Ionization basis for activation of enzymes soluble in ionic liquids

Guangnan Ou, Biyan He, Peter Halling

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

BACKGROUND: The complex interactions between electrolytes and proteins have been studied for more than a century. However, understanding is not yet complete and does not provide a basis for predicting the activity of enzymes in ionic media. The use of ionic liquids (ILs) as reaction medium has opened up new opportunities for better understanding of the mechanism of enzymatic catalysis. Although a number of properties of ILs have been correlated with enzyme function, these relationships are not completely understood at a molecular level. METHODS: We propose that ILs must be able to promote ionization of protein ionizable groups in order to dissolve active enzymes. The biocompatible IL need to possess a functional group with large donor number and acceptor number in both cationic and anionic units, each of which is based on a high dielectric constant lead structure. We designed and synthesized two series of ILs and determined their ionizing-dissociating abilities and activities of lipases soluble in these new ILs. RESULTS: The results showed that the ionizing-dissociating abilities of ILs paralleled the catalytic activity trend of lipases dissolved in the ILs. The activities of lipases soluble in the newly designed ILs were comparable to those in water. CONCLUSIONS: We can conclude that ionizing-dissociating abilities of an IL can be used as a basis for predicting the activity of enzymes soluble in the IL. GENERAL SIGNIFICANCE: Ionization basis for activation of enzymes gives a deeper understanding of the behavior of enzymes in non-aqueous media at a molecular level.
LanguageEnglish
Pages1404-1408
Number of pages5
JournalBiochimica et Biophysica Acta - General Subjects
Volume1860
Issue number7
Early online date7 Apr 2016
DOIs
Publication statusPublished - 1 Jul 2016

Fingerprint

Ionic Liquids
Enzyme Activation
Ionization
Chemical activation
Enzymes
Lipase
Catalysis
Functional groups
Electrolytes
Catalyst activity
Proteins
Permittivity

Keywords

  • ionization
  • activation
  • enzyme
  • ionic liquid

Cite this

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title = "Ionization basis for activation of enzymes soluble in ionic liquids",
abstract = "BACKGROUND: The complex interactions between electrolytes and proteins have been studied for more than a century. However, understanding is not yet complete and does not provide a basis for predicting the activity of enzymes in ionic media. The use of ionic liquids (ILs) as reaction medium has opened up new opportunities for better understanding of the mechanism of enzymatic catalysis. Although a number of properties of ILs have been correlated with enzyme function, these relationships are not completely understood at a molecular level. METHODS: We propose that ILs must be able to promote ionization of protein ionizable groups in order to dissolve active enzymes. The biocompatible IL need to possess a functional group with large donor number and acceptor number in both cationic and anionic units, each of which is based on a high dielectric constant lead structure. We designed and synthesized two series of ILs and determined their ionizing-dissociating abilities and activities of lipases soluble in these new ILs. RESULTS: The results showed that the ionizing-dissociating abilities of ILs paralleled the catalytic activity trend of lipases dissolved in the ILs. The activities of lipases soluble in the newly designed ILs were comparable to those in water. CONCLUSIONS: We can conclude that ionizing-dissociating abilities of an IL can be used as a basis for predicting the activity of enzymes soluble in the IL. GENERAL SIGNIFICANCE: Ionization basis for activation of enzymes gives a deeper understanding of the behavior of enzymes in non-aqueous media at a molecular level.",
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Ionization basis for activation of enzymes soluble in ionic liquids. / Ou, Guangnan; He, Biyan; Halling, Peter.

In: Biochimica et Biophysica Acta - General Subjects, Vol. 1860, No. 7, 01.07.2016, p. 1404-1408.

Research output: Contribution to journalArticle

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AU - Ou, Guangnan

AU - He, Biyan

AU - Halling, Peter

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N2 - BACKGROUND: The complex interactions between electrolytes and proteins have been studied for more than a century. However, understanding is not yet complete and does not provide a basis for predicting the activity of enzymes in ionic media. The use of ionic liquids (ILs) as reaction medium has opened up new opportunities for better understanding of the mechanism of enzymatic catalysis. Although a number of properties of ILs have been correlated with enzyme function, these relationships are not completely understood at a molecular level. METHODS: We propose that ILs must be able to promote ionization of protein ionizable groups in order to dissolve active enzymes. The biocompatible IL need to possess a functional group with large donor number and acceptor number in both cationic and anionic units, each of which is based on a high dielectric constant lead structure. We designed and synthesized two series of ILs and determined their ionizing-dissociating abilities and activities of lipases soluble in these new ILs. RESULTS: The results showed that the ionizing-dissociating abilities of ILs paralleled the catalytic activity trend of lipases dissolved in the ILs. The activities of lipases soluble in the newly designed ILs were comparable to those in water. CONCLUSIONS: We can conclude that ionizing-dissociating abilities of an IL can be used as a basis for predicting the activity of enzymes soluble in the IL. GENERAL SIGNIFICANCE: Ionization basis for activation of enzymes gives a deeper understanding of the behavior of enzymes in non-aqueous media at a molecular level.

AB - BACKGROUND: The complex interactions between electrolytes and proteins have been studied for more than a century. However, understanding is not yet complete and does not provide a basis for predicting the activity of enzymes in ionic media. The use of ionic liquids (ILs) as reaction medium has opened up new opportunities for better understanding of the mechanism of enzymatic catalysis. Although a number of properties of ILs have been correlated with enzyme function, these relationships are not completely understood at a molecular level. METHODS: We propose that ILs must be able to promote ionization of protein ionizable groups in order to dissolve active enzymes. The biocompatible IL need to possess a functional group with large donor number and acceptor number in both cationic and anionic units, each of which is based on a high dielectric constant lead structure. We designed and synthesized two series of ILs and determined their ionizing-dissociating abilities and activities of lipases soluble in these new ILs. RESULTS: The results showed that the ionizing-dissociating abilities of ILs paralleled the catalytic activity trend of lipases dissolved in the ILs. The activities of lipases soluble in the newly designed ILs were comparable to those in water. CONCLUSIONS: We can conclude that ionizing-dissociating abilities of an IL can be used as a basis for predicting the activity of enzymes soluble in the IL. GENERAL SIGNIFICANCE: Ionization basis for activation of enzymes gives a deeper understanding of the behavior of enzymes in non-aqueous media at a molecular level.

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