Artigo de periodico

Effects of cholinium‐based ionic liquids on <i>Aspergillus niger</i> lipase: Stabilizers or inhibitors (2019)

• Authors:
  • Nascimento, Paloma A. M.
  • Picheli, Flávio Pereira
  • Lopes, André Moreni
  • Pereira, Jorge Fernando Brandão
  • Ebinuma, Valéria de Carvalho Santos
• Autor USP: LOPES, ANDRÉ MORENI - EEL
• Unidade: EEL
• DOI: 10.1002/btpr.2838
• Subjects: ESTABILIDADE; INIBIÇÃO; LIPASE; LÍQUIDOS IÔNICOS
• Keywords: choline; enzymatic activity; inhibition; ionic liquid; lipase interaction; stability
• Agências de fomento:
  • Financiamento CAPES
  • Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
    Processo FAPESP: 2014/01580-3,2014/16424-7
  • Financiamento CNPq
• Language: Inglês
• Abstract: Lipases are well-known biocatalysts used in several industrial processes/applications.Thus, as with other enzymes, changes in their surrounding environment and/or theirthermodynamic parameters can induce structural changes that can increase, decrease,or even inhibit their catalytic activity. The use of ionic compounds as solvents or addi-tives is a common approach for adjusting reaction conditions and, consequently, forcontrolling the biocatalytic activity of enzymes. Herein, to elucidate the effects of ioniccompounds on the structure of lipase, the stability and enzymatic activity of lipase fromAspergillus nigerin aqueous solutions (at 0.05, 0.10, 0.50, and 1.00 M) of six cholinium-based ionic liquids (cholinium chloride [Ch]Cl; cholinium acetate ([Ch][Ac]); choliniumpropanoate ([Ch][Prop]); cholinium butanoate ([Ch][But]); cholinium pentanoate ([Ch][Pent]); and cholinium hexanoate ([Ch][Hex])) were evaluated over 24 hr. The enzy-matic activity of lipase was maintained or enhanced in the lower concentrations of allthe [Ch]+-ILs (below 0.1 M). [Ch][Ac] maintained the biocatalytic behavior of lipase,independent of the IL concentration and incubation time. However, above 0.1 M, [Ch][Pent] and [Ch][Hex] caused complete inhibition of the catalytic activity of the enzyme,demonstrating that the increase in the anionic alkyl chain length strongly affected theconformation of the lipase. The hydrophobicity and concentration of the [Ch]+-ILs playan important role in the enzyme activity, and these parameters can be controlled byadjusting the anionic alkyl chain length. The inhibitory effects of [Ch][Pent] and [Ch][Hex] may be of great interest to the pharmaceutical industry to induce pharmacologi-cal inhibition of gastric and pancreatic lipases.
• Imprenta:
  • Publisher: Aiche
  • Publisher place: Nova Iorque
  • Date published: 2019
• Source:
  • Título do periódico: Biotechnology Progress
  • ISSN: 8756-7938
  • Volume/Número/Paginação/Ano: v.35, n.5, art. e2838, pp.1-10, 2019

Informações sobre o DOI: 10.1002/btpr.2838 (Fonte: oaDOI API)
• Este periódico é de assinatura
• Este artigo NÃO é de acesso aberto
  
• Cor do Acesso Aberto: closed

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How to cite

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• ABNT

  NASCIMENTO, Paloma A. M. et al. Effects of cholinium‐based ionic liquids on <i>Aspergillus niger</i> lipase: Stabilizers or inhibitors. Biotechnology Progress, v. 35, n. 5, p. p1-10, 2019Tradução . . Disponível em: https://doi.org/10.1002/btpr.2838. Acesso em: 03 maio 2024.

• APA

  Nascimento, P. A. M., Picheli, F. P., Lopes, A. M., Pereira, J. F. B., & Ebinuma, V. de C. S. (2019). Effects of cholinium‐based ionic liquids on <i>Aspergillus niger</i> lipase: Stabilizers or inhibitors. Biotechnology Progress, 35( 5), p1-10. doi:10.1002/btpr.2838

• NLM

  Nascimento PAM, Picheli FP, Lopes AM, Pereira JFB, Ebinuma V de CS. Effects of cholinium‐based ionic liquids on <i>Aspergillus niger</i> lipase: Stabilizers or inhibitors [Internet]. Biotechnology Progress. 2019 ;35( 5): p1-10.[citado 2024 maio 03 ] Available from: https://doi.org/10.1002/btpr.2838

• Vancouver

  Nascimento PAM, Picheli FP, Lopes AM, Pereira JFB, Ebinuma V de CS. Effects of cholinium‐based ionic liquids on <i>Aspergillus niger</i> lipase: Stabilizers or inhibitors [Internet]. Biotechnology Progress. 2019 ;35( 5): p1-10.[citado 2024 maio 03 ] Available from: https://doi.org/10.1002/btpr.2838

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