메뉴 건너뛰기




Volumn 8, Issue 18, 2009, Pages 4582-4589

Extracellular acid protease from Aspergillus niger I1: Purification and characterization

Author keywords

Acid protease; Aspergillopepsin; Aspergillus niger; Glycosylation; Purification

Indexed keywords

ACID PROTEINASE; ASPARTIC PROTEINASE; SEPHADEX;

EID: 70349515516     PISSN: None     EISSN: 16845315     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (48)

References (36)
  • 1
    • 0019063784 scopus 로고
    • Partial purification and characterization of a yeast extracellular acid protease
    • Alessandro M, Federico F (1980). Partial purification and characterization of a yeast extracellular acid protease. J. Dairy Sci. 63: 1397-2402.
    • (1980) J. Dairy Sci. , vol.63 , pp. 1397-2402
    • Alessandro, M.1    Federico, F.2
  • 3
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein dye binding
    • Bradford M (1976). A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein dye binding. Anal Biochem. 72: 248-254
    • (1976) Anal Biochem. , vol.72 , pp. 248-254
    • Bradford, M.1
  • 5
    • 0026766457 scopus 로고
    • Purification and characterization of two serine carboxypeptidases from Aspergillus niger and their use in C-terminal sequencing of proteins and peptide synthesis
    • Dal Degan F, Ribadeau-Dumas B, Breddam K (1992). Purification and characterization of two serine carboxypeptidases from Aspergillus niger and their use in C-terminal sequencing of proteins and peptide synthesis. Appl. Environ. Microbiol. 58: 2144-2152
    • (1992) Appl. Environ. Microbiol. , vol.58 , pp. 2144-2152
    • Dal Degan, F.1    Ribadeau-Dumas, B.2    Breddam, K.3
  • 6
    • 0034764850 scopus 로고    scopus 로고
    • Enhanced heterologous protein production in Aspergillus niger through pH control of extracellular protease activity
    • Dara OD, Wang L, Xu J, Darin R, Gu T, Murray MY (2001). Enhanced heterologous protein production in Aspergillus niger through pH control of extracellular protease activity. Biochem. Eng. J. 8: 187-193.
    • (2001) Biochem. Eng. J. , vol.8 , pp. 187-193
    • Dara, O.D.1    Wang, L.2    Xu, J.3    Darin, R.4    Gu, T.5    Murray, M.Y.6
  • 8
    • 84986450064 scopus 로고
    • Characterization of proteinase classes in Langostilla (Pleuroncodes planipes) and crayfish (Pacifastacus astacus) extracts
    • Garcia-Carreno FL, Haard NF (1993). Characterization of proteinase classes in Langostilla (Pleuroncodes planipes) and crayfish (Pacifastacus astacus) extracts. J. Food Biochem. 17: 97-113.
    • (1993) J. Food Biochem. , vol.17 , pp. 97-113
    • Garcia-Carreno, F.L.1    Haard, N.F.2
  • 9
    • 0027638536 scopus 로고
    • Cloning and nucleotide sequence of the acid protease-encoding gene (pepA) from Aspergillus oryzae
    • Gomi K, Arikawa K, Kamiya N, Kitamoto K, Kumagai C (1993). Cloning and nucleotide sequence of the acid protease-encoding gene (pepA) from Aspergillus oryzae. Biosci Biotechnol. Biochem. 57: 1095-1100
    • (1993) Biosci Biotechnol. Biochem. , vol.57 , pp. 1095-1100
    • Gomi, K.1    Arikawa, K.2    Kamiya, N.3    Kitamoto, K.4    Kumagai, C.5
  • 10
    • 0036323668 scopus 로고    scopus 로고
    • Bacterial alkaline proteases: Molecular approaches and industrial applications
    • Gupta R, Beg QK, Lorenz P (2002). Bacterial alkaline proteases: molecular approaches and industrial applications. Appl. Microbiol. Biotechnol. 59: 15-32.
    • (2002) Appl. Microbiol. Biotechnol. , vol.59 , pp. 15-32
    • Gupta, R.1    Beg, Q.K.2    Lorenz, P.3
  • 11
    • 0032980597 scopus 로고    scopus 로고
    • Optimization of milk clotting enzyme productivity by Penicillium oxalicum
    • Hashem AM (1999). Optimization of milk clotting enzyme productivity by Penicillium oxalicum. Biores Technol. 70: 203-207.
    • (1999) Biores Technol. , vol.70 , pp. 203-207
    • Hashem, A.M.1
  • 12
    • 0015610280 scopus 로고
    • Some properties of acid protease from the thermophilic Penicillium duponti K1014
