Fusion to a pull-down domain: A novel approach of producing Trigonopsis variabilis D-amino acid oxidase as insoluble enzyme aggregates

Biotechnology and Bioengineering

Volumn 97, Issue 3, 2007, Pages 454-461

  Nahalka, Jozef ^a,b   Nidetzky, Bernd ^a  

^a GRAZ UNIVERSITY OF TECHNOLOGY   (Austria)

^b INSTITUTE OF CHEMISTRY   (Slovakia)

Author keywords

Active enzyme particles; Cellulose binding domain; D amino acid oxidase; Operational stabilization; Physiological aggregation

Indexed keywords

BINDING ENERGY; CROSSLINKING; ENZYME ACTIVITY; PRECIPITATION (CHEMICAL); SINGLE CRYSTALS;

ACTIVE ENZYME PARTICLES; CELLULOSE BINDING DOMAIN; D-AMINO ACID OXIDASE; OPERATIONAL STABILIZATION; PHYSIOLOGICAL AGGREGATION;

BIOCATALYSTS;

CELLULOSE; DEXTRO AMINO ACID OXIDASE;

AMINO TERMINAL SEQUENCE; ARTICLE; BIOCATALYST; CARBOXY TERMINAL SEQUENCE; CHIMERA; CLOSTRIDIUM CELLULOVORANS; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME BINDING; ENZYME ISOLATION; ENZYME STABILITY; ESCHERICHIA COLI; NONHUMAN; PROTEIN AGGREGATION; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN IMMOBILIZATION; TRIGONOPSIS VARIABILIS; YEAST;

ASCOMYCOTA; BINDING SITES; BIOTECHNOLOGY; CELLULOSE; D-AMINO-ACID OXIDASE; PARTICLE SIZE; SOLUBILITY;

CLOSTRIDIUM CELLULOVORANS; ESCHERICHIA COLI; TRIGONOPSIS VARIABILIS;

EID: 34249827218     PISSN: 00063592     EISSN: 10970290     Source Type: Journal    
DOI: 10.1002/bit.21244     Document Type: Article

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