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Volumn 55, Issue 3, 2007, Pages 978-984

Prolamin hydrolysis in wheat sourdoughs with differing proteolytic activities

Author keywords

Germination; Gluten sensitivity; Hydrolysis; Prolamin; Proteases; Proteolysis; Sourdough; Wheat

Indexed keywords

HORDEUM; SECALE CEREALE; TRITICUM AESTIVUM;

EID: 34247893978     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf062755g     Document Type: Article
Times cited : (47)

References (31)
  • 2
    • 0037183929 scopus 로고    scopus 로고
    • Shan, L.; Molberg, ø.; Parrot, 1.; Hausch, F.; Filiz, F.; Gray, G. M.; Sollid, L. M.; Khosla, C. Structural basis for gluten intolerance in celiac sprue. Science 2002, 297, 2275-2279.
    • Shan, L.; Molberg, ø.; Parrot, 1.; Hausch, F.; Filiz, F.; Gray, G. M.; Sollid, L. M.; Khosla, C. Structural basis for gluten intolerance in celiac sprue. Science 2002, 297, 2275-2279.
  • 3
    • 26844558196 scopus 로고    scopus 로고
    • Identification and analysis of multivalent proteolytically resistant peptides from gluten: Implications for celiac sprue
    • Shan, L.; Qiao, S.-W.; Arentz-Hansen, H.; Molberg, ø.; Gray, G. M.; Sollid, L. M.; Khosla, C. Identification and analysis of multivalent proteolytically resistant peptides from gluten: implications for celiac sprue. J. Proteome Res. 2005, 4, 1732-1741.
    • (2005) J. Proteome Res , vol.4 , pp. 1732-1741
    • Shan, L.1    Qiao, S.-W.2    Arentz-Hansen, H.3    Molberg, ø.4    Gray, G.M.5    Sollid, L.M.6    Khosla, C.7
  • 6
    • 0036154310 scopus 로고    scopus 로고
    • Proteolysis by sourdough lactic acid bacteria: Effects on wheat flour protein fractions and gliadin peptides involved in human cereal intolerance
    • Di Cagno, R.; De Angelis, M.; Lavermicocca, P.; De Vincenzi, M.; Giovannini, C.; Faccia, M.; Gobbetti, M. Proteolysis by sourdough lactic acid bacteria: effects on wheat flour protein fractions and gliadin peptides involved in human cereal intolerance. Appl. Environ. Microbiol. 2002, 68, 623-633.
    • (2002) Appl. Environ. Microbiol , vol.68 , pp. 623-633
    • Di Cagno, R.1    De Angelis, M.2    Lavermicocca, P.3    De Vincenzi, M.4    Giovannini, C.5    Faccia, M.6    Gobbetti, M.7
  • 9
    • 0000975925 scopus 로고
    • Aspartic proteinase from wheat seeds: Isolation, properties and action on gliadin
    • Belozersky, M. A.; Sarbakanova, S. T.; Dunaevsky, Y. E. Aspartic proteinase from wheat seeds: isolation, properties and action on gliadin. Planta 1989, 177, 321-326.
    • (1989) Planta , vol.177 , pp. 321-326
    • Belozersky, M.A.1    Sarbakanova, S.T.2    Dunaevsky, Y.E.3
  • 11
    • 0000990376 scopus 로고
    • Wheat seed carboxypeptidase and joint action on gliadin of proteases from dry and germinating-seeds
    • Dunaevsky, Y. E.; Sarbakanova, S. T.; Belozersky, M. A. Wheat seed carboxypeptidase and joint action on gliadin of proteases from dry and germinating-seeds. J. Exp. Bot. 1989, 40, 1323-1329.
    • (1989) J. Exp. Bot , vol.40 , pp. 1323-1329
    • Dunaevsky, Y.E.1    Sarbakanova, S.T.2    Belozersky, M.A.3
  • 12
    • 0030239307 scopus 로고    scopus 로고
    • Major proteinase hydrolysing gliadin during wheat germination
    • Bottari, A.; Capocchi, A.; Fontanini, D.; Galleschi, L. Major proteinase hydrolysing gliadin during wheat germination. Phytochemistry 1996, 43, 39-44.
    • (1996) Phytochemistry , vol.43 , pp. 39-44
