Reactivity and stability of mycelium-bound carboxylesterase from Aspergillus oryzae
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 es...
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Published in | Biotechnology and bioengineering Vol. 77; no. 2; pp. 232 - 237 |
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Main Authors | , , , , , |
Format | Journal Article |
Language | English |
Published |
New York
John Wiley & Sons, Inc
20.01.2002
Wiley |
Subjects | |
Online Access | Get full text |
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Summary: | 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. © 2002 John Wiley & Sons, Inc. Biotechnol Bioeng 77: 232–237, 2002. |
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Bibliography: | Italian National Council of Research (CNR), Biotechnology Project - No. 97.01019,PF115.086011 ark:/67375/WNG-DS8J35W3-6 istex:CC24533D33B6CCE3091220E865999ED02E66C817 ArticleID:BIT10124 ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 ObjectType-Article-1 ObjectType-Feature-2 |
ISSN: | 0006-3592 1097-0290 |
DOI: | 10.1002/bit.10124 |