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| Format: | Artículo científico |
| Language: | en |
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Academia Brasileira de Ciências
2004
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| Online Access: | https://www.redalyc.org/articulo.oa?id=32776406 |
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Table of Contents:
- Inactivation of yeast inorganic pyrophosphatase by organic solvents Rodrigo Garrido Grazinoli Mauro Sola-Penna Multidisciplinaria (Ciencias Naturales y Exactas) enzyme alcohol organic solvents yeast inorganic pyrophosphatase A number of application for enzymes in organic solvents have been developed in chemical processing, foodrelated conversions and analyses. The only unsolved problem related to nonaqueous enzymology is thenotion that enzymes in organic solvent are mostly far less active than in water. Therefore, studies concerningthe mechanisms by which enzymes are inactivated by organic solvents would reveal a clear understandingof the structure-function relationship of this phenomenon. Here we analyzed the effects of a series ofalcohols (methanol, ethanol, 1-propanol and 2-propanol) and acetone on the activity of yeast inorganicpyrophosphatase. We observed that solvents inactivated the enzyme in a dose-dependent manner. Thisinactivation is also dependent on the hydrophobicity of the solvent, where the most hydrophobic solvent isalso the most effective one. The I50 for inactivation by n-alcohols are 5.9±0.4, 2.7±0.1 and 2.5±0.1Mformethanol, ethanol and 1-propanol, respectively. Inactivation was less effective at 37◦C than at 5◦C, when theI50 for inactivation by methanol, ethanol and 1-propanol are 4.5±0.2, 2.1±0.2 and 1.7±0.1M, respectively.Our proposal is that solvent binds to the enzyme structure promoting the inactivation by stabilizing an unfoldedstructure, and that this binding is through the hydrophobic regions of either the protein or the solvent. 2004 artículo científico 0001-3765 https://www.redalyc.org/articulo.oa?id=32776406 en http://www.redalyc.org/revista.oa?id=327 Anais da Academia Brasileira de Ciências application/pdf Academia Brasileira de Ciências Anais da Academia Brasileira de Ciências (Brasil) Num.4 Vol.76