    • Bottari, A.1    Capocchi, A.2    Fontanini, D.3    Galleschi, L.4
  • 13
    • 21744460353 scopus 로고    scopus 로고
    • Endoproteases of barley and malt
    • Jones, B. L. Endoproteases of barley and malt. J. Cereal Sci. 2005, 42, 139-156.
    • (2005) J. Cereal Sci , vol.42 , pp. 139-156
    • Jones, B.L.1
  • 14
    • 0000062071 scopus 로고
    • Germinating barley grains contain five acid carboxypeptidases with complementary substrate specificities
    • Mikola, L. Germinating barley grains contain five acid carboxypeptidases with complementary substrate specificities. Biochim. Biophys. Acta 1983, 747, 241-252.
    • (1983) Biochim. Biophys. Acta , vol.747 , pp. 241-252
    • Mikola, L.1
  • 15
    • 0001678694 scopus 로고
    • Acid carboxypeptidases in grains and leaves of wheat, Triticum aestivum L
    • Mikola, L. Acid carboxypeptidases in grains and leaves of wheat, Triticum aestivum L. Plant Physiol. 1986, 81, 823-829.
    • (1986) Plant Physiol , vol.81 , pp. 823-829
    • Mikola, L.1
  • 16
    • 0034773313 scopus 로고    scopus 로고
    • Proteolytic degradation of cereal prolamins - the problem with proline
    • Simpson, D. J. Proteolytic degradation of cereal prolamins - the problem with proline. Plant Sci. 2001, 161, 825-838.
    • (2001) Plant Sci , vol.161 , pp. 825-838
    • Simpson, D.J.1
  • 17
    • 0032532618 scopus 로고    scopus 로고
    • Simplified endoproteinase assays using gelatin or azogelatin
    • Jones, B. L.; Fontanini, D.; Jarvinen, M.; Pekkarinen, A. Simplified endoproteinase assays using gelatin or azogelatin. Anal. Biochem. 1998, 263, 214-220,
    • (1998) Anal. Biochem , vol.263 , pp. 214-220
    • Jones, B.L.1    Fontanini, D.2    Jarvinen, M.3    Pekkarinen, A.4
  • 18
    • 0033795297 scopus 로고    scopus 로고
    • Quantitative study of the formation of endoproteolytic activities during malting and their stabilities to kilning
    • Jones, B. L.; Marinac, L. A.; Fontanini, D. Quantitative study of the formation of endoproteolytic activities during malting and their stabilities to kilning. J. Agric. Food Chem. 2000, 48, 3898-3905.
    • (2000) J. Agric. Food Chem , vol.48 , pp. 3898-3905
    • Jones, B.L.1    Marinac, L.A.2    Fontanini, D.3
  • 19
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem 1976, 72, 248-254.
    • (1976) Anal. Biochem , vol.72 , pp. 248-254
    • Bradford, M.1
  • 20
    • 0000700014 scopus 로고
    • Characterization of germinated barley endoproteolytic enzymes by two-dimensional gel electrophoresis
    • Zhang, N.; Jones, B. L. Characterization of germinated barley endoproteolytic enzymes by two-dimensional gel electrophoresis. J. Cereal Sci. 1995, 21, 145-153.
    • (1995) J. Cereal Sci , vol.21 , pp. 145-153
    • Zhang, N.1    Jones, B.L.2
  • 21
    • 0018946189 scopus 로고
    • Changes in prolyl endopeptidase during maturation of rat brain and hydrolysis of substance P by the purified enzyme
    • Kato, T.; Nakano, T.; Kojima, K.; Nagatsu, T.; Sakakibara, S. Changes in prolyl endopeptidase during maturation of rat brain and hydrolysis of substance P by the purified enzyme. J. Neurochem. 1980, 35, 527-535.
    • (1980) J. Neurochem , vol.35 , pp. 527-535
    • Kato, T.1    Nakano, T.2    Kojima, K.3    Nagatsu, T.4    Sakakibara, S.5
  • 22
    • 0018098536 scopus 로고
    • Fluorescence assay of X-prolyl dipeptidyl-aminopeptidase activity with a new fluorogenic substrate
