Extracellular α-amylase from Thermus filiformis Ork A2: Purification and biochemical characterization

Extremophiles

Volumn 2, Issue 1, 1998, Pages 23-32

  Egas, Maria C V ^a,b   Da Costa, Milton S ^a   Cowan, Don A ^c   Pires, Euclides M V ^a,b  

^a UNIVERSITY OF COIMBRA   (Portugal)

^b UNIVERSITY OF COIMBRA   (Portugal)

^c UNIVERSITY COLLEGE LONDON   (United Kingdom)

Author keywords

Amylase; Extracellular; Properties; Purification; Thermostability; Thermus filiformis

Indexed keywords

4 CHLOROMERCURIBENZOIC ACID; AMINO ACID SEQUENCE; AMYLASE; AMYLOPECTIN; AMYLOSE; DITHIOTHREITOL; EDETIC ACID; ENZYME ACTIVITY; ENZYME PURIFICATION; GLYCOGEN; HYDROLYSIS; ION EXCHANGE CHROMATOGRAPHY; PH; SDS POLYACRYLAMIDE GEL ELECTROPHORESIS; STARCH; TEMPERATURE; THERMOSTABILITY;

ALPHA-AMYLASE; AMINO ACID SEQUENCE; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ISOELECTRIC FOCUSING; KINETICS; MOLECULAR WEIGHT; PEPTIDE FRAGMENTS; SUBSTRATE SPECIFICITY; THERMODYNAMICS; THERMUS;

BACTERIA (MICROORGANISMS); FELIS CATUS; THERMUS; THERMUS FILIFORMIS;

EID: 0031683564     PISSN: 14310651     EISSN: None     Source Type: Journal    
DOI: 10.1007/s007920050039     Document Type: Article

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