Selective esterification of phthalic acids in two ionic liquids at high temperatures using a thermostable lipase of Bacillus thermocatenulatus: A comparative study

Martín, Jesús Antonio Martínez; Nus, Meritxel; Gago, José Vicente Sinisterra; Sánchez-Montero, J.M.

doi:10.1016/j.molcatb.2007.11.018

Cited by 21 publications

(10 citation statements)

References 34 publications

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“…The rates were the same as or slightly higher than those observed in the best organic solvents. There have been many reports of remarkable increases in enzyme stabilities in ILs containing noncoordinating anions, 115 and enhanced (enantio)selectivities have been observed in some cases. 116 These probably result from conformational changes of enzymes in IL media.…”

Section: Ionic Liquids (Ils)mentioning

confidence: 99%

Role of Biocatalysis in Sustainable Chemistry

2017

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Based on the principles and metrics of green chemistry and sustainable development, biocatalysis is both a green and sustainable technology. This is largely a result of the spectacular advances in molecular biology and biotechnology achieved in the past two decades. Protein engineering has enabled the optimization of existing enzymes and the invention of entirely new biocatalytic reactions that were previously unknown in Nature. It is now eminently feasible to develop enzymatic transformations to fit predefined parameters, resulting in processes that are truly sustainable by design. This approach has successfully been applied, for example, in the industrial synthesis of active pharmaceutical ingredients. In addition to the use of protein engineering, other aspects of biocatalysis engineering, such as substrate, medium, and reactor engineering, can be utilized to improve the efficiency and cost-effectiveness and, hence, the sustainability of biocatalytic reactions. Furthermore, immobilization of an enzyme can improve its stability and enable its reuse multiple times, resulting in better performance and commercial viability. Consequently, biocatalysis is being widely applied in the production of pharmaceuticals and some commodity chemicals. Moreover, its broader application will be further stimulated in the future by the emerging biobased economy.

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Section: Ionic Liquids (Ils)mentioning

confidence: 99%

Role of Biocatalysis in Sustainable Chemistry

2017

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“…imidazolium salts are the most frequently applied ionic liquids as media in lipase-catalyzed reactions. in many cases, it is observed that the imidazolium hexafluorophosphates, tetraborates, bis[(trifluoromethyl)sulfonyl]amides or trifluoromethylsulfonates improve the performance of the immobilized biocatalysts (28,31). there are several papers on increased enantioselectivity and activity of lipases from C. rugosa, C. antarctica and Ps.…”

Section: Stability Of Nanosno 2 -Mc7 In Organic Solventsmentioning

confidence: 99%

Excellent Stability and Synthetic Activity of Lipase fromB. StearothermophilusMC7 Immobilized on Tin Dioxide in Environmentally Friendly Medium

Guncheva

Dimitrov

Kambourova

2013

Biotechnology & Biotechnological Equipment

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“…Finally, lipases, that is, enzymes that catalyze triacylglycerol hydrolysis, are widely used in organic chemistry due to their high specificity and selectivity [8]. Thus, they have received considerable attention because of their potential use in industrial processes [9], especially as biocatalysts.…”

Section: Introductionmentioning

confidence: 99%

“…Thus, they have received considerable attention because of their potential use in industrial processes [9], especially as biocatalysts. Among the reasons for the enormous potential of these enzymes are their high stability in organic solvents, the nonrequirement for cofactors, and broad substrate specificity [8]. However, these enzymes are only moderately stable at high temperatures where most industrial processes are performed.…”

Section: Introductionmentioning

confidence: 99%

“…However, these enzymes are only moderately stable at high temperatures where most industrial processes are performed. This drawback might be solved with the use of lipases produced by thermophilic microorganisms [8]. Bacillus subtilis secretes different lipases that vary according to growth and environmental conditions, pH, and amino acid supply [10].…”

Section: Introductionmentioning

confidence: 99%

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Production of Enzymes from Agroindustrial Wastes by Biosurfactant-Producing Strains of Bacillus subtilis

Barros

Simiqueli

Andrade

et al. 2013

Biotechnology Research International

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Bacteria in the genus Bacillus are the source of several enzymes of current industrial interest. Hydrolases, such as amylases, proteases, and lipases, are the main enzymes consumed worldwide and have applications in a wide range of products and industrial processes. Fermentation processes by Bacillus subtilis using cassava wastewater as a substrate are reported in the technical literature; however, the same combination of microorganisms and this culture medium is limited or nonexistent. In this paper, the amylase, protease, and lipase production of ten Bacillus subtilis strains previously identified as biosurfactant producers in cassava wastewater was evaluated. The LB1a and LB5a strains were selected for analysis using a synthetic medium and cassava wastewater and were identified as good enzyme producers, especially of amylases and proteases. In addition, the enzymatic activity results indicate that cassava wastewater was better than the synthetic medium for the induction of these enzymes.

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Selective esterification of phthalic acids in two ionic liquids at high temperatures using a thermostable lipase of Bacillus thermocatenulatus: A comparative study

Cited by 21 publications

References 34 publications

Role of Biocatalysis in Sustainable Chemistry

Role of Biocatalysis in Sustainable Chemistry

Excellent Stability and Synthetic Activity of Lipase fromB. StearothermophilusMC7 Immobilized on Tin Dioxide in Environmentally Friendly Medium

Production of Enzymes from Agroindustrial Wastes by Biosurfactant-Producing Strains of Bacillus subtilis

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