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Volumn 37, Issue 1, 2005, Pages 155-161

A survey of amylolytic bacteria and fungi from native environmental samples

Author keywords

[No Author keywords available]

Indexed keywords

ASPERGILLUS; ASPERGILLUS SP.; BACILLUS SP.; BACTERIA (MICROORGANISMS); FUNGI;

EID: 18944375446     PISSN: 05563321     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (13)

References (16)
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  • 2
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    • High temperature alkaline α - Amylase from Bacillus licheniformis
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    • (1989) Biotech. Bioeng. , vol.33 , pp. 72-76
    • Bajpai, P.1
  • 4
    • 0030874212 scopus 로고    scopus 로고
    • Induction of α-amylase by maltooligosaccharide in Thermomonospora curvata
    • Busch, I.E., E.G. Porter and F.J. Stutzberger. 1996. Induction of α-amylase by maltooligosaccharide in Thermomonospora curvata. J. Appl. Microbiol., 82: 669-676.
    • (1996) J. Appl. Microbiol. , vol.82 , pp. 669-676
    • Busch, I.E.1    Porter, E.G.2    Stutzberger, F.J.3
  • 5
    • 0034799919 scopus 로고    scopus 로고
    • Influence of Carbon source on α-amylase production by Aspergillus oryzae
    • Carlsen, M. and J. Nielsen. 2001. Influence of Carbon source on α-amylase production by Aspergillus oryzae. Appl. Microbiol. Biotechnol., 57(3): 346-349.
    • (2001) Appl. Microbiol. Biotechnol. , vol.57 , Issue.3 , pp. 346-349
    • Carlsen, M.1    Nielsen, J.2
  • 7
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    • Activity and stability of a thermostable α-amylase compared to its mesophilic homologue: Mechanism of thermal adaptation
    • Fitter, J., R., Herrmann, N.A., Dencher, A., Blume and T. Hauss. 2001. Activity and stability of a thermostable α-amylase compared to its mesophilic homologue : mechanism of thermal adaptation. Biochem., 40(35): 10723-10731.
    • (2001) Biochem. , vol.40 , Issue.35 , pp. 10723-10731
    • Fitter, J.1    Herrmann, R.2    Dencher, N.A.3    Blume, A.4    Hauss, T.5
  • 8
    • 18944391288 scopus 로고
    • Microbial Amylases
    • (Ed.) W. M. Fogarty. Academic Press Inc. New York
    • Fogarty, W. and C.T. Kelly. 1990. Microbial Amylases. In: Industrial Enzymes. (Ed.) W. M. Fogarty. Academic Press Inc. New York
    • (1990) Industrial Enzymes
    • Fogarty, W.1    Kelly, C.T.2
  • 9
    • 33645811843 scopus 로고
    • A new method of microdetermination of amylase activity by the use of amylose as a substrate
    • Fuwa, H. 1954. A new method of microdetermination of amylase activity by the use of amylose as a substrate. J. Biochem., 41: 583-603.
    • (1954) J. Biochem. , vol.41 , pp. 583-603
    • Fuwa, H.1
  • 11
    • 0035318737 scopus 로고    scopus 로고
    • Novel α-amylase that is highly resistant to chelating agents and chemical oxidants from the alkalophilic Bacillus isolate KSM - K38
    • Highara, H., K. Igarashi, Y. Hayashi, K. Endo, K. Ikawa-Kitayama, K. Ozaki, S. Kawai and S. Ito. 2001. Novel α-amylase that is highly resistant to chelating agents and chemical oxidants from the alkalophilic Bacillus isolate KSM - K38. Appl. Environ. Microbiol., 67(4): 1744-1750.
    • (2001) Appl. Environ. Microbiol. , vol.67 , Issue.4 , pp. 1744-1750
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  • 12
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    • Production and properties of a raw starch-degrading amylase from the thermophilic and alkaliphilic Bacillus Sp. TS - 23
    • Lin, L.L., C.C., Chyan and W.H. Hsu. 1998. Production and properties of a raw starch-degrading amylase from the thermophilic and alkaliphilic Bacillus Sp. TS - 23. Biotechnol. Appl. Biochem., 28(1): 61-68.
    • (1998) Biotechnol. Appl. Biochem. , vol.28 , Issue.1 , pp. 61-68
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  • 13
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    • Mayes, A.P.1
  • 15
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    • Narang S. and T. Satyanarayama. 2001. Thermostable α-amylase by extreme thermophile Bacillus thermooleovorans. Lett. Appl. Microbiol., 32(1): 31-5.
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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.