메뉴 건너뛰기




Volumn 97, Issue 10, 2006, Pages 1217-1224

Enzymatic detergent formulation containing amylase from Aspergillus niger: A comparative study with commercial detergent formulations

Author keywords

Amylase; Aspergillus niger; Detergent formulation; Enzymatic detergents

Indexed keywords

BIODEGRADATION; DETERGENTS; DRAINAGE; ENZYMES; MEDICAL APPLICATIONS; PH EFFECTS;

EID: 33645975174     PISSN: 09608524     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biortech.2005.05.022     Document Type: Article
Times cited : (100)

References (26)
  • 1
    • 0029170412 scopus 로고
    • α-Amylase production by thermophilic Bacillus coagulans in solid state fermentation
    • Babu K.R., and Satyanarayana T. α-Amylase production by thermophilic Bacillus coagulans in solid state fermentation. Process Biochemistry 30 (1995) 305-309
    • (1995) Process Biochemistry , vol.30 , pp. 305-309
    • Babu, K.R.1    Satyanarayana, T.2
  • 2
    • 33748037939 scopus 로고
    • Colowick S.P., and Kaplan N.O. (Eds), Academic Press, New York
    • Benfeld P. In: Colowick S.P., and Kaplan N.O. (Eds). Methods in Enzymology vol. 1 (1955), Academic Press, New York 149
    • (1955) Methods in Enzymology , vol.1 , pp. 149
    • Benfeld, P.1
  • 3
    • 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. 72 (1976) 248-254
    • (1976) Anal Biochem. , vol.72 , pp. 248-254
    • Bradford, M.1
  • 4
    • 33645967325 scopus 로고
    • A tecnologia enzimática no Brasil
    • Bon E.P.S. A tecnologia enzimática no Brasil. ENZITEC 95 (1995) 9-14
    • (1995) ENZITEC , vol.95 , pp. 9-14
    • Bon, E.P.S.1
  • 5
    • 0000113960 scopus 로고    scopus 로고
    • Cereal grain starch and exogenous enzymes in poultry diets
    • Classen H.L. Cereal grain starch and exogenous enzymes in poultry diets. Animal Feed Science and Technology 62 (1996) 21-27
    • (1996) Animal Feed Science and Technology , vol.62 , pp. 21-27
    • Classen, H.L.1
  • 6
    • 0033955301 scopus 로고    scopus 로고
    • Production and biochemical characterization of an α-amylase from the moderate halophile Halomonas meridiana
    • Coronado M.J., Vargas C., Hofemeister J., Ventosa A., and Nieto J. Production and biochemical characterization of an α-amylase from the moderate halophile Halomonas meridiana. FEMS Microbiology Letters 183 (2000) 67-71
    • (2000) FEMS Microbiology Letters , vol.183 , pp. 67-71
    • Coronado, M.J.1    Vargas, C.2    Hofemeister, J.3    Ventosa, A.4    Nieto, J.5
  • 8
    • 0000844654 scopus 로고
    • Extracellular protease and amylase activities in ligninase-producing liquid culture of Phanerochaete chrysosporium
    • Dey S., Maiti T.K., Saha N., Banerjee R., and Bhattacharyya B.C. Extracellular protease and amylase activities in ligninase-producing liquid culture of Phanerochaete chrysosporium. Process Biochemistry 26 (1991) 325-329
    • (1991) Process Biochemistry , vol.26 , pp. 325-329
    • Dey, S.1    Maiti, T.K.2    Saha, N.3    Banerjee, R.4    Bhattacharyya, B.C.5
  • 9
    • 0037263637 scopus 로고    scopus 로고
    • Production and partial characterization of β-amylase by Xanthophyllomyces dentrorhous
    • Díaz A., Sieiro C., and Villa T.G. Production and partial characterization of β-amylase by Xanthophyllomyces dentrorhous. Letters in Applied Microbiology 36 (2003) 203-207
