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Volumn 36, Issue 2, 1996, Pages 83-88

Characterization and chillproofing activity of two enzymes from Streptomyces species

Author keywords

[No Author keywords available]

Indexed keywords

STREPTOMYCES; ZEA MAYS;

EID: 0029686256     PISSN: 0233111X     EISSN: None     Source Type: Journal    
DOI: 10.1002/jobm.3620360204     Document Type: Article
Times cited : (3)

References (16)
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    • Studies on the production of exo-enzymes by antibiotic producing strains of Streptomyces species
    • EKA, O. U. and FOGARTY, W. M., 1974. Studies on the production of exo-enzymes by antibiotic producing strains of Streptomyces species. Nigerian Journal of Science, 1, 41-47.
    • (1974) Nigerian Journal of Science , vol.1 , pp. 41-47
    • Eka, O.U.1    Fogarty, W.M.2
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    • Selective isolation and enumeration of actinomycetes using rifampicin
    • MEDA, A., LACEY, J. and GOODFELLOW, M., 1981. Selective isolation and enumeration of actinomycetes using rifampicin. J. Appl. Bacteriol., 50, 289-291.
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  • 9
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    • Studies on the proteolytic enzymes of thermophilic Streptomyces. II. Identification of the organism and some conditions of protease formation
    • MISUZANA, K., ICHISHIMA, E. and YOSHIDA, F., 1966. Studies on the proteolytic enzymes of thermophilic Streptomyces. II. Identification of the organism and some conditions of protease formation. Agricultural and Biological Chemistry, 30, 35-41.
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  • 10
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    • Characterization of a thermostable α-amylase from Bacillus licheniformis
    • MORGAN, F. J. and PRIEST, F. G., 1981. Characterization of a thermostable α-amylase from Bacillus licheniformis. J. Appl. Bacteriol., 50, 107-109.
    • (1981) J. Appl. Bacteriol. , vol.50 , pp. 107-109
    • Morgan, F.J.1    Priest, F.G.2
  • 11
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    • Thermal stability of immobilized glucoamylase entrapped in polyacrylamide gels and bound to Sephadex G 50
    • MORIYAMA, S., NODA, A., NAKANISHI, K. and KAMIKUBO, T., 1980. Thermal stability of immobilized glucoamylase entrapped in polyacrylamide gels and bound to Sephadex G 50. Agricultural and Biological Chemistry, 44, 2047-2050.
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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.