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Volumn 110, Issue 6, 2010, Pages 670-674

Characterization of glucoamylase and α-amylase from Monascus anka: Enhanced production of α-amylase in red koji

Author keywords

Amylase; Enzyme production; Glucoamylase; Monascus anka; Red koji

Indexed keywords

ACIDIC PH; AMYLASE PRODUCTION; CULTURE CONDITIONS; EFFECT OF TEMPERATURE; ENZYME PRODUCTION; GLUCOAMYLASE; GLUCOAMYLASE PRODUCTION; GROWTH AREAS; LATE STAGE; MONASCUS; MYCELIAL GROWTH; PROTEIN STABILITY; PURIFIED ENZYME; RED KOJI; WAXY RICE;

EID: 78449233769     PISSN: 13891723     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jbiosc.2010.07.005     Document Type: Article
Times cited : (32)

References (31)
  • 1
    • 0019195217 scopus 로고
    • A new hypocholesterolemic agent that specifically inhibits 3-hydroxy-3-methylglutaryl coenzyme A reductase
    • Endo A., Monacolin K. A new hypocholesterolemic agent that specifically inhibits 3-hydroxy-3-methylglutaryl coenzyme A reductase. J. Antibiot. (Tokyo) 1980, 33:334-336.
    • (1980) J. Antibiot. (Tokyo) , vol.33 , pp. 334-336
    • Endo, A.1    Monacolin, K.2
  • 2
    • 0024810125 scopus 로고
    • Biochemical aspect of HMG CoA reductase inhibitors
    • Endo A., Hasumi K. Biochemical aspect of HMG CoA reductase inhibitors. Adv. Enzyme Regul. 1989, 28:53-64.
    • (1989) Adv. Enzyme Regul. , vol.28 , pp. 53-64
    • Endo, A.1    Hasumi, K.2
  • 3
    • 18544404963 scopus 로고    scopus 로고
    • Production and indentification of N-glucosylrubropunctamine and N-glucosylmonascorubramine from Monascus ruber and occurrence of electron donor-acceptor complexes in these red pigments
    • Hajaj H., Klaebe A., Loret M.O., Tzedakis T., Goma G., Blank P.J. Production and indentification of N-glucosylrubropunctamine and N-glucosylmonascorubramine from Monascus ruber and occurrence of electron donor-acceptor complexes in these red pigments. Appl. Environ. Microbiol. 1997, 63:2671-2678.
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 2671-2678
    • Hajaj, H.1    Klaebe, A.2    Loret, M.O.3    Tzedakis, T.4    Goma, G.5    Blank, P.J.6
  • 4
    • 0033588174 scopus 로고    scopus 로고
    • Improvement of red pigment/citrinin production ratio as a function of environmental conditions by Monacus ruber
    • Hajaj H., Blanc P.J., Groussac E., Goma G., Uribelarrea J.L., Loubiere P. Improvement of red pigment/citrinin production ratio as a function of environmental conditions by Monacus ruber. Biochnol. Bioeng. 1999, 64:497-501.
    • (1999) Biochnol. Bioeng. , vol.64 , pp. 497-501
    • Hajaj, H.1    Blanc, P.J.2    Groussac, E.3    Goma, G.4    Uribelarrea, J.L.5    Loubiere, P.6
  • 5
    • 0040037345 scopus 로고
    • Koji, in: B.J.B. Wood (Ed.), Microbiology of fermented food, Elsevier, New York
    • Lotong, N.: Koji, in: B.J.B. Wood (Ed.), Microbiology of fermented food, vol. 2. Elsevier, New York, pp. 252-254 (1985).
    • (1985) , vol.2 , pp. 252-254
    • Lotong, N.1
  • 6
    • 34648834899 scopus 로고
    • Chinese red rice Anka
    • Marcel Dekker, New York, K.H. Steinkraus, R.E. Cullen, C.S. Pederson, L.F. Nellis, B.K. Gavitt (Eds.)
    • Su Y.C., Wang W.H. Chinese red rice Anka. Handbook of indigenous fermented foods 1983, 547-553. Marcel Dekker, New York. K.H. Steinkraus, R.E. Cullen, C.S. Pederson, L.F. Nellis, B.K. Gavitt (Eds.).
    • (1983) Handbook of indigenous fermented foods , pp. 547-553
