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Volumn 63, Issue 5, 1999, Pages 805-812

Production and Properties of the Linamarase and Amygdalase Activities of Penicillium aurantiogriseum P35

Author keywords

Anthocyanin; Nasunin; Oxidative stress; Paraquat

Indexed keywords

BETA GLUCOSIDASE; CYANOGENIC BETA GLUCOSIDASE; CYANOGENIC BETA-GLUCOSIDASE; ENZYME INHIBITOR;

EID: 0033125289     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.63.805     Document Type: Article
Times cited : (4)

References (43)
  • 1
    • 0002157873 scopus 로고
    • Properties and functions of the cyanogenic system in higher plants
    • Kakes, P., Properties and functions of the cyanogenic system in higher plants. Euphytica, 48, 25-43 (1990).
    • (1990) Euphytica , vol.48 , pp. 25-43
    • Kakes, P.1
  • 2
    • 0001134935 scopus 로고
    • Kinetic properties of /Tglucosidase from cassava
    • Yeoh, H.-H., Kinetic properties of /Tglucosidase from cassava. Phytochem., 28, 721-724 (1989).
    • (1989) Phytochem. , vol.28 , pp. 721-724
    • Yeoh, H.-H.1
  • 3
    • 0026543728 scopus 로고
    • Bitter cassava poisoning in eight children: A case report
    • Espinoza, O. B., Perez, M., and Raminez, M., Bitter cassava poisoning in eight children: a case report. Vet. Hum. Toxicol., 34, 65-68 (1992).
    • (1992) Vet. Hum. Toxicol. , vol.34 , pp. 65-68
    • Espinoza, O.B.1    Perez, M.2    Raminez, M.3
  • 4
    • 0026767790 scopus 로고
    • An outbreak of acute intoxications from consumption of insufficiently processed cassava in Tanzania
    • Mlingi, N., Poulter, N., and Rosling, H., An outbreak of acute intoxications from consumption of insufficiently processed cassava in Tanzania. Nutr. Res., 12, 677-687 (1992).
    • (1992) Nutr. Res. , vol.12 , pp. 677-687
    • Mlingi, N.1    Poulter, N.2    Rosling, H.3
  • 5
    • 0001743004 scopus 로고
    • Chronic cyanide intoxication of dietary origin and a degenerative neuropathy in Nigerians
    • Osuntokun, B. O., Chronic cyanide intoxication of dietary origin and a degenerative neuropathy in Nigerians. Acta Horticul-turae, 375, 311-321 (1994).
    • (1994) Acta Horticul-Turae , vol.375 , pp. 311-321
    • Osuntokun, B.O.1
  • 6
    • 0013233142 scopus 로고
    • The association between cassava and the paralytic disease Konzo
    • Tylleskar, T., The association between cassava and the paralytic disease Konzo. Acta Horticulturae, 375, 331-339 (1994).
    • (1994) Acta Horticulturae , vol.375 , pp. 331-339
    • Tylleskar, T.1
  • 7
  • 8
    • 0002335391 scopus 로고
    • A-glucosidase: Overview
    • Esen, A., ACS Symposium Series 533, American Chemical Society, Washington
    • Esen, A., a-glucosidase: overview. In: “/Tglucosidases, biochemistry and molecular biology”, ed. Esen, A., ACS Symposium Series 533, American Chemical Society, Washington, pp. 1-14 (1993).
    • (1993) Tglucosidases, Biochemistry and Molecular Biology , pp. 1-14
    • Esen, A.1
  • 9
    • 0028871182 scopus 로고
    • Microbial degradation of amygdalin of bitter apricot seeds (Prunus armeniaca)
    • Nout, M. J. R., Tuncel, G., and Brimer, L., Microbial degradation of amygdalin of bitter apricot seeds (Prunus armeniaca). Int. J. Food Microbiol., 24, 407-412 (1995).
