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Title: A chemically modified alpha-amylase with a molten-globule state has entropically driven enhanced thermal stability
Authors: Siddiqui, KS
Poljak, A
Francisci, D
Guerriero, G
Pilak, O
Burg, D
Raftery, MJ
Parkin, DM
Trewhella, J
Cavicchioli, R
Keywords: Calorimetry
Protein structure
Issue Date: 1-Oct-2010
Publisher: Oxford University Press
Citation: Siddiqui, K. S., Poljak, A., De Francisci, D., Guerriero. G., Pilak, O., Burg, D., Rafterfy, M. J., Parkin, D. M., Trewhella, J., & Cavicchioli, R. (2010). A chemically modified α-amylase with a molten-globule state has entropically driven enhanced thermal stability. Protein Engineering, Design and Selection 23(10): 769-780. doi:10.1093/protein/gzq051
Abstract: The thermostability properties of TAA were investigated by chemically modifying carboxyl groups on the surface of the enzyme with AMEs. The TAA(MOD) exhibited a 200% improvement in starch-hydrolyzing productivity at 60 degrees C. By studying the kinetic, thermodynamic and biophysical properties, we found that TAAMOD had formed a thermostable, MG state, in which the unfolding of the tertiary structure preceded that of the secondary structure by at least 20 degrees C. The X-ray crystal structure of TAAMOD revealed no new permanent interactions (electrostatic or other) resulting from the modification. By deriving thermodynamic activation parameters of TAAMOD, we rationalised that thermostabilisation have been caused by a decrease in the entropy of the transition state, rather than being enthalpically driven. Far-UV CD shows that the origin of decreased entropy may have arisen from a higher helical content of TAAMOD. This study provides new insight into the intriguing properties of an MG state resulting from the chemical modification of TAA.© 2010, Oxford University Press (OUP)
Gov't Doc #: 3775
ISSN: 1741-0126
Appears in Collections:Journal Articles

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