Abstract
Background: Proteins tend to form inactive aggregates under harsh conditions used in industrial processes. Lipases are enzymes that hydrolyse triglycerides to glycerol and free fatty acids, but are able to catalyse various other transformations in the presence of organic solvents.
Objectives: The main objective of this study was to investigate lipases behavior at high temperature and in presence of organic solvents.
Methods: Heat-induced aggregation of porcine pancreatic lipase (PPL) was followed by UV-visible spectroscopy at 400 nm wavelength for 600 seconds, at the isoelectric point (pH 5, phosphate solution) and 50°C, and in presence or absence of various percentages of dimethyl sulfoxide (DMSO), propanol, isopropanol, acetone and trifluoroethanol (TFE). Possible positioning of each organic solvent molecule relative to PPL was investigated using docking method.
Results: Native enzyme aggregated under aforementioned conditions and amorphous aggregates formed which were visible to the naked eye. From the tested solvents, DMSO reduced protein aggregation in a concentration-dependent manner. On the other hand, protein aggregation intensified by adding any of propanol, isopropanol, acetone or TFE. This effect was more pronounced in TFE and propanol compared to isopropanol and acetone.
Conclusion: Solvents with lower polarity led to aggregation, while solvent with higher polarity inhibited PPL aggregation, and DMSO could be effectively used to counteract lipase aggregation.
Keywords: Porcine pancreatic lipase, thermal aggregation, organic solvent, docking, stability, DMSO.
Graphical Abstract
Protein & Peptide Letters
Title:Effect of Organic Solvents on Porcine Pancreatic Lipase Thermal Aggregation
Volume: 24 Issue: 10
Author(s): Mahsa Vaezzadeh, Marjan Sabbaghian*, Parichehreh Yaghmaei and Azadeh Ebrahim-Habibi *
Affiliation:
- Department of Andrology, Reproductive Biomedicine Research Center, Royan Institute for Reproductive Biomedicine, ACECR, Tehran,Iran
- Biosensor Research Center, Endocrinology and Metabolism Molecular-Cellular Sciences Institute, Tehran University of Medical Sciences, Tehran,Iran
Keywords: Porcine pancreatic lipase, thermal aggregation, organic solvent, docking, stability, DMSO.
Abstract: Background: Proteins tend to form inactive aggregates under harsh conditions used in industrial processes. Lipases are enzymes that hydrolyse triglycerides to glycerol and free fatty acids, but are able to catalyse various other transformations in the presence of organic solvents.
Objectives: The main objective of this study was to investigate lipases behavior at high temperature and in presence of organic solvents.
Methods: Heat-induced aggregation of porcine pancreatic lipase (PPL) was followed by UV-visible spectroscopy at 400 nm wavelength for 600 seconds, at the isoelectric point (pH 5, phosphate solution) and 50°C, and in presence or absence of various percentages of dimethyl sulfoxide (DMSO), propanol, isopropanol, acetone and trifluoroethanol (TFE). Possible positioning of each organic solvent molecule relative to PPL was investigated using docking method.
Results: Native enzyme aggregated under aforementioned conditions and amorphous aggregates formed which were visible to the naked eye. From the tested solvents, DMSO reduced protein aggregation in a concentration-dependent manner. On the other hand, protein aggregation intensified by adding any of propanol, isopropanol, acetone or TFE. This effect was more pronounced in TFE and propanol compared to isopropanol and acetone.
Conclusion: Solvents with lower polarity led to aggregation, while solvent with higher polarity inhibited PPL aggregation, and DMSO could be effectively used to counteract lipase aggregation.
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Cite this article as:
Vaezzadeh Mahsa, Sabbaghian Marjan*, Yaghmaei Parichehreh and Ebrahim-Habibi Azadeh *, Effect of Organic Solvents on Porcine Pancreatic Lipase Thermal Aggregation, Protein & Peptide Letters 2017; 24 (10) . https://dx.doi.org/10.2174/0929866524666170724114947
DOI https://dx.doi.org/10.2174/0929866524666170724114947 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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