    • (1995) Int. J. Food Microbiol. , vol.24 , pp. 407-412
    • Nout, M.J.R.1    Tuncel, G.2    Brimer, L.3
  • 10
    • 0029334536 scopus 로고
    • Cyanide detoxification in cassava for food and feed uses
    • Padmaja, G., Cyanide detoxification in cassava for food and feed uses. Crit. Rev. Food Sci. Nutrition, 35, 299-339 (1995).
    • (1995) Crit. Rev. Food Sci. Nutrition , vol.35 , pp. 299-339
    • Padmaja, G.1
  • 11
    • 0005789287 scopus 로고
    • Enzymology of cyanogenesis in Rosaceous stone fruit
    • Esen, A., ACS Symposium Series 533, American Chemical Society, Washington
    • Poulton, J. E., Enzymology of cyanogenesis in Rosaceous stone fruit. In “/I-glucosidases, biochemistry and molecular biology”, ed. Esen, A., ACS Symposium Series 533, American Chemical Society, Washington, pp. 170-190 (1993).
    • (1993) I-Glucosidases, Biochemistry and Molecular Biology , pp. 170-190
    • Poulton, J.E.1
  • 12
    • 0000367038 scopus 로고
    • Simple screening procedure for microorganisms to degrade amygdalin
    • Brimer, L., Tuncel, G., and Nout, M. J. R., Simple screening procedure for microorganisms to degrade amygdalin. Biotechnol. Techn., 7, 683-687 (1993).
    • (1993) Biotechnol. Techn. , vol.7 , pp. 683-687
    • Brimer, L.1    Tuncel, G.2    Nout, M.J.R.3
  • 13
    • 0027954138 scopus 로고
    • Production of beta-glycosidases (Linamarase and amygdalase) and pectolytic enzymes by Penicillium spp. World. J
    • Brimer, L., Cicalini, A. R., Federici, F., and Petruccioli, M., Production of beta-glycosidases (linamarase and amygdalase) and pectolytic enzymes by Penicillium spp. World. J. Microbiol. Biotechnol., 10, 203-206 (1994).
    • (1994) Microbiol. Biotechnol. , vol.10 , pp. 203-206
    • Brimer, L.1    Cicalini, A.R.2    Federici, F.3    Petruccioli, M.4
  • 15
    • 0030988789 scopus 로고    scopus 로고
    • Purification and characterization of an intracellular y8-glucosidases from a new strain of Leuconostoc mesenteroides isolated from cassava
    • Gueguen, Y., Chemardin, P., Labrot, P., Arnaud, A., and Galzy, P., Purification and characterization of an intracellular y8-glucosidases from a new strain of Leuconostoc mesenteroides isolated from cassava. J. Appl. Microbiol., 82, 469-476 (1997).
    • (1997) J. Appl. Microbiol. , vol.82 , pp. 469-476
    • Gueguen, Y.1    Chemardin, P.2    Labrot, P.3    Arnaud, A.4    Galzy, P.5
  • 16
    • 0031281652 scopus 로고    scopus 로고
    • Glucose oxidase overproduction by the mutant strain M-80.10 of Penicillium variable in benchtop fermenter
    • Petruccioli, M., Piccioni, P., and Federici, F., Glucose oxidase overproduction by the mutant strain M-80.10 of Penicillium variable in benchtop fermenter. Enzyme Microb. Technol., 21, 458-462 (1997).
    • (1997) Enzyme Microb. Technol. , vol.21 , pp. 458-462
    • Petruccioli, M.1    Piccioni, P.2    Federici, F.3
  • 17
    • 84988164352 scopus 로고
    • Studies on the quantification of specific cyanogens in cassava products and introduction of a new chromogen
    • Essers, A. J. A., Bosveld, M., Van der Grift, R. M., and Voragen, A. G. J., Studies on the quantification of specific cyanogens in cassava products and introduction of a new chromogen. J. Sci. Food Agric., 63, 287-296 (1993).
    • (1993) J. Sci. Food Agric. , vol.63 , pp. 287-296
    • Essers, A.J.A.1    Bosveld, M.2    Van Der Grift, R.M.3    Voragen, A.G.J.4
  • 18
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during of the assembly of the head of bacterriophage T4
    • Laemmli, U. K., Cleavage of structural proteins during of the assembly of the head of bacterriophage T4. Nature, 227, 680-685 (1970).