    • Su, Y.C.1    Wang, W.H.2
  • 7
    • 2142765421 scopus 로고
    • Enzymes affecting the fermentation of sake moromi-mash
    • Nunokawa Y., Sumiya S., Iwano K. Enzymes affecting the fermentation of sake moromi-mash. J. Ferment. Technol. 1978, 56:380-388.
    • (1978) J. Ferment. Technol. , vol.56 , pp. 380-388
    • Nunokawa, Y.1    Sumiya, S.2    Iwano, K.3
  • 8
    • 0036306294 scopus 로고    scopus 로고
    • Specific expression and temperature-dependent expression of the acid protease-encoding gene (pepA) in Aspergillus oryzae in solid-state culture (rice-koji)
    • Kitano H., Kataoka K., Furukawa K., Hara S. Specific expression and temperature-dependent expression of the acid protease-encoding gene (pepA) in Aspergillus oryzae in solid-state culture (rice-koji). J. Biosci. Bioeng. 2002, 93:563-567.
    • (2002) J. Biosci. Bioeng. , vol.93 , pp. 563-567
    • Kitano, H.1    Kataoka, K.2    Furukawa, K.3    Hara, S.4
  • 10
    • 37049019042 scopus 로고    scopus 로고
    • Some distinguishable properties between acid-stable and neutral types of α-amylase from acid-producing koji
    • Suganuma T., Fujita K., Kitahara K. Some distinguishable properties between acid-stable and neutral types of α-amylase from acid-producing koji. J. Biosci. Bioeng. 2007, 104:353-362.
    • (2007) J. Biosci. Bioeng. , vol.104 , pp. 353-362
    • Suganuma, T.1    Fujita, K.2    Kitahara, K.3
  • 11
    • 0020687024 scopus 로고
    • Subsite structure and ligand binding mechanism of glucoamylase
    • Hiromi K., Ohnishi M., Tanaka A. Subsite structure and ligand binding mechanism of glucoamylase. Mol. Cell. Biochem. 1983, 51:79-95.
    • (1983) Mol. Cell. Biochem. , vol.51 , pp. 79-95
    • Hiromi, K.1    Ohnishi, M.2    Tanaka, A.3
  • 12
    • 0017585290 scopus 로고
    • Purification and properties of two forms of glucoamylase from Monascus kaoliang NOV. SP. F-1
    • Iizuka H., Mineki S. Purification and properties of two forms of glucoamylase from Monascus kaoliang NOV. SP. F-1. J. Gen. Appl. Microbiol. 1977, 23:217-230.
    • (1977) J. Gen. Appl. Microbiol. , vol.23 , pp. 217-230
    • Iizuka, H.1    Mineki, S.2
  • 13
    • 36148973586 scopus 로고    scopus 로고
    • Purification and characterization of heterogeneous glucoamylases from Monascus purpureus
    • Tachibana S., Yasuda M. Purification and characterization of heterogeneous glucoamylases from Monascus purpureus. Biosci. Biotechnol. Biochem. 2007, 71:2573-2576.
    • (2007) Biosci. Biotechnol. Biochem. , vol.71 , pp. 2573-2576
    • Tachibana, S.1    Yasuda, M.2
  • 14
    • 0016638615 scopus 로고
    • Crystallization and preliminary X-ray investigation of soybean α-amylase
    • Morita Y., Aibara S., Yamashita H., Yagi F., Suganuma T. Crystallization and preliminary X-ray investigation of soybean α-amylase. J. Biochem. 1975, 77:343-351.
    • (1975) J. Biochem. , vol.77 , pp. 343-351
    • Morita, Y.1    Aibara, S.2    Yamashita, H.3    Yagi, F.4    Suganuma, T.5
  • 15
    • 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.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.M.1
  • 16
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature 1970, 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 17
    • 17444425679 scopus 로고    scopus 로고
    • Different control mechanisms regulate glucoamylase and protease gene transcription in Aspergillus oryzae in solid-state and submerged fermentation
