Extremophilic lipases for industrial applications: A general review

Vivek, K.; Sandhia, G.S.; Subramaniyan, S.

doi:10.1016/j.biotechadv.2022.108002

Cited by 63 publications

(29 citation statements)

References 202 publications

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“…1,2 Lipase can catalyze esterification and transesterification reactions, and its application in the synthesis of flavor and fragrance esters is among its important applications. 3,4 Enzymatic reactions are promising with high efficiency, specificity and mildness. Studies have shown that short chain esters synthesized by immobilized lipase has good application prospects.…”

Section: Introductionmentioning

confidence: 99%

Covalent immobilization of lipase on an ionic liquid-functionalized magnetic Cu-based metal–organic framework with boosted catalytic performance in flavor ester synthesis

et al. 2023

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Section: Introductionmentioning

confidence: 99%

Covalent immobilization of lipase on an ionic liquid-functionalized magnetic Cu-based metal–organic framework with boosted catalytic performance in flavor ester synthesis

et al. 2023

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“…Lipases (triacylglycerol ester hydrolase, EC 3.1.1.3) can catalyze many different reactions due to their broad specificity for some substrates. In addition to the hydrolysis that converts triglycerides into fatty acids and glycerol, lipases have been efficiently employed to catalyze numerous reactions, such as the synthesis of esters, amination, transesterification, interesterification, alcoholysis, acidolysis, aminolysis, and acylation. − Hence, lipases have been used in various industries, including chemicals, detergents, food, cosmetics, pharmaceuticals, paper industries, and biodiesel production. − …”

Section: Introductionmentioning

confidence: 99%

Novel Lipase Reactor based on Discontinuous Interfaces in Hydrogel-Organogel Hybrid Gel: A Preliminary Exploration

Ming

Sun

Chen

et al. 2023

J. Agric. Food Chem.

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According to the "interfacial activation" mechanism, constructing a sufficient interface is the key strategy for lipasecatalytic system designing. Based on the "infinite interface in finite three-dimensional space" logic, in the current study, poly(N,Ndimethylacrylamide) (PDMA)-polybutyl methacrylate (PBMA) hybrid gels were prepared by a two-step crosslinking strategy, subsequently constructed as lipase-interfacial catalytic systems. The results confirm that the PDMA-PBMA hybrid gels with "networks in pores" structures could swell both the aqueous phase and organic phase. The balance between water swelling and isooctane swelling, hybrid gel space (height control), and the lipase entry manner significantly affect the interface construction and consequently the catalytic efficiency. The enzyme−substrate contact rate affected by swelling leads to three catalytic stages. Considering the spatial barrier and distribution of lipases, a potential high-performance lipase reactor can be assembled from smallsize, lamellar-like, and porous hybrid gels. The reactors also show good time storage and low temperature tolerance.

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“…12,13 Most of the enzymatic conversions in industrial processes occur in severe environments, for example, nonaqueous phase, high temperature, high pressure, and extreme pH, and these specific requirements must be met for industrial application of enzymes. 14,15 Although a large number of lipases had been isolated, identified, and characterized, only a few of them have been used commercially, and the main reason is the harsh reaction conditions mentioned above. 15 Therefore, efforts were devoted to discovering or modifying new enzymes with extreme properties such as immobilization, 16 protein engineering (random mutation, rational design), in vitro directed evolution, and use of recombinases.…”

Section: ■ Introductionmentioning

confidence: 99%

“…14,15 Although a large number of lipases had been isolated, identified, and characterized, only a few of them have been used commercially, and the main reason is the harsh reaction conditions mentioned above. 15 Therefore, efforts were devoted to discovering or modifying new enzymes with extreme properties such as immobilization, 16 protein engineering (random mutation, rational design), in vitro directed evolution, and use of recombinases. Motif-directed recombination enhanced the thermostability of a lipase from Candida rugosa by 100-fold at 50 °C; 17 the rational design and saturation mutagenesis improved the thermal stability of coldadapted LipC from Pseudomonas aeruginosa by up to 7-fold; 18 and resonance assignments promoted the thermostable evolution of lipase A from Bacillus subtilis.…”

Section: ■ Introductionmentioning

confidence: 99%

Hotspots and Mechanisms of Action of the Thermostable Framework of a Microbial Thermolipase

et al. 2022

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The lipase TrLipB from Thermomicrobium roseum is highly thermostable. However, its thermostable skeleton and mechanism of action should be investigated for industrial applications. Toward this, TrLipB was crystallized using the hanging-drop vapor diffusion method and subjected to Xray diffraction at 2.0 Å resolution in this study. The rigid sites, such as the prolines on the relatively flexible loops on the enzyme surface, were scanned. Soft substitutions of these sites were designed using both molecular dynamics (MD) simulation and site-directed mutagenesis. The thermostability of several substitutions decreased markedly, while the catalytic efficiencies of the P9G, P127G, P194G, and P300G mutants reduced substantially; additionally, the thermostable framework of the double mutant, P194G/P300G, was considerably perturbed. However, the substitutions on the lid of the enzyme, including P49G and P48G, promoted the catalytic efficiency to approximately 150% and slightly enhanced the thermostability below 80 °C. In MD simulations, the P100G, P194G, P100G/P194G, P194G/ P300G, and P100G/P194G/P300G mutants showed high B-factors and RMSD values, whereas the secondary structures, radius of gyration, H-bonds, and solvent accessible surface areas of these mutants were markedly affected. Our observations will assist in understanding the natural framework of a stable lipase, which might contribute to its industrial applications.

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Extremophilic lipases for industrial applications: A general review

Cited by 63 publications

References 202 publications

Covalent immobilization of lipase on an ionic liquid-functionalized magnetic Cu-based metal–organic framework with boosted catalytic performance in flavor ester synthesis

Covalent immobilization of lipase on an ionic liquid-functionalized magnetic Cu-based metal–organic framework with boosted catalytic performance in flavor ester synthesis

Novel Lipase Reactor based on Discontinuous Interfaces in Hydrogel-Organogel Hybrid Gel: A Preliminary Exploration

Hotspots and Mechanisms of Action of the Thermostable Framework of a Microbial Thermolipase

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