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 19
    • 0003709143 scopus 로고
    • Isoelectric focusing: Theory, methodology and appliations
    • In, eds. Work, T. W., and Burdon, R. H., Elsevier Biomedical Press, Amsterdam
    • Righetti, P. G., Isoelectric focusing: theory, methodology and appliations. In “Laboratory techniques in biochemistry and molecular biology”, eds. Work, T. W., and Burdon, R. H., Elsevier Biomedical Press, Amsterdam, pp. 175-180 (1987).
    • (1987) Laboratory Techniques in Biochemistry and Molecular Biology , pp. 175-180
    • Righetti, P.G.1
  • 20
    • 0017184389 scopus 로고
    • A rapid and sensitive method for quantification of microgram quantities of protein utilizing the principle of protein dye binding
    • Bradford, M., A rapid and sensitive method for quantification of microgram quantities of protein utilizing the principle of protein dye binding. Anal. Biochem., 72, 248-254 (1976).
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.1
  • 21
    • 0024812439 scopus 로고
    • Purification and properties of the /Tglucosidase from a nitrile hydratase-producing Brevibacterium sp. Strain R312
    • Legras, J. L., Kaakeh, M. R., Arnaud, A., and Galzy, P., Purification and properties of the /Tglucosidase from a nitrile hydratase-producing Brevibacterium sp. strain R312. J. Basic. Microbiol., 29, 655-669 (1989).
    • (1989) J. Basic. Microbiol. , vol.29 , pp. 655-669
    • Legras, J.L.1    Kaakeh, M.R.2    Arnaud, A.3    Galzy, P.4
  • 22
    • 0013611553 scopus 로고
    • Influence of media composition on linamarase production by some fungi
    • Abalaka, J. A., and Garba, S. A., Influence of media composition on linamarase production by some fungi. Agric. Biol. Chem., 53, 561-563 (1989).
    • (1989) Agric. Biol. Chem. , vol.53 , pp. 561-563
    • Abalaka, J.A.1    Garba, S.A.2
  • 23
    • 84985320957 scopus 로고
    • The linamarase of Leuconostoc mesenteroides: Production, isolation and some properties
    • Okafor, N., and Ejiofor, M. A. N., The linamarase of Leuconostoc mesenteroides: Production, isolation and some properties. J. Sci. Food Agric., 36, 669-678 (1985).
    • (1985) J. Sci. Food Agric. , vol.36 , pp. 669-678
    • Okafor, N.1    Ejiofor, M.A.N.2
  • 24
    • 0026710201 scopus 로고
    • Degradation of cassava linamarin by lactic acid bacteria
    • Giraud, E., Gosselin, L., and Raimbault, M., Degradation of cassava linamarin by lactic acid bacteria. Biotehnol. Lett., 14, 593-598 (1992).
    • (1992) Biotehnol. Lett. , vol.14 , pp. 593-598
    • Giraud, E.1    Gosselin, L.2    Raimbault, M.3
  • 25
    • 0029139174 scopus 로고
    • Origin of enzymes involved in detoxification and root softening during cassava retting
    • Ampe, F., and Brauman, A., Origin of enzymes involved in detoxification and root softening during cassava retting. World. J. Microbiol. Biotechnol., 11, 178-182 (1995).
    • (1995) J. Microbiol. Biotechnol. , vol.11 , pp. 178-182
    • Ampe, F.1    Brauman, A.2
  • 27
    • 0030776779 scopus 로고    scopus 로고
    • The contribution of moulds and yeasts to the fermentation of ‘agbelima’ cassava dough
    • Amoa-Awua, W. K., Frisvad, J. C., Sefa-Dedeh, S., and Jakobsen, M., The contribution of moulds and yeasts to the fermentation of ‘agbelima’ cassava dough. J. Appl. Microbiol., 83, 288-296 (1997).
