Savage A.V., Tuohy M.G. Catalytic properties and mode of action of three endo-β-glucanases from Talaromyces emersonii on soluble β-1,4- and β-1,3;1,4-linked glucans. Int J Biol Macromol 2003, 33:141-148.
    • (2003) Int J Biol Macromol , vol.33 , pp. 141-148
    • McCarthy, T.1    Hanniffy, O.2    Savage, A.V.3    Tuohy, M.G.4
  • 11
    • 0035811982 scopus 로고    scopus 로고
    • Isolation and characterization of a thermostable endo-β-glucanase active on 1,3-1,4-β-d-glucans from the aerobic fungus Talaromyces emersonii CBS 814.70
    • Murray P.G., Grassick A., Laffey C.D., Cuffe M.M., Higgins T., Savage A.V., et al. Isolation and characterization of a thermostable endo-β-glucanase active on 1,3-1,4-β-d-glucans from the aerobic fungus Talaromyces emersonii CBS 814.70. Enzyme Microb Technol 2001, 29:90-98.
    • (2001) Enzyme Microb Technol , vol.29 , pp. 90-98
    • Murray, P.G.1    Grassick, A.2    Laffey, C.D.3    Cuffe, M.M.4    Higgins, T.5    Savage, A.V.6
  • 12
    • 0026800103 scopus 로고
    • Production of thermostable xylan-degrading enzymes by Talaromyces emersonii
    • Tuohy M.G., Coughlan M.P. Production of thermostable xylan-degrading enzymes by Talaromyces emersonii. Bioresour Technol 1992, 39:131-137.
    • (1992) Bioresour Technol , vol.39 , pp. 131-137
    • Tuohy, M.G.1    Coughlan, M.P.2
  • 13
    • 0004006053 scopus 로고
    • Cereals in breadmaking: a molecular colloidal approach
    • Marcel Dekker, Inc, New York, A.-C. Eliasson, K. Larsson (Eds.)
    • Eliasson A.-C., Larsson K. Cereals in breadmaking: a molecular colloidal approach. Food Science and Technology 1993, Marcel Dekker, Inc, New York. A.-C. Eliasson, K. Larsson (Eds.).
    • (1993) Food Science and Technology
    • Eliasson, A.-C.1    Larsson, K.2
  • 15
    • 0035985093 scopus 로고    scopus 로고
    • Wheat protein composition and properties of wheat glutenin in relation to breadmaking functionality
    • Veraverbeke W.S., Delcour J.A. Wheat protein composition and properties of wheat glutenin in relation to breadmaking functionality. Crit Rev Food Sci Nutr 2002, 42:179-208.
    • (2002) Crit Rev Food Sci Nutr , vol.42 , pp. 179-208
    • Veraverbeke, W.S.1    Delcour, J.A.2
  • 16
    • 0034953338 scopus 로고    scopus 로고
    • Structural properties of starch in bread and bread model systems - influence of an antistaling α-amylase
    • Hug-Iten S., Conde-Petit B., Echer F. Structural properties of starch in bread and bread model systems - influence of an antistaling α-amylase. Cereal Chem 2001, 78:421-428.
    • (2001) Cereal Chem , vol.78 , pp. 421-428
    • Hug-Iten, S.1    Conde-Petit, B.2    Echer, F.3
  • 18
    • 70449108132 scopus 로고    scopus 로고
    • Effects of two barley β-glucan isolates on wheat flour dough and bread properties
    • Skendi A., Biliaderis C.G., Papageorgiou M., Izydorczyk M.S. Effects of two barley β-glucan isolates on wheat flour dough and bread properties. Food Chem 2010, 119:1159-1167.
    • (2010) Food Chem , vol.119 , pp. 1159-1167
    • Skendi, A.1    Biliaderis, C.G.2    Papageorgiou, M.3    Izydorczyk, M.S.4
  • 19
    • 33846610642 scopus 로고    scopus 로고
    • Improvement of dough rheology, bread quality and bread shelf-life by enzymes combination
    • Caballero P.A., Gómez M., Rosell C.M. Improvement of dough rheology, bread quality and bread shelf-life by enzymes combination. J Food Eng 2007, 81:42-53.
    • (2007) J Food Eng , vol.81 , pp. 42-53
    • Caballero, P.A.1    Gómez, M.2    Rosell, C.M.3
  • 20
    • 0025057853 scopus 로고
    • The formation and properties of wheat flour doughs
    • Hoseney R.C., Rogers D.E. The formation and properties of wheat flour doughs. Crit Rev Food Sci Nutr 1990, 29:73-93.