    • te Biesebeke R., van Biezen N., de Vos W.M., van den Hondel C.A.M.J.J., Punt P.J. Different control mechanisms regulate glucoamylase and protease gene transcription in Aspergillus oryzae in solid-state and submerged fermentation. Appl. Microbiol. Biotechnol. 2005, 67:75-82.
    • (2005) Appl. Microbiol. Biotechnol. , vol.67 , pp. 75-82
    • te Biesebeke, R.1    van Biezen, N.2    de Vos, W.M.3    van den Hondel, C.A.M.J.J.4    Punt, P.J.5
  • 18
    • 33646570211 scopus 로고    scopus 로고
    • Proteomic analysis of extracellular proteins from Aspergillus oryzae grown under submerged and solid-state culture conditions
    • Oda K., Kakizono D., Yamada O., Iefuji H., Akita O., Iwashita K. Proteomic analysis of extracellular proteins from Aspergillus oryzae grown under submerged and solid-state culture conditions. Appl. Environ. Microbiol. 2006, 72:3448-3457.
    • (2006) Appl. Environ. Microbiol. , vol.72 , pp. 3448-3457
    • Oda, K.1    Kakizono, D.2    Yamada, O.3    Iefuji, H.4    Akita, O.5    Iwashita, K.6
  • 19
    • 51649122745 scopus 로고    scopus 로고
    • Temperature-dependent regulation of proteins in Aspergillus flavus: whole organism stable isotope labeling by amino acids
    • Georgianna D.R., Hawkridge A.M., Muddiman D.C., Payne G.A. Temperature-dependent regulation of proteins in Aspergillus flavus: whole organism stable isotope labeling by amino acids. J. Proteome Res. 2008, 7:2973-2979.
    • (2008) J. Proteome Res. , vol.7 , pp. 2973-2979
    • Georgianna, D.R.1    Hawkridge, A.M.2    Muddiman, D.C.3    Payne, G.A.4
  • 20
    • 0038735078 scopus 로고    scopus 로고
    • Three different types of α-amylases from Aspergillus awamori KT-11: their purifications, properties, and specificities
    • Anindyawati T., Melliawati R., Ito K., Iizuka M., Minamiura N. Three different types of α-amylases from Aspergillus awamori KT-11: their purifications, properties, and specificities. Biosci. Biotechnol. Biochem. 1998, 62:1351-1357.
    • (1998) Biosci. Biotechnol. Biochem. , vol.62 , pp. 1351-1357
    • Anindyawati, T.1    Melliawati, R.2    Ito, K.3    Iizuka, M.4    Minamiura, N.5
  • 21
    • 33846494025 scopus 로고    scopus 로고
    • Purification by expanded bed adsorption and characterization of an α-amylases FORILASE NTL® from A. niger
    • Toledo A.L., Severo J.B., Souza R.R., Campos E.S., Santana J.C.C., Tambourgi E.B. Purification by expanded bed adsorption and characterization of an α-amylases FORILASE NTL® from A. niger. J. Chromatogr. B 2007, 846:51-56.
    • (2007) J. Chromatogr. B , vol.846 , pp. 51-56
    • Toledo, A.L.1    Severo, J.B.2    Souza, R.R.3    Campos, E.S.4    Santana, J.C.C.5    Tambourgi, E.B.6
  • 22
    • 78449259292 scopus 로고
    • Biological control of phytopathogens and weeds
    • Marcel Dekker Inc, New York, D.K. Arora, K.G. Mukerji, E.H. Marth (Eds.)
    • Bigelis R. Biological control of phytopathogens and weeds. Handbook of applied mycology 1991, 3:293-328. Marcel Dekker Inc, New York. D.K. Arora, K.G. Mukerji, E.H. Marth (Eds.).
    • (1991) Handbook of applied mycology , vol.3 , pp. 293-328
    • Bigelis, R.1
  • 24
    • 0034095399 scopus 로고    scopus 로고
    • Growth, pigment production and protease activity of Monascus purpureus as affected by salt, sodium nitrite, polyphosphate and various sugars
    • Tseng Y.Y., Chen M.T., Lin C.F. Growth, pigment production and protease activity of Monascus purpureus as affected by salt, sodium nitrite, polyphosphate and various sugars. J. Appl. Microbiol. 2000, 88:31-37.