    • (1997) J. Appl. Microbiol. , vol.83 , pp. 288-296
    • Amoa-Awua, W.K.1    Frisvad, J.C.2    Sefa-Dedeh, S.3    Jakobsen, M.4
  • 28
    • 0042576647 scopus 로고
    • Studies on cellulose metabolism by yeast
    • Sill, A. M., and Stewart, G. G., Studies on cellulose metabolism by yeast. Dev. Ind. Microbiol., 26, 527-534 (1984).
    • (1984) Dev. Ind. Microbiol. , vol.26 , pp. 527-534
    • Sill, A.M.1    Stewart, G.G.2
  • 29
    • 0023108707 scopus 로고
    • Effect of media composition and growth conditions on production of cellulase and /5-glucosidase by a mixed fungal fermentation
    • Duff, S. J. B., Cooper, D. G., and Fuller, O. M., Effect of media composition and growth conditions on production of cellulase and /5-glucosidase by a mixed fungal fermentation. Enzyme Microb. Technol., 9, 47-52 (1987).
    • (1987) Enzyme Microb. Technol. , vol.9 , pp. 47-52
    • Duff, S.J.B.1    Cooper, D.G.2    Fuller, O.M.3
  • 30
    • 0029680252 scopus 로고    scopus 로고
    • Temperature-induced dénaturation of /5-glycosidase from the Archeon Sulfolobus sol-fataricus
    • D’Auria, S., Rossi, M., Barone, G., Catanzano, F., Del Vecchio, P., Graziano, G., and Nucci, R., Temperature-induced dénaturation of /5-glycosidase from the Archeon Sulfolobus sol-fataricus. J. Biochem., 120, 292-300 (1996).
    • (1996) J. Biochem. , vol.120 , pp. 292-300
    • D’auria, S.1    Rossi, M.2    Barone, G.3    Catanzano, F.4    Del Vecchio, P.5    Graziano, G.6    Nucci, R.7
  • 31
    • 0001334290 scopus 로고
    • Purification and characterization of a /i-glucosidase (Linamarase) from the haemo-lymph of Zygaena trifolii Esper, 1783 (Insecta, Lepidoptera)
    • Franzl, S., Ackermann, I., and Nahrstedt, A., Purification and characterization of a /i-glucosidase (linamarase) from the haemo-lymph of Zygaena trifolii Esper, 1783 (Insecta, Lepidoptera). Ex-perientia, 45, 712-717 (1989).
    • (1989) Ex-Perientia , vol.45 , pp. 712-717
    • Franzl, S.1    Ackermann, I.2    Nahrstedt, A.3
  • 32
    • 0022379565 scopus 로고
    • Isolation and characterization of two cyanogenic /Tglucosidases from flax seeds
    • Fan, T. W.-M., and Conn, E. E., Isolation and characterization of two cyanogenic /Tglucosidases from flax seeds. Arch. Biochem. Biophys., 243, 361-373 (1985).
    • (1985) Arch. Biochem. Biophys. , vol.243 , pp. 361-373
    • Fan, T.W.1    Conn, E.E.2
  • 33
    • 0027479060 scopus 로고
    • Crystallization and preliminary crystallographic analysis of the cyanogenic /Tglucosidase from the white clover Trifolium repens L
    • Tolley, S. P., Barrett, T. E., Suresh, C. G., and Hughes, M. A., Crystallization and preliminary crystallographic analysis of the cyanogenic /Tglucosidase from the white clover Trifolium repens L. J. Mol. Biol, 229, 791-793 (1993).
    • (1993) J. Mol. Biol , vol.229 , pp. 791-793
    • Tolley, S.P.1    Barrett, T.E.2    Suresh, C.G.3    Hughes, M.A.4
  • 34
    • 85004246138 scopus 로고
    • Purification of two β-glucosidases from P. Herquei Banier and Sartoro
    • Funaguma, T., and Hara, A., Purification of two β-glucosidases from P. herquei Banier and Sartoro. Agric. Biol. Chem., 52, 749-755 (1988).