    • (1990) Crit Rev Food Sci Nutr , vol.29 , pp. 73-93
    • Hoseney, R.C.1    Rogers, D.E.2
  • 21
    • 0001042101 scopus 로고    scopus 로고
    • Amino acids, peptides, and proteins
    • Marcel Dekker, Inc., New York, O.R. Fennema (Ed.)
    • Damodaran S. Amino acids, peptides, and proteins. Food Chemistry 1996, Marcel Dekker, Inc., New York. Third ed. O.R. Fennema (Ed.).
    • (1996) Food Chemistry
    • Damodaran, S.1
  • 22
    • 0020737995 scopus 로고
    • Cellulose hydrolysis by the cellulases produced by Talaromyces emersonii when grown on different inducing substrates
    • Moloney A.P., Considine P.J., Coughlan M.P. Cellulose hydrolysis by the cellulases produced by Talaromyces emersonii when grown on different inducing substrates. Biotechnol Bioeng 1983, 25:1169-1173.
    • (1983) Biotechnol Bioeng , vol.25 , pp. 1169-1173
    • Moloney, A.P.1    Considine, P.J.2    Coughlan, M.P.3
  • 23
    • 0000150675 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T W
    • Laemmili U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T W. Nature 1970, 227:472-482.
    • (1970) Nature , vol.227 , pp. 472-482
    • Laemmili, U.K.1
  • 24
    • 64949115349 scopus 로고    scopus 로고
    • Effect of low lactose dairy powder addition on the properties of gluten-free batters and bread quality
    • Nunes M.H., Ryan L.A., Arendt E.K. Effect of low lactose dairy powder addition on the properties of gluten-free batters and bread quality. Eur Food. Res Technol 2009, 229:31-41.
    • (2009) Eur Food. Res Technol , vol.229 , pp. 31-41
    • Nunes, M.H.1    Ryan, L.A.2    Arendt, E.K.3
  • 25
    • 33747333106 scopus 로고
    • Use of dinitrosalicylic acid reagent for determination of reducing sugar
    • Miller G.L. Use of dinitrosalicylic acid reagent for determination of reducing sugar. Anal Chem 1959, 31:426-428.
    • (1959) Anal Chem , vol.31 , pp. 426-428
    • Miller, G.L.1
  • 26
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins D.N., Pappin D.J., Creasy D.M., Cottrell J.S. Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 1999, 20:3551-3567.
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.2    Creasy, D.M.3    Cottrell, J.S.4
  • 28
    • 0027399530 scopus 로고
    • Identification of protein coding regions by database similarity search
    • Gish W., States D.J. Identification of protein coding regions by database similarity search. Nat Genet 1993, 3:266-272.
    • (1993) Nat Genet , vol.3 , pp. 266-272
    • Gish, W.1    States, D.J.2
  • 29
    • 21244433623 scopus 로고    scopus 로고
    • Structural changes in the wheat dough and bread with the addition of α-amylases
    • Błaszczak W., Sadowska J., Rosell C.M., Fornal J. Structural changes in the wheat dough and bread with the addition of α-amylases. Eur Food Res Technol 2004, 219:348-354.
    • (2004) Eur Food Res Technol , vol.219 , pp. 348-354
    • Błaszczak, W.1    Sadowska, J.2    Rosell, C.M.3    Fornal, J.4
  • 30
    • 33846230958 scopus 로고    scopus 로고
    • Enzymatic hydrolysis of wheat gluten by proteases and properties of the resulting hydrolysates
    • Kong X., Zhou H., Qian H. Enzymatic hydrolysis of wheat gluten by proteases and properties of the resulting hydrolysates. Food Chem 2007, 102:759-763.
    • (2007) Food Chem , vol.102 , pp. 759-763
    • Kong, X.1    Zhou, H.2    Qian, H.3
  • 31
    • 33744521246 scopus 로고    scopus 로고
    • Improvement on functional properties of wheat gluten by enzymatic hydrolysis and ultrafiltration
    • Wang J., Zhao M., Yang X., Jiang Y. Improvement on functional properties of wheat gluten by enzymatic hydrolysis and ultrafiltration. J Cereal Sci 2006, 44:93-100.
    • (2006) J Cereal Sci , vol.44 , pp. 93-100
    • Wang, J.1    Zhao, M.2    Yang, X.3    Jiang, Y.4
  • 32
    • 0003016529 scopus 로고
    • Milling and baking
    • Academic Press, San Diego, T. Nagodawithana, G. Reed (Eds.)
    • Sproessler B.G. Milling and baking. Enzymes in Food Processing 1993, 293-320. Academic Press, San Diego. T. Nagodawithana, G. Reed (Eds.).
