Less explored plant lipases: Modeling and molecular dynamics simulations of plant lipases in different solvents and temperatures to understand structure-function relationship

Sankar, Sreejanani; Ponnuraj, Karthe

doi:10.1016/j.ijbiomac.2020.08.227

Cited by 21 publications

(9 citation statements)

References 56 publications

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“…Lipases are versatile enzymes, very important in the industry due to their use as a catalyst in the synthesis of several industrial processes, such as detergent supply, 1 depolymerization of polyesters and environmental remediation, 2–4 synthesis of aroma and biodiesel esters, 5,6 butters, and cosmetics production, 7 in addition to vitamin C synthesis 8 . This enzyme may be produced by microorganisms, animals, and plants 9–11 . Fungal lipases obtained have become a promising alternative in the production of these enzymes 12–14 .…”

Section: Introductionmentioning

confidence: 99%

Production of a fermented solid containing lipases from Penicillium roqueforti ATCC 10110 and its direct employment in organic medium in ethyl oleate synthesis

Soares¹,

Alnoch

Dias

et al. 2021

Biotech and App Biochem

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The production and direct employment in organic medium in the ethyl-oleate synthesis of a fermented solid (FS) containing lipases by Penicillium roqueforti ATCC 10110 (PR10110) was investigated. For the production of this FS, the solidstate fermentation of different agroindustrial waste was used, such as: cocoa shell, sugarcane bagasse, sugarcane bagasse with cocoa shell, and cocoa shell with soybean oil and nutrient solution. The response surface methodology was used to study the effect of independent variables of initial moisture content and inductor concentration, as carbon source and inducer on lipase production. The characterization of the fermented solid in organic medium was also carried out. The highest lipase activity (53 ± 5 U g −1 ) was 16% higher than that obtained with the nonoptimized conditions. The characterization studies observed high stability of the FS in organic solvents for 5 h at 30 • C, as well as at different temperatures, and the residual activity was measured against triolein. The FS was also

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Section: Introductionmentioning

confidence: 99%

Production of a fermented solid containing lipases from Penicillium roqueforti ATCC 10110 and its direct employment in organic medium in ethyl oleate synthesis

Soares¹,

Alnoch

Dias

et al. 2021

Biotech and App Biochem

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“…For the stability assays, the relative activity (RA, %) of lipase from A. japonicus lipase immobilized by physical adsorption were calculated according to the Equation (2): RA = (L A × 100)/L A0 (2) where: L A is the free/immobilized lipase activity after the incubation time and L A0 initial enzymatic activity.…”

Section: Stability Of the Free And Immobilized Microbial Lipasementioning

confidence: 99%

“…Lipases (also triacylglycerol ester hydrolase) [EC 3.1.1.3] are enzymes that hydrolyze ester linkages of triglycerides [1,2]. Since these enzymes present large structural and functional versatility, they are of greatest importance in industrial sector to be applied in the food, pharmaceutical, detergent, textile, biodiesel production, cosmetic, among others [3,4].…”

Section: Introductionmentioning

confidence: 99%

“…Considering the high number of lipase applications, the microbial lipase market was valued at $400.6 million in 2017, with expectations to achieve a $590 million in 2023 at a Compound annual growth rate (CAGR) of 6.8% [5]. Over the last years, the growing interest in large-scale production of more natural enzymes, i.e., microbial lipase, has increased due to its outstanding advantages, viz., high stability, high productivity yield, no seasonal restrictions, use of agro-waste/residues as feedstock and low-cost production as compared to other sources (animal or vegetable) [2,3,6].…”

Section: Introductionmentioning

confidence: 99%

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Utilization of Clay Materials as Support for Aspergillus japonicus Lipase: An Eco-Friendly Approach

et al. 2021

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Lipase is an important group of biocatalysts, which combines versatility and specificity, and can catalyze several reactions when applied in a high amount of industrial processes. In this study, the lipase produced by Aspergillus japonicus under submerged cultivation, was immobilized by physical adsorption, using clay supports, namely, diatomite, vermiculite, montmorillonite KSF (MKSF) and kaolinite. Besides, the immobilized and free enzyme was characterized, regarding pH, temperature and kinetic parameters. The most promising clay support was MKSF that presented 69.47% immobilization yield and hydrolytic activity higher than the other conditions studied (270.7 U g−1). The derivative produced with MKSF showed high stability at pH and temperature, keeping 100% of its activity throughout 12 h of incubation in the pH ranges between 4.0 and 9.0 and at a temperature from 30 to 50 °C. In addition, the immobilized lipase on MKSF support showed an improvement in the catalytic performance. The study shows the potential of using clays as support to immobilized lipolytic enzymes by adsorption method, which is a simple and cost-effective process.

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“…Researchers are contributing greatly to insights into the effects of organic solvents on lipases. Sanker et al [5] performed MD simulation with plant lipase to study the lid changes of lipase in toluene solvent. Zhu et al [6] investigated the conformational stability of porcine pancreatic lipase in three non-aqueous organic solvents, including dimethyl sulfoxide, propylene glycol and ethanol, through MD simulation.…”

Section: Introductionmentioning

confidence: 99%

Micro-Aqueous Organic System: A Neglected Model in Computational Lipase Design?

Wang

Xiang

2021

Biomolecules

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Water content is an important factor in lipase-catalyzed reactions in organic media but is frequently ignored in the study of lipases by molecular dynamics (MD) simulation. In this study, Candida antarctica lipase B, Candida rugosa lipase and Rhizopus chinensis lipase were used as research models to explore the mechanisms of lipase in micro-aqueous organic solvent (MAOS) media. MD simulations indicated that lipases in MAOS systems showed unique conformations distinguished from those seen in non-aqueous organic solvent systems. The position of water molecules aggregated on the protein surface in MAOS media is the major determinant of the unique conformations of lipases and particularly impacts the distribution of hydrophilic and hydrophobic amino acids on the lipase surface. Additionally, two maxima were observed in the water-lipase radial distribution function in MAOS systems, implying the formation of two water shells around lipase in these systems. The energy landscapes of lipases along solvent accessible areas of catalytic residues and the minimum energy path indicated the dynamic open states of lipases in MAOS systems differ from those in other solvent environments. This study confirmed the necessity of considering the influence of the microenvironment on MD simulations of lipase-catalyzed reactions in organic media.

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Less explored plant lipases: Modeling and molecular dynamics simulations of plant lipases in different solvents and temperatures to understand structure-function relationship

Cited by 21 publications

References 56 publications

Production of a fermented solid containing lipases from Penicillium roqueforti ATCC 10110 and its direct employment in organic medium in ethyl oleate synthesis

Production of a fermented solid containing lipases from Penicillium roqueforti ATCC 10110 and its direct employment in organic medium in ethyl oleate synthesis

Utilization of Clay Materials as Support for Aspergillus japonicus Lipase: An Eco-Friendly Approach

Micro-Aqueous Organic System: A Neglected Model in Computational Lipase Design?

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