thermal stability of a castor bean seed acid phosphatase

The effect of temperature on the activity and structural stability of an acid phosphatase (EC 3.1.3.2.) purified from castor bean (Ricinus communis L.) seeds have been examined. The enzyme showed high activity at 45 degrees C using p-nitrophenylphosphate (p-NPP) as substrate. The activation energy f...

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Veröffentlicht in:	Molecular and cellular biochemistry 2004-11, Vol.266 (1-2), p.11-15
Hauptverfasser:	Granjeiro, P.A, Cavagis, A.D.M, Leite, L. de C, Ferreira, C.V, Granjeiro, J.M, Aoyama, H
Format:	Artikel
Sprache:	eng
Schlagworte:	acid phosphatase Acid Phosphatase - chemistry castor beans Enzymatic activity enzyme activity Enzyme Stability Enzymes heat inactivation heat stability Hot Temperature Inactivation Nitrophenols - chemistry Organophosphorus Compounds - chemistry Phosphates - chemistry Plant Proteins - chemistry protein conformation Protein Denaturation Ricinus communis Ricinus communis - enzymology Seeds - enzymology Thermodynamics transition temperature Transition temperatures
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