Co-conjugation vis-à-vis individual conjugation of α-amylase and glucoamylase for hydrolysis of starch

Carbohydrate Polymers

Volumn 98, Issue 1, 2013, Pages 1191-1197

  Jadhav, Swati B ^a   Singhal, Rekha S ^a  

^a INSTITUTE OF CHEMICAL TECHNOLOGY   (India)

Author keywords

Activation energy; Co conjugate; Inactivation rate constant; Stability; Starch hydrolysis

Indexed keywords

ACTIVATION ENERGY; CHEMICAL ACTIVATION; CONVERGENCE OF NUMERICAL METHODS; ELECTROPHORESIS; ENZYMES; HYDROLYSIS; PH EFFECTS; RATE CONSTANTS; STARCH;

ALPHA AMYLASE; CONJUGATED ENZYMES; COVALENT BINDING; ENZYME SYSTEMS; GLUCOAMYLASE; PH STABILITY; SDS-POLYACRYLAMIDE GEL ELECTROPHORESIS; STARCH HYDROLYSIS;

AMYLASES;

AMYLASE; GLUCAN 1,4 ALPHA GLUCOSIDASE; GLUCOSE; PECTIN; STARCH;

ACTIVATION ENERGY; ARTICLE; ASPERGILLUS NIGER; BACILLUS; CHEMISTRY; CO-CONJUGATE; ENZYME ACTIVATION; ENZYME STABILITY; ENZYMOLOGY; HYDROLYSIS; INACTIVATION RATE CONSTANT; KINETICS; METABOLISM; PH; STABILITY; STARCH HYDROLYSIS; TEMPERATURE;

ACTIVATION ENERGY; CO-CONJUGATE; INACTIVATION RATE CONSTANT; STABILITY; STARCH HYDROLYSIS;

ALPHA-AMYLASES; ASPERGILLUS NIGER; BACILLUS; ENZYME ACTIVATION; ENZYME STABILITY; GLUCAN 1,4-ALPHA-GLUCOSIDASE; GLUCOSE; HYDROGEN-ION CONCENTRATION; HYDROLYSIS; KINETICS; PECTINS; STARCH; TEMPERATURE;

EID: 84880966671     PISSN: 01448617     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.carbpol.2013.07.032     Document Type: Article

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