    • Hashimoto H, Iwaasa T, Yokotsuka T (1973). Some properties of acid protease from the thermophilic Penicillium duponti K1014. Appl. Microbiol. 25: 578-583.
    • (1973) Appl. Microbiol. , vol.25 , pp. 578-583
    • Hashimoto, H.1    Iwaasa, T.2    Yokotsuka, T.3
  • 13
    • 84944043841 scopus 로고    scopus 로고
    • Aspergillopepsin I
    • Barrett,A.J., Rawlings,N.D. & Woessner,J.F. eds Elsevier, London
    • Ichishima E (2004). Aspergillopepsin I. In Handbook of Proteolytic Enzymes, 2 edn (Barrett,A.J., Rawlings,N.D. & Woessner,J.F. eds), pp. 92-99, Elsevier, London.
    • (2004) Handbook of Proteolytic Enzymes, 2 Edn , pp. 92-99
    • Ichishima, E.1
  • 15
    • 0029979080 scopus 로고    scopus 로고
    • Heterologous expression and site-directed mutagenesis studies on the activation mechanism and the roles of the basic residues in the prosegment of aspergillopepsinogen I
    • Inoue H, Hayashi T, Huang XP, Lu J, Athanda SBP, Kong K, Yamagata H, Ukada S, Takahashi K (1996). Heterologous expression and site-directed mutagenesis studies on the activation mechanism and the roles of the basic residues in the prosegment of aspergillopepsinogen I. Eur. J. Biochem. 237: 719-725
    • (1996) Eur. J. Biochem. , vol.237 , pp. 719-725
    • Inoue, H.1    Hayashi, T.2    Huang, X.P.3    Lu, J.4    Athanda, S.B.P.5    Kong, K.6    Yamagata, H.7    Ukada, S.8    Takahashi, K.9
  • 17
    • 0027352759 scopus 로고
    • Salt-tolerant and thermostable alkaline protease from Bacillus subtilis NCIM No.64
    • Kembhavi AA, Kulharni A, Pant AA (1993). Salt-tolerant and thermostable alkaline protease from Bacillus subtilis NCIM No.64. Appl. Biochem. Biotechnol. 38: 83-92.
    • (1993) Appl. Biochem. Biotechnol. , vol.38 , pp. 83-92
    • Kembhavi, A.A.1    Kulharni, A.2    Pant, A.A.3
  • 18
    • 13844298133 scopus 로고    scopus 로고
    • Extracellular acid protease from Rhizopus oryzae: Purification and characterization
    • Kumar S, Sharma NS, Saharan MR, Singh R (2005). Extracellular acid protease from Rhizopus oryzae: purification and characterization. Proc. Biochem. 40: 1701-1705.
    • (2005) Proc. Biochem. , vol.40 , pp. 1701-1705
    • Kumar, S.1    Sharma, N.S.2    Saharan, M.R.3    Singh, R.4
  • 19
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 21
    • 0036304602 scopus 로고    scopus 로고
    • Silencing of the aspergillopepsin B gene of Aspergillus awamori by antisense RNA expression of protease removal by gene disruption results in a large increase in Thaumatin production
    • Moralejo FJ, Cardoza RE, Gutierrez S, Lombraña M, Fierro F, Martin JF (2002). Silencing of the aspergillopepsin B gene of Aspergillus awamori by antisense RNA expression of protease removal by gene disruption results in a large increase in Thaumatin production. Appl Environ Microbiol. 68:3550-3559.
    • (2002) Appl Environ Microbiol. , vol.68 , pp. 3550-3559
    • Moralejo, F.J.1    Cardoza, R.E.2    Gutierrez, S.3    Lombraña, M.4    Fierro, F.5    Martin, J.F.6
  • 22
    • 0028213807 scopus 로고
    • Purification of protease using waste water from the manufacture of Shochu
    • Morimura S, Kida K, Sonoda Y (1994). Purification of protease using waste water from the manufacture of Shochu. J. Ferm. Bioeng. 77: 183-187.
    • (1994) J. Ferm. Bioeng. , vol.77 , pp. 183-187
    • Morimura, S.1    Kida, K.2    Sonoda, Y.3
  • 24
    • 70349489926 scopus 로고    scopus 로고
    • Some physicochemical properties of acid protease produced during growth of Aspergillus niger (NRRL 1785)
    • Olajuyigbe FM, Ajele JO, Olawoye, TL (2003). Some physicochemical properties of acid protease produced during growth of Aspergillus niger (NRRL 1785). Global J. Pure Appl. Sci. 9: 523-528.
    • (2003) Global J. Pure Appl. Sci. , vol.9 , pp. 523-528
    • Olajuyigbe, F.M.1    Ajele, J.O.2    Olawoye, T.L.3
  • 25
    • 56649097362 scopus 로고    scopus 로고
