The reactivity and thermostability of a novel mycelium-bound carboxylesterase from lyophilized cells of Aspergillus oryzae are explored in organic solvent. Ethanol acetylation was selected as reference esterification reaction. High carboxylesterase activity cells were used as biocatalyst in batch esterification tests at 12.5 < So < 125 mmol L-1, 5.0 < Xo < 30 g L-1, 0.49 < log P < 4.5 and 30 < T < 80°C, as well as in residual activity tests after incubation at 40 < T < 90°C. The starting rates of product formation were used to estimate with the Arrhenius model the apparent activation enthalpies of the enzymatic reaction (29-33 kJ mol-1), the reversible unfolding (56-63 kJ mol-1), and the irreversible denaturation (22 kJ mol-1) of the biocatalyst.

Reactivity and stability of mycelium-bound carboxylesterase from Aspergillus oryzae / A. Converti, A. del Borghi, R. Gandolfi, F.E. Molinari, E. Palazzi, P. Perego, M. Zilli. - In: BIOTECHNOLOGY AND BIOENGINEERING. - ISSN 0006-3592. - 77:2(2002), pp. 232-237.

Reactivity and stability of mycelium-bound carboxylesterase from Aspergillus oryzae

R. Gandolfi;F.E. Molinari;
2002

Abstract

The reactivity and thermostability of a novel mycelium-bound carboxylesterase from lyophilized cells of Aspergillus oryzae are explored in organic solvent. Ethanol acetylation was selected as reference esterification reaction. High carboxylesterase activity cells were used as biocatalyst in batch esterification tests at 12.5 < So < 125 mmol L-1, 5.0 < Xo < 30 g L-1, 0.49 < log P < 4.5 and 30 < T < 80°C, as well as in residual activity tests after incubation at 40 < T < 90°C. The starting rates of product formation were used to estimate with the Arrhenius model the apparent activation enthalpies of the enzymatic reaction (29-33 kJ mol-1), the reversible unfolding (56-63 kJ mol-1), and the irreversible denaturation (22 kJ mol-1) of the biocatalyst.
Settore CHIM/11 - Chimica e Biotecnologia delle Fermentazioni
2002
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2434/168155
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