Characterization of a neutral and thermostable glucoamylase from the thermophilic mold thermomucor indicae-seudaticae: Activity, stability, and structural correlation

Applied Biochemistry and Biotechnology

Volumn 160, Issue 3, 2010, Pages 879-890

  Kumar, Pardeep ^a   Islam, Asimul ^b   Ahmad, Faizan ^b   Satyanarayana, T ^a  

^a UNIVERSITY OF DELHI   (India)

^b JAMIA MILLIA ISLAMIA CENTRAL UNIVERSITY   (India)

Author keywords

Circular dichroism; Glucoamylase; Heat denaturation; Thermomucor indicae seudaticae; Transglycosylation

Indexed keywords

ANION EXCHANGE; AROMATIC AMINO ACID; CATALYTIC DOMAINS; CD SPECTRA; CHROMATOGRAPHIC SYSTEMS; CHROMATOGRAPHIC TECHNIQUES; CIRCULAR DICHROISM; GEL FILTRATION; GLUCOAMYLASE; HEAT DENATURATION; HELIX CONTENT; OBSERVATION POINT; PH VALUE; SECONDARY STRUCTURES; STRUCTURAL CORRELATION; TEMPERATURE RANGE; TERTIARY STRUCTURES; THERMAL DENATURATIONS; THERMAL STABILITY; THERMOPHILIC MOLD; TRANS GLYCOSYLATION ACTIVITY; TRANSGLYCOSYLATION; TRANSITION CURVES;

AMINO ACIDS; DENATURATION; DICHROISM; GLUCOSE; LIQUID CHROMATOGRAPHY; MOLDS; ORGANIC ACIDS; PROTEINS; PYROLYSIS; SACCHARIFICATION; STARCH; SYSTEM STABILITY; THERMODYNAMIC STABILITY; THERMOGRAVIMETRIC ANALYSIS;

FILTRATION;

GLUCAN 1,4 ALPHA GLUCOSIDASE; GLUCOSE; STARCH; TRYPTOPHAN; TYROSINE;

ALPHA HELIX; ANION EXCHANGE; ARTICLE; CATALYSIS; CIRCULAR DICHROISM; CONTROLLED STUDY; DENATURATION; ENZYME ACTIVE SITE; ENZYME ANALYSIS; ENZYME STABILITY; ENZYME STRUCTURE; GEL FILTRATION; GLYCOSYLATION; NONHUMAN; PH; PROTEIN DOMAIN; PROTEIN PURIFICATION; PROTEIN SECONDARY STRUCTURE; SACCHARIFICATION; THERMOPHILIC BACTERIUM; THERMOSTABILITY; ULTRAVIOLET RADIATION;

AMINO ACID SEQUENCE; BIOCATALYSIS; CIRCULAR DICHROISM; ENZYME STABILITY; GLUCAN 1,4-ALPHA-GLUCOSIDASE; GLYCOSYLATION; MUCORALES; PROTEIN DENATURATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SEQUENCE ANALYSIS, DNA; TEMPERATURE;

THERMOMUCOR INDICAE-SEUDATICAE;

EID: 77949278164     PISSN: 02732289     EISSN: None     Source Type: Journal    
DOI: 10.1007/s12010-009-8666-0     Document Type: Article

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