    • (2000) J. Appl. Microbiol. , vol.88 , pp. 31-37
    • Tseng, Y.Y.1    Chen, M.T.2    Lin, C.F.3
  • 25
    • 81155161131 scopus 로고    scopus 로고
    • Standard tables of food composition in Japan
    • Kagawa Nutrition University Publishing Division, Japan, (in Japanese), A. Kagawa (Ed.)
    • Kagawa Y. Standard tables of food composition in Japan. Standard tables of food composition in Japan fifth revised and enlarged edition 2008, 28-36. Kagawa Nutrition University Publishing Division, Japan, (in Japanese). A. Kagawa (Ed.).
    • (2008) Standard tables of food composition in Japan fifth revised and enlarged edition , pp. 28-36
    • Kagawa, Y.1
  • 26
    • 37449025531 scopus 로고    scopus 로고
    • Phylogenetic and biochemical characterization of a novel cluster of intracellular fungal α-amylase enzymes
    • van der Kaaij R.M., Janecek S., van der Maarel M.J.E.C., Dijkhuizen L. Phylogenetic and biochemical characterization of a novel cluster of intracellular fungal α-amylase enzymes. Microbiology 2007, 153:4003-4015.
    • (2007) Microbiology , vol.153 , pp. 4003-4015
    • van der Kaaij, R.M.1    Janecek, S.2    van der Maarel, M.J.E.C.3    Dijkhuizen, L.4
  • 27
    • 0017938730 scopus 로고
    • Effect of the composition of the medium and the conditions of Aspergillus foetidus cultivation on the biosynthesis of glucoamylase
    • Makhmud S.A., Mashkhur V.A., EI-Khaddad M.E., El-Gammal S.E. Effect of the composition of the medium and the conditions of Aspergillus foetidus cultivation on the biosynthesis of glucoamylase. Mikrobiologiia 1978, 47:220-225.
    • (1978) Mikrobiologiia , vol.47 , pp. 220-225
    • Makhmud, S.A.1    Mashkhur, V.A.2    EI-Khaddad, M.E.3    El-Gammal, S.E.4
  • 28
    • 0020523493 scopus 로고
    • Effect of the physiological conditions on α-amylase and glucoamylase formation by a selected strain of Aspergillus oryzae
    • Kassim E.A. Effect of the physiological conditions on α-amylase and glucoamylase formation by a selected strain of Aspergillus oryzae. Mikrobiologiia 1983, 52:422-427.
    • (1983) Mikrobiologiia , vol.52 , pp. 422-427
    • Kassim, E.A.1
  • 29
    • 33947186739 scopus 로고    scopus 로고
    • Simultaneous production of glucoamylase and acid-stable α-amylase using novel submerged culture of Aspergillus kawachii NBRC 4308
    • Shoji H., Sugimoto T., Hosoi K., Shibata K., Tanabe M., Kawatsura K. Simultaneous production of glucoamylase and acid-stable α-amylase using novel submerged culture of Aspergillus kawachii NBRC 4308. J. Biosci. Bioeng. 2007, 103:203-205.
    • (2007) J. Biosci. Bioeng. , vol.103 , pp. 203-205
    • Shoji, H.1    Sugimoto, T.2    Hosoi, K.3    Shibata, K.4    Tanabe, M.5    Kawatsura, K.6
  • 31
    • 43049162197 scopus 로고    scopus 로고
    • Application of a statistical design to the optimization of parameters and culture medium for α-amylase production by Aspergillus oryzae CBS 819.72 grown on gruel (wheat grinding by-product)
    • Kammoun R., Naili B., Bejar S. Application of a statistical design to the optimization of parameters and culture medium for α-amylase production by Aspergillus oryzae CBS 819.72 grown on gruel (wheat grinding by-product). Bioresour. Technol. 2008, 99:5602-5609.
    • (2008) Bioresour. Technol. , vol.99 , pp. 5602-5609
    • Kammoun, R.1    Naili, B.2    Bejar, S.3


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