Immobilization of a thermostable α-amylase by covalent binding to an alginate matrix increases high temperature usability

Biotechnology Progress

Volumn 25, Issue 2, 2009, Pages 436-445

  Tee, Boon L ^a,b   Kaletunç, Gönül ^a  

^a OHIO STATE UNIVERSITY   (United States)

^b ButylFuel LLC   (United States)

Author keywords

amylase; Alginate; Covalent binding; EDAC; EDTA; Immobilization; Liquefaction; Starch; Sulfo NHS

Indexed keywords

COVALENT BINDING; EDAC; EDTA; IMMOBILIZATION; SULFO-NHS;

ALGINATE; AMINES; BATCH REACTORS; CALCIUM; CALCIUM ALLOYS; CALCIUM CHLORIDE; CARBOXYLATION; ENZYME ACTIVITY; ENZYMES; HYDROLYSIS; LIQUEFACTION; METAL ANALYSIS; REACTION RATES; REUSABILITY;

STARCH;

1 ETHYL 3 (3 DIMETHYLAMINOETHYL)CARBODIIMIDE; 1-ETHYL-3-(3-DIMETHYLAMINOETHYL)CARBODIIMIDE; ALGINIC ACID; AMYLASE; CROSS LINKING REAGENT; CYANAMIDE; EDETIC ACID; GLUCURONIC ACID; HEXURONIC ACID; IMMOBILIZED ENZYME;

ARTICLE; CHEMISTRY; ENZYME STABILITY; EVALUATION; HEAT; KINETICS; METHODOLOGY; PROTEIN BINDING;

ALGINATES; ALPHA-AMYLASES; CARBODIIMIDES; CHEMISTRY; CROSS-LINKING REAGENTS; EDETIC ACID; ENZYME STABILITY; ENZYMES, IMMOBILIZED; GLUCURONIC ACID; HEXURONIC ACIDS; HOT TEMPERATURE; KINETICS; PROTEIN BINDING;

EID: 66149187121     PISSN: 87567938     EISSN: None     Source Type: Journal    
DOI: 10.1002/btpr.117     Document Type: Article

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