    • (2003) Letters in Applied Microbiology , vol.36 , pp. 203-207
    • Díaz, A.1    Sieiro, C.2    Villa, T.G.3
  • 10
    • 0000519206 scopus 로고
    • Amylases, amyloglucosidases and related glucanases
    • Rose A.H. (Ed), Academic Press, New York
    • Fogarty W.M., and Kelly C.T. Amylases, amyloglucosidases and related glucanases. In: Rose A.H. (Ed). Microbial Enzymes and Bioconversions (1980), Academic Press, New York 115-170
    • (1980) Microbial Enzymes and Bioconversions , pp. 115-170
    • Fogarty, W.M.1    Kelly, C.T.2
  • 11
    • 33645811843 scopus 로고
    • A new method for microdetermination of amylaseactivity by use of amylose as the substrate
    • Fuwa H. A new method for microdetermination of amylaseactivity by use of amylose as the substrate. Journal Biochemistry 41 (1954) 583-603
    • (1954) Journal Biochemistry , vol.41 , pp. 583-603
    • Fuwa, H.1
  • 12
    • 0030271795 scopus 로고    scopus 로고
    • Electron microscopic investigation of diffusion of Bacillus licheniformis α-amylase into starch granules
    • Helbert W., Schülein M., and Henrissat B. Electron microscopic investigation of diffusion of Bacillus licheniformis α-amylase into starch granules. International Journal Biological Macromolecules 19 (1996) 165-169
    • (1996) International Journal Biological Macromolecules , vol.19 , pp. 165-169
    • Helbert, W.1    Schülein, M.2    Henrissat, B.3
  • 13
    • 0037332979 scopus 로고    scopus 로고
    • Production of alpha amylase by Bacillus licheniformis using an economical médium
    • Ikram-Ul H., Ashraf H., Iqbal J., and Qadeer M.A. Production of alpha amylase by Bacillus licheniformis using an economical médium. Bioresource Technology 87 (2003) 57-61
    • (2003) Bioresource Technology , vol.87 , pp. 57-61
    • Ikram-Ul, H.1    Ashraf, H.2    Iqbal, J.3    Qadeer, M.A.4
  • 14
    • 0035139405 scopus 로고    scopus 로고
    • Thermostable α-amylase and -galactosidase production from the thermophilic and aerobic Bacillus sp. JF strain
    • Jin F., Li Y., Zhang C., and Yu H. Thermostable α-amylase and -galactosidase production from the thermophilic and aerobic Bacillus sp. JF strain. Process Biochemistry 36 (2001) 559-564
    • (2001) Process Biochemistry , vol.36 , pp. 559-564
    • Jin, F.1    Li, Y.2    Zhang, C.3    Yu, H.4
  • 15
    • 0035855207 scopus 로고    scopus 로고
    • Chemical modification of bacterial α-amylases: changes in tertiary structures and the effect of additional calcium
    • Khajeh K., Ranjbar B., Manesh H.N., Habibi A.E., and Gorgani M.N. Chemical modification of bacterial α-amylases: changes in tertiary structures and the effect of additional calcium. Biochimica and Biophysica Acta 1548 (2001) 229-237
    • (2001) Biochimica and Biophysica Acta , vol.1548 , pp. 229-237
    • Khajeh, K.1    Ranjbar, B.2    Manesh, H.N.3    Habibi, A.E.4    Gorgani, M.N.5
  • 16
    • 0343990713 scopus 로고    scopus 로고
    • Amylase production by solid state culture of Aspergillus oryzae on polyurethane foams. Some mechanistic approaches from an empirical model
    • Murado M.A., González M.P., Torrado A., and Pastrana L.M. Amylase production by solid state culture of Aspergillus oryzae on polyurethane foams. Some mechanistic approaches from an empirical model. Process Biochemistry 32 (1997) 35-42
