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Volumn 85, Issue 4, 2005, Pages 549-562

Identification and characterization of the major aspartic proteinase activity in Theobroma cacao seeds

Author keywords

Aspartic proteinase; Flavour precursor peptides; Proteolysis; Theobroma cacao; Trypsin inhibitor

Indexed keywords

PHASEOLUS (ANGIOSPERM); THEOBROMA CACAO;

EID: 14144252975     PISSN: 00225142     EISSN: None     Source Type: Journal    
DOI: 10.1002/jsfa.1777     Document Type: Article
Times cited : (26)

References (29)
  • 1
    • 0028814328 scopus 로고
    • Regulation of protein degradation
    • Callis J, Regulation of protein degradation. Plant Cell 7:845-857 (1995).
    • (1995) Plant Cell , vol.7 , pp. 845-857
    • Callis, J.1
  • 2
    • 0345120944 scopus 로고    scopus 로고
    • Plant aspartic proteinases; enzymes on the way to function
    • Mutlu A and Gal S, Plant aspartic proteinases; enzymes on the way to function. Physiol Plant 105:569-576 (1999).
    • (1999) Physiol Plant , vol.105 , pp. 569-576
    • Mutlu, A.1    Gal, S.2
  • 4
    • 0029004315 scopus 로고
    • Families of aspartic peptidases, and those of unknown catalytic mechanism
    • Rawlings ND and Barret AJ, Families of aspartic peptidases, and those of unknown catalytic mechanism. Methods Enzymol 248:105-120 (1995).
    • (1995) Methods Enzymol , vol.248 , pp. 105-120
    • Rawlings, N.D.1    Barret, A.J.2
  • 5
    • 0032933405 scopus 로고    scopus 로고
    • The aspartic proteinase is expressed in Arabidopsis thaliana seeds and localized in the protein bodies
    • Mutlu A, Chen X, Reddy SM and Gal S, The aspartic proteinase is expressed in Arabidopsis thaliana seeds and localized in the protein bodies. Seed Science Res 9:75-84 (1999).
    • (1999) Seed Science Res , vol.9 , pp. 75-84
    • Mutlu, A.1    Chen, X.2    Reddy, S.M.3    Gal, S.4
  • 6
    • 0026321028 scopus 로고
    • Primary structure of a barley-grain aspartic proteinase
    • Runeberg-Roos P, Tormakangas K and Ostman A, Primary structure of a barley-grain aspartic proteinase. Eur J Biochem 202:1021-1027 (1991).
    • (1991) Eur J Biochem , vol.202 , pp. 1021-1027
    • Runeberg-Roos, P.1    Tormakangas, K.2    Ostman, A.3
  • 7
    • 0028317608 scopus 로고
    • Tissue specific localization of aspartic proteinase in developing and germinating barley grains
    • Tormakangas K, Kervinen J, Ostman A and Teeri T, Tissue specific localization of aspartic proteinase in developing and germinating barley grains. Planta 195:116-125 (1994).
    • (1994) Planta , vol.195 , pp. 116-125
    • Tormakangas, K.1    Kervinen, J.2    Ostman, A.3    Teeri, T.4
  • 8
    • 0028425479 scopus 로고
    • The aspartic proteinase of barley is a vacuolar enzyme that processes probarley lectin in-vitro
    • Runeberg-Roos P, Kervinen J, Kovaleva V, Gal S and Raikhel NV, The aspartic proteinase of barley is a vacuolar enzyme that processes probarley lectin in-vitro. Plant Physiol 105:321-329 (1994).
    • (1994) Plant Physiol , vol.105 , pp. 321-329
    • Runeberg-Roos, P.1    Kervinen, J.2    Kovaleva, V.3    Gal, S.4    Raikhel, N.V.5
  • 10
    • 0029107096 scopus 로고
    • Developmental stage-dependent variation of the levels of globular storage protein and aspartic endoproteinase during ripening and germination of Theobroma cacao seeds
    • Voigt J, Kamaruddin S, Heinrichs H, Wrann D, Senyuk V and Biehl B, Developmental stage-dependent variation of the levels of globular storage protein and aspartic endoproteinase during ripening and germination of Theobroma cacao seeds. J Plant Physiol 145:299-307 (1995).
