Chemical modification of bacterial α-amylases: Changes in tertiary structures and the effect of additional calcium

Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology

Volumn 1548, Issue 2, 2001, Pages 229-237

  Khajeh, Khosro ^a   Ranjbar, Bijan ^b   Naderi Manesh, Hossein ^b   Ebrahim Habibi, Azadeh ^a   Nemat Gorgani, Mohsen ^a  

^a UNIVERSITY OF TEHRAN   (Iran)

^b TARBIAT MODARES UNIVERSITY   (Iran)

Author keywords

Chemical modification; Domain domain interaction; Mesophilic thermophilic amylase; Stabilization; Thermal denaturation

Indexed keywords

AMYLASE; BACTERIAL ENZYME; CALCIUM; SORBITOL;

ARTICLE; BACILLUS AMYLOLIQUEFACIENS; BACILLUS LICHENIFORMIS; CATALYSIS; CHEMICAL MODIFICATION; CIRCULAR DICHROISM; COMPARATIVE STUDY; ENZYME ANALYSIS; ENZYME CONFORMATION; ENZYME INACTIVATION; PRIORITY JOURNAL; PROTEIN STABILITY;

ALPHA-AMYLASE; BACILLUS; BACTERIAL PROTEINS; CALCIUM; CIRCULAR DICHROISM; ENZYME STABILITY; PROTEIN DENATURATION; PROTEIN STRUCTURE, TERTIARY; TEMPERATURE;

BACTERIA (MICROORGANISMS);

EID: 0035855207     PISSN: 01674838     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4838(01)00236-9     Document Type: Article

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