    • (1997) Process Biochemistry , vol.32 , pp. 35-42
    • Murado, M.A.1    González, M.P.2    Torrado, A.3    Pastrana, L.M.4
  • 17
    • 0029361087 scopus 로고
    • Enzyme and microbial systems involved in starch processing
    • Nigam P., and Singh D. Enzyme and microbial systems involved in starch processing. Enzyme and Microbial Technology 17 (1995) 770-778
    • (1995) Enzyme and Microbial Technology , vol.17 , pp. 770-778
    • Nigam, P.1    Singh, D.2
  • 19
    • 84987177874 scopus 로고
    • Purification and characterization of thermophilic alpha-amylase of Aspergillus niger
    • Ramasesh N., Sreekantiah K.R., Murthy K.R., and Ramasesh V.S. Purification and characterization of thermophilic alpha-amylase of Aspergillus niger. Van Thieghem Starke 34 (1982) 274-279
    • (1982) Van Thieghem Starke , vol.34 , pp. 274-279
    • Ramasesh, N.1    Sreekantiah, K.R.2    Murthy, K.R.3    Ramasesh, V.S.4
  • 20
    • 0029737903 scopus 로고    scopus 로고
    • Induction and carbon catabolite repression in the biosynthesis of beta-amylase by Bacillus megaterium B-6
    • Ray R.R., Jana S.C., and Nanda G. Induction and carbon catabolite repression in the biosynthesis of beta-amylase by Bacillus megaterium B-6. Biochemistry and Molecular Biology International 38 (1996) 223-230
    • (1996) Biochemistry and Molecular Biology International , vol.38 , pp. 223-230
    • Ray, R.R.1    Jana, S.C.2    Nanda, G.3
  • 21
    • 0025162390 scopus 로고
    • Characterization of thermostable cyclodextrinase from Clostridium thermohydrosulfuricum 39 E
    • Saha B.C., and Zeikus J.G. Characterization of thermostable cyclodextrinase from Clostridium thermohydrosulfuricum 39 E. Applied and Environmental Microbiology 56 (1990) 2941-2943
    • (1990) Applied and Environmental Microbiology , vol.56 , pp. 2941-2943
    • Saha, B.C.1    Zeikus, J.G.2
  • 24
    • 0242473815 scopus 로고    scopus 로고
    • Production and characterization of a thermostable α-amylase from Nocardiopsis sp. Endophyte of yam bean
    • Stamford T.L.M., Stamford N.P., Coelho L.C.B.B., and Araújo J.M. Production and characterization of a thermostable α-amylase from Nocardiopsis sp. Endophyte of yam bean. Bioresource Technology 76 (2001) 137-141
    • (2001) Bioresource Technology , vol.76 , pp. 137-141
    • Stamford, T.L.M.1    Stamford, N.P.2    Coelho, L.C.B.B.3    Araújo, J.M.4
  • 25
    • 0031193688 scopus 로고    scopus 로고
    • The use of yam peel for growth of locally isolated Aspergillus niger and amylase production
    • Uguru G.C., Akinyanju J.A., and Sani A. The use of yam peel for growth of locally isolated Aspergillus niger and amylase production. Enzyme and Microbial Technology 21 (1997) 48-51
    • (1997) Enzyme and Microbial Technology , vol.21 , pp. 48-51
    • Uguru, G.C.1    Akinyanju, J.A.2    Sani, A.3
  • 26
    • 0034033652 scopus 로고    scopus 로고
    • α-Amylase production by Bacillus subtilis with dregs in an external-loop airlift bioreactor
    • Yuguo Z., Zhao W., and Xiaolong C. α-Amylase production by Bacillus subtilis with dregs in an external-loop airlift bioreactor. Biochemical Engineering Journal 5 (2000) 115-121
    • (2000) Biochemical Engineering Journal , vol.5 , pp. 115-121
    • Yuguo, Z.1    Zhao, W.2    Xiaolong, C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.