    • (1995) J Plant Physiol , vol.145 , pp. 299-307
    • Voigt, J.1    Kamaruddin, S.2    Heinrichs, H.3    Wrann, D.4    Senyuk, V.5    Biehl, B.6
  • 11
    • 0027965355 scopus 로고
    • In vitro studies on the proteolytic formation of the characteristic aroma precursors of fermented cocoa seeds: The significance of endoprotease specificity
    • Voigt J, Voigt G, Heinrichs D, Wrann D and Biehl B, In vitro studies on the proteolytic formation of the characteristic aroma precursors of fermented cocoa seeds: the significance of endoprotease specificity. Food Chem 51:7-14 (1994).
    • (1994) Food Chem , vol.51 , pp. 7-14
    • Voigt, J.1    Voigt, G.2    Heinrichs, D.3    Wrann, D.4    Biehl, B.5
  • 12
    • 0036947360 scopus 로고    scopus 로고
    • Molecular and biochemical characterization of two proteinases TcAP1 and TcAP2 from Theobroma cacao seeds
    • Laloi M, McCarthy J, Morandi O, Gysler C and Bucheli P, Molecular and biochemical characterization of two proteinases TcAP1 and TcAP2 from Theobroma cacao seeds. Planta 215:754-762 (2002).
    • (2002) Planta , vol.215 , pp. 754-762
    • Laloi, M.1    McCarthy, J.2    Morandi, O.3    Gysler, C.4    Bucheli, P.5
  • 15
    • 84986841598 scopus 로고
    • Effect of acetic acid on subcellular structures of cocoa bean cotyleydons
    • Biehl B, Passern D and Sagemann W, Effect of acetic acid on subcellular structures of cocoa bean cotyleydons. J Sci Food Agric 33:1101-1109 (1982).
    • (1982) J Sci Food Agric , vol.33 , pp. 1101-1109
    • Biehl, B.1    Passern, D.2    Sagemann, W.3
  • 16
    • 84985345642 scopus 로고
    • Acidification, proteolysis and flavour potential in fermenting cocoa beans
    • Biehl B, Brunner E, Passern D, Quesnel VC and Adomako D, Acidification, proteolysis and flavour potential in fermenting cocoa beans. J Sci Food Agric 36:583-598 (1985).
    • (1985) J Sci Food Agric , vol.36 , pp. 583-598
    • Biehl, B.1    Brunner, E.2    Passern, D.3    Quesnel, V.C.4    Adomako, D.5
  • 17
    • 84981861624 scopus 로고
    • The precursors of chocolate aroma: A comparative study of fermented and unfermented cocoa beans
    • Rohan T, The precursors of chocolate aroma: a comparative study of fermented and unfermented cocoa beans. J Food Sci 29:456-459 (1964).
    • (1964) J Food Sci , vol.29 , pp. 456-459
    • Rohan, T.1
  • 18
    • 0028814503 scopus 로고
    • Precursors of the cocoa specific aroma components are derived from the vicilin-class (7S) globulin of the cocoa seeds by proteolytic processing
    • Voigt J and Biehl B, Precursors of the cocoa specific aroma components are derived from the vicilin-class (7S) globulin of the cocoa seeds by proteolytic processing. Bot Acta 108:283-289 (1995).
    • (1995) Bot Acta , vol.108 , pp. 283-289
    • Voigt, J.1    Biehl, B.2
  • 19
    • 0028212313 scopus 로고
    • Cocoa-specific aroma precursors are generated by proteolytic digestion of the vicilin-like globulin of cocoa seeds
    • Voigt J, Heinrichs H, Voigt G and Biehl B, Cocoa-specific aroma precursors are generated by proteolytic digestion of the vicilin-like globulin of cocoa seeds. Food Chem 50:177-184 (1994).
    • (1994) Food Chem , vol.50 , pp. 177-184
    • Voigt, J.1    Heinrichs, H.2    Voigt, G.3    Biehl, B.4
  • 20
    • 0031838718 scopus 로고    scopus 로고
    • Enzyme activities in cocoa beans during fermentation
    • Hansen C, del Olmo M and Burri C, Enzyme activities in cocoa beans during fermentation. J Sci Food Agric 77:273-281 (1998).
    • (1998) J Sci Food Agric , vol.77 , pp. 273-281
    • Hansen, C.1    Del Olmo, M.2    Burri, C.3
  • 21
