pH-dependent aggregation of cutinase is efficiently suppressed by 1,8-ANS

Biopolymers

Volumn 83, Issue 6, 2006, Pages 619-629

  Pedersen, Shona ^a,b   Nesgaard, Lise ^a   Baptista, Ricardo P ^c   Melo, Eduardo P ^c,d   Kristensen, Søren R ^b   Otzen, Daniel E ^a  

^a AALBORG UNIVERSITY   (Denmark)

^b AALBORG UNIVERSITY HOSPITAL   (Denmark)

^c INSTITUTO SUPERIOR TÉCNICO   (Portugal)

^d UNIVERSITY OF ALGARVE   (Portugal)

Author keywords

Anionic detergents; ANS binding; Enzyme activity; Protein aggregation; Thermal stability; Urea

Indexed keywords

ADDITIVES; BINDING ENERGY; HYDROPHOBICITY; MELTING; STOICHIOMETRY; THERMODYNAMIC STABILITY;

ANIONIC DETERGENTS; ANS BINDING; ENZYME ACTIVITY; PROTEIN AGGREGATION;

ENZYMES;

AMYLASE; ARGININE; CUTINASE; DETERGENT; DYE; ENZYME INHIBITOR; LYSOZYME; TRIACYLGLYCEROL LIPASE; UREA;

ARTICLE; BINDING AFFINITY; COOLING; ENZYME ACTIVITY; ENZYME BINDING; FUSARIUM SOLANI; GENE MUTATION; HYDROPHOBICITY; INFRARED SPECTROSCOPY; MELTING POINT; NONHUMAN; OSMOLALITY; PH; TEMPERATURE SENSITIVITY; THERMOSTABILITY;

ANILINO NAPHTHALENESULFONATES; CARBOXYLIC ESTER HYDROLASES; HYDROGEN-ION CONCENTRATION; ISOELECTRIC POINT;

SUIDAE;

EID: 33845596138     PISSN: 00063525     EISSN: 10970282     Source Type: Journal    
DOI: 10.1002/bip.20598     Document Type: Article

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