    • Kato, T.; Nagatsu, T.; Kimura, T.; Sakakibara, S. Fluorescence assay of X-prolyl dipeptidyl-aminopeptidase activity with a new fluorogenic substrate. Biochem. Med. 1978, 19, 351-359.
    • (1978) Biochem. Med , vol.19 , pp. 351-359
    • Kato, T.1    Nagatsu, T.2    Kimura, T.3    Sakakibara, S.4
  • 25
    • 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
  • 26
    • 64349101773 scopus 로고
    • Free amino nitrogen (international method)
    • ASBC, 8th ed, technical and editorial committees of the ASBC; American Society of Brewing Chemists: St. Paul, MN, Wort-12
    • ASBC. Free amino nitrogen (international method). In Methods of Analysis of the American Society of Brewing Chemists, 8th ed.; technical and editorial committees of the ASBC; American Society of Brewing Chemists: St. Paul, MN, 1992; Wort-12.
    • (1992) Methods of Analysis of the American Society of Brewing Chemists
  • 27
    • 0037726720 scopus 로고    scopus 로고
    • Innovative approach to low-level gluten determination in foods using a novel sandwich enzyme-linked immunosorbent assay protocol
    • Valdés, I.; Garcia, E.; Llorente, M.; Méndez, E. Innovative approach to low-level gluten determination in foods using a novel sandwich enzyme-linked immunosorbent assay protocol. Eur. J. Gastroenterol. Hepatol. 2003, 15, 461-463.
    • (2003) Eur. J. Gastroenterol. Hepatol , vol.15 , pp. 461-463
    • Valdés, I.1    Garcia, E.2    Llorente, M.3    Méndez, E.4
  • 28
    • 1542317114 scopus 로고    scopus 로고
    • Gluten hydrolysis and depolymerization during sourdough fermentation
    • Thiele, C.; Grassl, S.; Ganzle, M. G. Gluten hydrolysis and depolymerization during sourdough fermentation. J. Agric. Food Chem. 2004, 52, 1307-1314.
    • (2004) J. Agric. Food Chem , vol.52 , pp. 1307-1314
    • Thiele, C.1    Grassl, S.2    Ganzle, M.G.3
  • 29
    • 11144304186 scopus 로고    scopus 로고
    • How various malt endoproteinase classes affect wort soluble protein levels
    • Jones, B. L.; Budde, A. D. How various malt endoproteinase classes affect wort soluble protein levels. J. Cereal Sci. 2005, 41, 95-106.
    • (2005) J. Cereal Sci , vol.41 , pp. 95-106
    • Jones, B.L.1    Budde, A.D.2
  • 30
    • 0034527302 scopus 로고    scopus 로고
    • Degradation of gluten by proteases from dry and germinating wheat (Triticum durum) seeds: An in vitro approach to storage protein mobilization
    • Capocchi, A.; Cinollo, M.; Galleschi, L.; Saviozzi, F.; Calucci, L.; Pinzino, C.; Zandomeneghi, M. Degradation of gluten by proteases from dry and germinating wheat (Triticum durum) seeds: an in vitro approach to storage protein mobilization. J. Agric. Food Chem. 2000, 48, 6271-6279.
    • (2000) J. Agric. Food Chem , vol.48 , pp. 6271-6279
    • Capocchi, A.1    Cinollo, M.2    Galleschi, L.3    Saviozzi, F.4    Calucci, L.5    Pinzino, C.6    Zandomeneghi, M.7
  • 31
    • 33750618989 scopus 로고    scopus 로고
    • Rapid degradation of gliadin peptides toxic for coeliac disease patients by proteases from germinating cereals
    • Hartmann, G.; Koehler, P.; Wieser, H. Rapid degradation of gliadin peptides toxic for coeliac disease patients by proteases from germinating cereals. J. Cereal Sci. 2006, 44, 368-371.
    • (2006) J. Cereal Sci , vol.44 , pp. 368-371
    • Hartmann, G.1    Koehler, P.2    Wieser, H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.