Comparative studies on trifluoroethanol (TFE) state of a thermophilic α-amylase and its mesophilic counterpart: Limited proteolysis, conformational analysis, aggregation and reactivation of the enzymes

International Journal of Biological Macromolecules

Volumn 34, Issue 3, 2004, Pages 173-179

  Asghari, S Mohsen ^a   Khajeh, Khosro ^a   Ranjbar, Bijan ^a   Sajedi, Reza H ^a   Naderi Manesh, Hossein ^a  

^a TARBIAT MODARES UNIVERSITY   (Iran)

Author keywords

1 anilino naphthalene 8 sulfonate; ANS; BAA; BLA; EPS; p nitrophenyl D maltoheptaoside 4,6 O ethylidene; SEC; TFE; thermolysin; TL; trifluoroethanol; amylase from Bacillus amyloliquefaciens; amylase from Bacillus licheniformis

Indexed keywords

8 ANILINO 1 NAPHTHALENESULFONIC ACID; AMYLASE; BACTERIAL ENZYME; THERMOLYSIN; TRIFLUOROETHANOL; WATER;

ARTICLE; BACILLUS AMYLOLIQUEFACIENS; BACILLUS LICHENIFORMIS; CIRCULAR DICHROISM; COMPARATIVE STUDY; CONCENTRATION RESPONSE; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME REACTIVATION; ENZYME STRUCTURE; FLUORESCENCE; PROTEIN AGGREGATION; PROTEIN BINDING; PROTEIN DEGRADATION; PROTEIN FOLDING; STATISTICAL SIGNIFICANCE; STRUCTURE ANALYSIS; THERMOSTABILITY;

BACILLUS AMYLOLIQUEFACIENS; BACILLUS LICHENIFORMIS; BACTERIA (MICROORGANISMS);

EID: 3042653305     PISSN: 01418130     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ijbiomac.2004.03.006     Document Type: Article

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