    • (1993) Enzymes in Food Processing , pp. 293-320
    • Sproessler, B.G.1
  • 33
    • 15544372680 scopus 로고    scopus 로고
    • Effect of different enzymes on the textural stability of shelf-stable bread
    • Barrett A.H., Marando G., Leung H., Kaletunc G. Effect of different enzymes on the textural stability of shelf-stable bread. Cereal Chem 2005, 82:152-157.
    • (2005) Cereal Chem , vol.82 , pp. 152-157
    • Barrett, A.H.1    Marando, G.2    Leung, H.3    Kaletunc, G.4
  • 34
    • 0036315660 scopus 로고    scopus 로고
    • Arabinoxylans and endoxylanases in wheat flour bread-making
    • Courtin C.M., Delcour J.A. Arabinoxylans and endoxylanases in wheat flour bread-making. J Cereal Sci 2002, 35:225-243.
    • (2002) J Cereal Sci , vol.35 , pp. 225-243
    • Courtin, C.M.1    Delcour, J.A.2
  • 35
    • 0034845871 scopus 로고    scopus 로고
    • Use of two endoxylanases with different substrate selectivity for understanding arabinoxylan functionality in wheat flour breadmaking
    • Courtin C.M., Gelders G.G., Delcour J.A. Use of two endoxylanases with different substrate selectivity for understanding arabinoxylan functionality in wheat flour breadmaking. Cereal Chem 2001, 78:564-571.
    • (2001) Cereal Chem , vol.78 , pp. 564-571
    • Courtin, C.M.1    Gelders, G.G.2    Delcour, J.A.3
  • 36
    • 0000491882 scopus 로고
    • Xylanases and their application in bakery
    • Elsevier, Amsterdam, The Netherlands, Elsevier (Ed.)
    • Maat J., Roza M., Verbakel J., Stam H., Santos daSilva M.J., Bosse M., et al. Xylanases and their application in bakery. Xylans and Xylanases 1992, 349-360. Elsevier, Amsterdam, The Netherlands. Elsevier (Ed.).
    • (1992) Xylans and Xylanases , pp. 349-360
    • Maat, J.1    Roza, M.2    Verbakel, J.3    Stam, H.4    Santos daSilva, M.J.5    Bosse, M.6
  • 37
    • 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., El-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    El-Hayek, M.L.2    Moreau, D.3
  • 38
    • 1042303792 scopus 로고    scopus 로고
    • Novel tailor-made xylanases: their characterisation, performance in cereal processing and use as a tool to understand xylanase functionality in baking
    • Laboratory of Food Chemistry, Katholieke Universiteit Leuven, Leuven, Belgium, C.M. Courtin, W.S. Veraverbeke, J.A. Delcour (Eds.)
    • Sørensen J.F. Novel tailor-made xylanases: their characterisation, performance in cereal processing and use as a tool to understand xylanase functionality in baking. Recent Advances in Enzymes in Grain Processing 2003, 241-245. Laboratory of Food Chemistry, Katholieke Universiteit Leuven, Leuven, Belgium. C.M. Courtin, W.S. Veraverbeke, J.A. Delcour (Eds.).
    • (2003) Recent Advances in Enzymes in Grain Processing , pp. 241-245
    • Sørensen, J.F.1
  • 42
    • 0034960208 scopus 로고    scopus 로고
    • Relative activity of endoxylanases towards water-extractable and water-unextractable arabinoxylan
    • Courtin C.M., Delcour J.A. Relative activity of endoxylanases towards water-extractable and water-unextractable arabinoxylan. J Cereal Sci 2001, 33:301-312.
    • (2001) J Cereal Sci , vol.33 , pp. 301-312
    • Courtin, C.M.1    Delcour, J.A.2
  • 43
    • 77951625514 scopus 로고    scopus 로고
    • Bread improvers: comparison of a range of lipases with a traditional emulsifier
    • Moayedallaie S., Mirzaei M., Paterson J. Bread improvers: comparison of a range of lipases with a traditional emulsifier. Food Chem 2009, 122:495-499.
    • (2009) Food Chem , vol.122 , pp. 495-499
    • Moayedallaie, S.1    Mirzaei, M.2    Paterson, J.3
  • 45
    • 33746913962 scopus 로고    scopus 로고
    • Mode of action and properties of the β-xylosidases from Talaromyces emersonii and Trichoderma reesei
    • Rasmussen L.E., Sørensen H.R., Vind J., Viksø-Nielsen A. Mode of action and properties of the β-xylosidases from Talaromyces emersonii and Trichoderma reesei. Biotechnol Bioeng 2006, 94:869-876.
    • (2006) Biotechnol Bioeng , vol.94 , pp. 869-876
    • Rasmussen, L.E.1    Sørensen, H.R.2    Vind, J.3    Viksø-Nielsen, A.4


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