    • 85022241054 scopus 로고
    • Spectrophotometric assay using o-phthaldialdehyde for determination of proteolysis in milk and isolated milk proteins
    • Church F, Swaisgood H, Porter D and Catignani G, Spectrophotometric assay using o-phthaldialdehyde for determination of proteolysis in milk and isolated milk proteins. J Dairy Sci 66:1219-1227 (1983).
    • (1983) J Dairy Sci , vol.66 , pp. 1219-1227
    • Church, F.1    Swaisgood, H.2    Porter, D.3    Catignani, G.4
  • 22
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulphate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schagger H and von Jagow G, Tricine-sodium dodecyl sulphate- polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal Biochem 166:368-379 (1987).
    • (1987) Anal Biochem , vol.166 , pp. 368-379
    • Schagger, H.1    Von Jagow, G.2
  • 23
    • 0033672232 scopus 로고    scopus 로고
    • Primary structure of the abundant seed albumin of Theobroma cacao by mass spectrometry
    • Kochhar S, Gartenmenn K and Juillerat M, Primary structure of the abundant seed albumin of Theobroma cacao by mass spectrometry. J Agric Food Chem 48:5593-5599 (2000).
    • (2000) J Agric Food Chem , vol.48 , pp. 5593-5599
    • Kochhar, S.1    Gartenmenn, K.2    Juillerat, M.3
  • 24
    • 0026768309 scopus 로고
    • Specificity of a milk clotting enzyme extracted from the thistle Cynara cardunculus L.; action on oxidized insulin and K-casein
    • Faro C, Moir A and Pires E, Specificity of a milk clotting enzyme extracted from the thistle Cynara cardunculus L.; action on oxidized insulin and K-casein. Biotechnol Lett 14:841-846 (1992).
    • (1992) Biotechnol Lett , vol.14 , pp. 841-846
    • Faro, C.1    Moir, A.2    Pires, E.3
  • 26
    • 0000093378 scopus 로고
    • Purification and characterization of an aspartyl proteinase from dry jack pine seeds
    • Bourgeois J and Malek L, Purification and characterization of an aspartyl proteinase from dry jack pine seeds. Seed Sci Res 1:139-147 (1991).
    • (1991) Seed Sci Res , vol.1 , pp. 139-147
    • Bourgeois, J.1    Malek, L.2
  • 27
    • 0020536688 scopus 로고
    • Ultrastructural localization of Bowman-Birk inhibitor on thin sections of Glycine max (soyabean) cv. Maple Arrow by the gold method
    • Horisberger M and Tacchini-Vonlanthen M, Ultrastructural localization of Bowman-Birk inhibitor on thin sections of Glycine max (soyabean) cv. Maple Arrow by the gold method. Histochemistry 77:37-50 (1983).
    • (1983) Histochemistry , vol.77 , pp. 37-50
    • Horisberger, M.1    Tacchini-Vonlanthen, M.2
  • 28
    • 0032008223 scopus 로고    scopus 로고
    • The abundant 31-kilodalton banana pulp protein is homologous to class-III acidic chitinases
    • Clendennen S, Lopez-Gomez R, Gomez-Lim M, Arntzen C and May G, The abundant 31-kilodalton banana pulp protein is homologous to class-III acidic chitinases. Phytochemistry 47:613-619 (1998).
    • (1998) Phytochemistry , vol.47 , pp. 613-619
    • Clendennen, S.1    Lopez-Gomez, R.2    Gomez-Lim, M.3    Arntzen, C.4    May, G.5
  • 29
    • 0033711401 scopus 로고    scopus 로고
    • Purification, cloning, and autoproteolytic processing of an aspartic proteinase from Centaurea calcitrapa
    • Domingos A, Cardoso P, Xue Z, Clemente A, Brodelius P and Pais M, Purification, cloning, and autoproteolytic processing of an aspartic proteinase from Centaurea calcitrapa. Eur J Biochem 267:6824-6831 (2000).
    • (2000) Eur J Biochem , vol.267 , pp. 6824-6831
    • Domingos, A.1    Cardoso, P.2    Xue, Z.3    Clemente, A.4    Brodelius, P.5    Pais, M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.