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Modulation and Determination of Lipases Activity
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Modulation and Determination of Lipases Activity

A special issue of Molecules (ISSN 1420-3049). This special issue belongs to the section "Chemical Biology".

Deadline for manuscript submissions: closed (30 April 2024) | Viewed by 8702

Special Issue Editor

Dr. Silvana Casati

E-Mail Website
Guest Editor
Dipartimento di Scienze Biomediche e Cliniche L. Sacco, Università degli Studi di Milano, 20157 Milano, Italy
Interests: study of the activity of enzymes in water and organic solvents; use of enzymes in organic synthesis; synthesis and characterization of organic molecules with potential pharmacological activity; synthesis of inhibitors of endocannabinoid system; synthesis of modified nucleosides as potential antitumoral drugs

Special Issue Information

Dear Colleagues,

Lipases are ubiquitous enzymes in nature. Besides their relevant role in physiological processes, lipases have important applications in organic synthesis and are widely used in the chemical, pharmaceutical, food and detergent industries. Altering lipase activity can either lead to therapeutic benefits or cause disease and can also improve the applicability of these enzymes as biocatalysts. Modulators of lipases include activators and inhibitors, either obtained from natural sources or synthesized. Several drugs are currently approved for treatment of various pathologies, such as obesity, pain, inflammation, anxiety, and cardiovascular disease; other compounds are under study for further therapeutic exploitation, and there is still much to discover. Since the mechanisms of action of lipases have not been fully understood or clarified, research on their modulatary activities remains exploratory. Methods to modify enzymes in order to enhance their catalytic activity are in constant evolution. Lipase properties can be improved by using different tools in order to solve specific problems, such as stability in organic medium or solubility. Immobilization, for example, can enhance lipase activities, improving their resistance to high temperature, pH, reusability and storage capacity. However, these methods require increasingly sensitive methods for determining lipase activity. For this reason, the development of analytical methods for the detection and assay of lipases is an important target.

Dr. Silvana Casati
Guest Editor

Manuscript Submission Information

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Keywords

  • lipases
  • lipases inhibitors
  • lipases activity
  • immobilization
  • biocatalysis
  • enzyme assay
  • high-throughput screening

Published Papers (4 papers)