    • (1988) Agric. Biol. Chem. , vol.52 , pp. 749-755
    • Funaguma, T.1    Hara, A.2
  • 35
    • 0026844932 scopus 로고
    • YS-glucosidase from Pénicillium purpurogenum: Purification and properties
    • Hidalgo, M., Steiner, J., and Eyzaguirre, J., yS-glucosidase from Pénicillium purpurogenum: purification and properties. Biotechnol. Appl. Biochem., 15, 185-191 (1992).
    • (1992) Biotechnol. Appl. Biochem , vol.15 , pp. 185-191
    • Hidalgo, M.1    Steiner, J.2    Eyzaguirre, J.3
  • 38
    • 0021051662 scopus 로고
    • Determination of cyanogenic compounds by Thin-Layer Chromatography. 1. A densitometric method for quantification of cyanogenic glycosides, employing enzyme preparations (/?-glucuronidase) from Helix pomatia and picrate-impregnated ion-exchange sheets
    • Brimer, L., Christensen, S. B., Molgaard, P., and Nartey, F., Determination of cyanogenic compounds by Thin-Layer Chromatography. 1. A densitometric method for quantification of cyanogenic glycosides, employing enzyme preparations (/?-glucuronidase) from Helix pomatia and picrate-impregnated ion-exchange sheets. J. Agric. Food Chem., 31, 789-793 (1983).
    • (1983) J. Agric. Food Chem. , vol.31 , pp. 789-793
    • Brimer, L.1    Christensen, S.B.2    Molgaard, P.3    Nartey, F.4
  • 39
    • 0022725310 scopus 로고
    • Comparison of kinetic and molecular properties of two forms of amygdalin hydrolase from black cherry (Prunus serotina Ehrh.) seeds
    • Kuroki, G. W., and Poulton, J. E., Comparison of kinetic and molecular properties of two forms of amygdalin hydrolase from black cherry (Prunus serotina Ehrh.) seeds. Arch. Biochem. Biophys., 247, 433-439 (1986).
    • (1986) Arch. Biochem. Biophys. , vol.247 , pp. 433-439
    • Kuroki, G.W.1    Poulton, J.E.2
  • 40
    • 0000974053 scopus 로고
    • Hevea linamarase —a nonspecific /Lglycosidase
    • Selmar, D., Lieberei, R., Biehl, B., and Viogt, J., Hevea linamarase —a nonspecific /Lglycosidase. Plant Physiol., 83, 557-563 (1987).
    • (1987) Plant Physiol. , vol.83 , pp. 557-563
    • Selmar, D.1    Lieberei, R.2    Biehl, B.3    Viogt, J.4
  • 41
    • 0028056118 scopus 로고
    • Some properties of /1-glucosi-dases from tropical plant species
    • Yeoh, H.-H., and Wee, Y.-C., Some properties of /1-glucosi-dases from tropical plant species. Phytochem., 35, 1391-1393 (1994).
    • (1994) Phytochem. , vol.35 , pp. 1391-1393
    • Yeoh, H.-H.1    Wee, Y.-C.2
  • 42
    • 0014094888 scopus 로고
    • Inhibition of glycosides by aldonolactones of corresponding configuration
    • Conchie, J., Gelmanm A. L., and Levvy, G. A., Inhibition of glycosides by aldonolactones of corresponding configuration. Biochem. J., 103, 609-615 (1967).
    • (1967) Biochem. J. , vol.103 , pp. 609-615
    • Conchie, J.1    Gelmanm, A.L.2    Levvy, G.A.3
  • 43
    • 0024720439 scopus 로고
    • Kinetic inves-tigtion of the substrate specificity of the cyanogenic yg-D-glucosi-dase (Linamarase) of white clover
    • Pocsi, I., Kiss, L., Hughes, M. A., and Nanasi, P., Kinetic inves-tigtion of the substrate specificity of the cyanogenic yg-D-glucosi-dase (linamarase) of white clover. Arch. Biochem. Biophys., 272, 496-506 (1989)
    • (1989) Arch. Biochem. Biophys. , vol.272 , pp. 496-506
    • Pocsi, I.1    Kiss, L.2    Hughes, M.A.3    Nanasi, P.4


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