메뉴 건너뛰기




Volumn 20, Issue 2, 2000, Pages 162-168

Purification of α-amylase isoenzymes from Scytalidium thermophilum on a fluidized bed of alginate beads followed by concanavalin A-agarose column chromatography

Author keywords

Alginate beads; Fluidized bed chromatography; S. thermophilum; Thermostable enzymes; amylase

Indexed keywords

ALGINIC ACID; AMYLASE; ANALYTIC METHOD; CONCANAVALIN A; ENZYME BINDING; ENZYME PURIFICATION; FLUIDIZED BED REACTOR; ISOENZYME; MOLECULAR WEIGHT; TEMPERATURE;

EID: 0033777126     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1006/prep.2000.1308     Document Type: Article
Times cited : (16)

References (40)
  • 8
    • 0031751080 scopus 로고    scopus 로고
    • Simultaneous measurement of α-amylase and glucoamylase activities in sake rice koji by capillary electrophoresis of sodium dodecyl sulfate-protein complexes and activity measurement of glucoamylase by in-capillary enzyme reaction method
    • (1998) Electrophoresis , vol.19 , pp. 2331-2337
    • Watanabe, T.1    Yamamoto, A.2    Nagai, S.3    Terabe, S.4
  • 25
    • 33747333106 scopus 로고
    • Use of dinitrosalicylic acid reagent for determination of reducing sugar
    • (1959) Anal. Chem. , vol.31 , pp. 426-428
    • Miller, G.L.1
  • 26
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 27
    • 0001232852 scopus 로고
    • An introduction to polyacrylamide gel electrophoresis
    • 'Gel Electrophoresis of Proteins: A Practical Approach' (Hames, B. D., and Rickwood, D., Eds.) IRL Press, Oxford
    • (1986) , pp. 1-86
    • Hames, B.D.1
  • 34
    • 0001051874 scopus 로고    scopus 로고
    • Amylases of the thermophilic fungus Thermomyces lanuginosus: Their purification, properties and action of starch and response to heat
    • (1996) J. Biosci. , vol.21 , pp. 653-672
    • Mishra, R.1    Maheshwari, R.2
  • 36
    • 0021754269 scopus 로고
    • Prediction of the performance of preparative affinity chromatography
    • (1984) J. Chromatogr. , vol.297 , pp. 179-202
    • Chase, H.A.1
  • 38
    • 0001927953 scopus 로고
    • Models of enzyme deactivation
    • 'Thermostability of Enzymes' (Gupta, M. N., Ed.), Springer-Verlag, Berlin/Narosa, India
    • (1993) , pp. 84-95
    • Sadana, A.1
  • 40
    • 0009877953 scopus 로고
    • Immobilization techniques for altering thermal stability of enzymes
    • 'Thermostability of Enzymes' (Gupta, M. N., Ed.), Springer-Verlag, Berlin/Narosa, India
    • (1993) , pp. 161-179
    • Cabral, J.M.S.1    Kennedy, J.F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.