    • Optimization of conditions for acid protease partitioning and purification in aqueous two-phase systems using response surface methodology
    • Pericin DM, Madarev-Popovic SZ, Radulovic-Popovic LM (2009). Optimization of conditions for acid protease partitioning and purification in aqueous two-phase systems using response surface methodology. Biotechnol. Lett. 31: 43-47.
    • (2009) Biotechnol. Lett. , vol.31 , pp. 43-47
    • Pericin, D.M.1    Madarev-Popovic, S.Z.2    Radulovic-Popovic, L.M.3
  • 27
    • 0029056552 scopus 로고
    • Molecular cloning and sequencing of the gene encoding an extracellular aspartic proteinase from Aspergillus fumigatus
    • Reichard U, Monod M, Ruechel R (1995). Molecular cloning and sequencing of the gene encoding an extracellular aspartic proteinase from Aspergillus fumigatus. FEMS. Microbiol. Lett. 130: 69-74.
    • (1995) FEMS. Microbiol. Lett. , vol.130 , pp. 69-74
    • Reichard, U.1    Monod, M.2    Ruechel, R.3
  • 28
    • 0014273840 scopus 로고
    • Purification and properties of Mucor pusillus acid protease
    • Somkuti G/A, Babel FJ (1968). Purification and properties of Mucor pusillus acid protease. J. Bacteriol. 95: 1407-1414
    • (1968) J. Bacteriol. , vol.95 , pp. 1407-1414
    • Somkuti, G.A.1    Babel, F.J.2
  • 29
    • 33745821234 scopus 로고    scopus 로고
    • Microbiology and industrial biotechnology of food-grade proteases: A perspective
    • Sumantha A, Larroche C, Pandey A (2006). Microbiology and industrial biotechnology of food-grade proteases: a perspective. Food Technol. Biotechnol. 44: 211-220.
    • (2006) Food Technol. Biotechnol. , vol.44 , pp. 211-220
    • Sumantha, A.1    Larroche, C.2    Pandey, A.3
  • 31
    • 0028871971 scopus 로고
    • Effect of irreversibility on the thermodynamic characterization of the thermal denaturation of Aspergillus saitoi acid proteinase
    • Tello-Solis SR, Hernandez-Arana A (1995). Effect of irreversibility on the thermodynamic characterization of the thermal denaturation of Aspergillus saitoi acid proteinase. Biochem. J. 311: 969-974
    • (1995) Biochem. J. , vol.311 , pp. 969-974
    • Tello-Solis, S.R.1    Hernandez-Arana, A.2
  • 32
    • 0017821223 scopus 로고
    • Purification and characterization of the two molecular forms of membrane acid protease from Aspergillus oryzae
    • DOI 10.1111/j.1432-1033.1978.tb12174.x
    • Tsujita Y, Endo A (1978). Purification and characterization of the two molecular forms of membrane acid protease from Aspergillus oryzae. Eur. J. Biochem. 15: 347-353. (Pubitemid 8301263)
    • (1978) European Journal of Biochemistry , vol.84 , Issue.2 , pp. 347-353
    • Tsujita, Y.1    Endo, A.2
  • 34
    • 0003074147 scopus 로고
    • Proteinases
    • WM. (Ed.): Applied Science Publishers. New York.
    • Ward OP (1983). Proteinases. In Microbiol Enzymes and Biotechnology Fogarty, WM. (Ed.): Applied Science Publishers. New York. 251-305.
    • (1983) Microbiol Enzymes and Biotechnology Fogarty , pp. 251-305
    • Ward, O.P.1
  • 35
    • 0031823808 scopus 로고    scopus 로고
    • Purification and characterization of acid proteinase from Neosartorya fischeri var. spinosa IBT 4872
    • Wu LC, Hang YD (1998). Purification and characterization of acid proteinase from Neosartorya fischeri var. spinosa IBT 4872. Lett. Appl. Microbiol. 27: 71-75.
    • (1998) Lett. Appl. Microbiol. , vol.27 , pp. 71-75
    • Wu, L.C.1    Hang, Y.D.2
  • 36
    • 0025260415 scopus 로고
    • Purification and characterization of an extracellular acid proteinase from the ectomycorrhizal fungus Hebeloma crustuliniforme
    • Zhu H, Guo DC, Dancik BP (1990). Purification and characterization of an extracellular acid proteinase from the ectomycorrhizal fungus Hebeloma crustuliniforme. Appl. Environ. Microbiol. 56: 837-843. (Pubitemid 20114430)
    • (1990) Applied and Environmental Microbiology , vol.56 , Issue.4 , pp. 837-843
    • Zhu, H.1    Guo, D.-C.2    Dancik, B.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.