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Research

10 pages, 2004 KiB  
Article
2-Arachidonoylglycerol Synthesis: Facile and Handy Enzymatic Method That Allows to Avoid Isomerization
by Roberta Ottria, Silvana Casati, Paola Rota and Pierangela Ciuffreda
Molecules 2022, 27(16), 5190; https://doi.org/10.3390/molecules27165190 - 15 Aug 2022
Cited by 1 | Viewed by 1252
Abstract
A simple and practical synthesis of 2-arachidonoyl glycerol (2-AG), an endogenous agonist for cannabinoid receptors, based on a two-step enzymatic process and a chemical coupling, was achieved with a good yield and negligible amount of the isomerization product 1-AG. Commercial preparation of immobilized [...] Read more.
A simple and practical synthesis of 2-arachidonoyl glycerol (2-AG), an endogenous agonist for cannabinoid receptors, based on a two-step enzymatic process and a chemical coupling, was achieved with a good yield and negligible amount of the isomerization product 1-AG. Commercial preparation of immobilized lipase from Mucor miehei (MML) was selected as the most suitable enzyme to catalyze the efficient protection of glycerol using vinyl benzoate as an acyl transfer reagent in tetrahydrofuran. The same enzyme was used to remove the protective groups in positions 1 and 3. Owing to the mild neutral conditions and easy suitability of the method, 2-AG was obtained without any isomerization to the more stable 1-AG and air oxidation of acid chain. The synthetic method proposed here allows us to easily obtain 2-AG from the protected precursor in a one-step reaction without purification requirement. Full article
(This article belongs to the Special Issue Modulation and Determination of Lipases Activity)
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9 pages, 1494 KiB  
Article
ThermoSlope: A Software for Determining Thermodynamic Parameters from Single Steady-State Experiments
by Bjarte Aarmo Lund and Bjørn Olav Brandsdal
Molecules 2021, 26(23), 7155; https://doi.org/10.3390/molecules26237155 - 26 Nov 2021
Cited by 2 | Viewed by 1840
Abstract
The determination of the temperature dependence of enzyme catalysis has traditionally been a labourious undertaking. We have developed a new approach to the classical Arrhenius parameter estimation by fitting the change in velocity under a gradual change in temperature. The evaluation with a [...] Read more.
The determination of the temperature dependence of enzyme catalysis has traditionally been a labourious undertaking. We have developed a new approach to the classical Arrhenius parameter estimation by fitting the change in velocity under a gradual change in temperature. The evaluation with a simulated dataset shows that the approach is valid. The approach is demonstrated as a useful tool by characterizing the Bacillus pumilus LipA enzyme. Our results for the lipase show that the enzyme is psychrotolerant, with an activation energy of 15.3 kcal/mol for the chromogenic substrate para-nitrophenyl butyrate. Our results demonstrate that this can produce equivalent curves to the traditional approach while requiring significantly less sample, labour and time. Our method is further validated by characterizing three α-amylases from different species and habitats. The experiments with the α-amylases show that the approach works over a wide range of temperatures and clearly differentiates between psychrophilic, mesophilic and thermophilic enzymes. The methodology is released as an open-source implementation in Python, available online or used locally. This method of determining the activation parameters can make studies of the temperature dependence of enzyme catalysis more widely adapted to understand how enzymes have evolved to function in extreme environments. Moreover, the thermodynamic parameters that are estimated serve as functional validations of the empirical valence bond calculations of enzyme catalysis. Full article
(This article belongs to the Special Issue Modulation and Determination of Lipases Activity)
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19 pages, 3226 KiB  
Article
The Role of Surface Exposed Lysine in Conformational Stability and Functional Properties of Lipase from Staphylococcus Family
by Nurul Nadirah Ahmad, Nor Hafizah Ahmad Kamarudin, Adam Thean Chor Leow and Raja Noor Zaliha Raja Abd. Rahman
Molecules 2020, 25(17), 3858; https://doi.org/10.3390/molecules25173858 - 25 Aug 2020
Cited by 5 | Viewed by 2320
Abstract
Surface charge residues have been recognized as one of the stability determinants in protein. In this study, we sought to compare and analyse the stability and conformational dynamics of staphylococcal lipase mutants with surface lysine mutation using computational and experimental methods. Three highly [...] Read more.
Surface charge residues have been recognized as one of the stability determinants in protein. In this study, we sought to compare and analyse the stability and conformational dynamics of staphylococcal lipase mutants with surface lysine mutation using computational and experimental methods. Three highly mutable and exposed lysine residues (Lys91, Lys177, Lys325) were targeted to generate six mutant lipases in silico. The model structures were simulated in water environment at 25 °C. Our simulations showed that the stability was compromised when Lys177 was substituted while mutation at position 91 and 325 improved the stability. To illustrate the putative alterations of enzyme stability in the stabilising mutants, we characterized single mutant K325G and double mutant K91A/K325G. Both mutants showed a 5 °C change in optimal temperature compared to their wild type. Single mutant K325G rendered a longer half-life at 25 °C (T1/2 = 21 h) while double mutant K91A/K325G retained only 40% of relative activity after 12 h incubation. The optimal pH for mutant K325G was shifted from 8 to 9 and similar substrate preference was observed for the wild type and two mutants. Our findings indicate that surface lysine mutation alters the enzymatic behaviour and, thus, rationalizes the functional effects of surface exposed lysine in conformational stability and activity of this lipase. Full article
(This article belongs to the Special Issue Modulation and Determination of Lipases Activity)
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17 pages, 3082 KiB  
Article
Ion-Pair Interaction and Hydrogen Bonds as Main Features of Protein Thermostability in Mutated T1 Recombinant Lipase Originating from Geobacillus zalihae
by Siti Nor Hasmah Ishak, Nor Hafizah Ahmad Kamarudin, Mohd Shukuri Mohamad Ali, Adam Thean Chor Leow and Raja Noor Zaliha Raja Abd. Rahman
Molecules 2020, 25(15), 3430; https://doi.org/10.3390/molecules25153430 - 28 Jul 2020
Cited by 8 | Viewed by 2199
Abstract
A comparative structure analysis between space- and an Earth-grown T1 recombinant lipase from Geobacillus zalihae had shown changes in the formation of hydrogen bonds and ion-pair interactions. Using the space-grown T1 lipase validated structure having incorporated said interactions, the recombinant T1 lipase was [...] Read more.
A comparative structure analysis between space- and an Earth-grown T1 recombinant lipase from Geobacillus zalihae had shown changes in the formation of hydrogen bonds and ion-pair interactions. Using the space-grown T1 lipase validated structure having incorporated said interactions, the recombinant T1 lipase was re-engineered to determine the changes brought by these interactions to the structure and stability of lipase. To understand the effects of mutation on T1 recombinant lipase, five mutants were developed from the structure of space-grown T1 lipase and biochemically characterized. The results demonstrate an increase in melting temperature up to 77.4 °C and 76.0 °C in E226D and D43E, respectively. Moreover, the mutated lipases D43E and E226D had additional hydrogen bonds and ion-pair interactions in their structures due to the improvement of stability, as observed in a longer half-life and an increased melting temperature. The biophysical study revealed differences in β-Sheet percentage between less stable (T118N) and other mutants. As a conclusion, the comparative analysis of the tertiary structure and specific residues associated with ion-pair interactions and hydrogen bonds could be significant in revealing the thermostability of an enzyme with industrial importance. Full article
(This article belongs to the Special Issue Modulation and Determination of Lipases Activity)
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