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Lozano, Pedro; Diego, Teresa De; Carrié, Daniel; Vaultier, Michel; Iborra, José L.

doi:10.1023/a:1011697609756

Cited by 259 publications

(117 citation statements)

References 16 publications

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“…This diverse repertoire of enzymatic reactions demonstrates the potential value of RTILs as novel media for enzymatic reactions. In addition, RTILs have been shown to support enhanced operational properties of enzymes, such as increased thermal stability [7,14,15].…”

Section: Introductionmentioning

confidence: 99%

Enzyme–Carbon Nanotube Conjugates in Room-temperature Ionic Liquids

Eker

Asuri

Murugesan

et al. 2007

Appl Biochem Biotechnol

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Room-temperature ionic liquids (RTILs) are intriguing solvents, which are recognized as "green" alternatives to volatile organics. Although RTILs are nonvolatile and can dissolve a wide range of charged, polar, and nonpolar organic and inorganic molecules, there remain substantial challenges in their use, not the least of which is the solvents' high viscosity that leads to potential mass transfer limitations. In the course of this work, we discovered that the simple adsorption of the bacterial protease, proteinase K, onto singlewalled carbon nanotubes (SWNTs) results in intrinsically high catalytic turnover. The high surface area and the nanoscopic dimensions of SWNTs offered high enzyme loading and low mass transfer resistance. Furthermore, the enzyme-SWNT conjugates displayed enhanced thermal stability in RTILs over the native suspended enzyme counterpart and allowed facile reuse. These enzyme-SWNT conjugates may therefore provide a way to overcome key operational limitations of RTIL systems.

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Section: Introductionmentioning

confidence: 99%

Enzyme–Carbon Nanotube Conjugates in Room-temperature Ionic Liquids

Eker

Asuri

Murugesan

et al. 2007

Appl Biochem Biotechnol

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“…而"在亲水性离子液体-酶"组成的微环境中(图 1b), 离子液体由于本身具有更高的介电常数, 从而取代结合在酶表面的水分子, 引起脂肪酶的肽链解折叠, 最终表现为酶的活性降低甚至失活 [3] . 图 1 疏水性和亲水性离子液体对酶表面微环境的影响 Figure 1 Hydrophobic and hydrophilic ILs' effects on microenvironment on the surface of lipase Rubio 等 [42] 在离子液体中以向日葵和废弃食用油为原料进行酯交换反应, 结果表明 CaLB 在亲水性较强的 [5] . 因此, 脂肪酶催化酯类合成中, 常选择疏水性离子液体作为反应介质.…”

Section: 影响脂肪酶的微环境unclassified

Progress of Lipase-Catalyzed Ester Synthesis in Ionic Liquid

Li¹,

Wang²,

Leixia³

et al. 2012

Chin. J. Org. Chem.

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“…(E) As an environmentally friendly alternative, 1 was used as reaction media for butylbutyrate synthesis 14 catalyzed by free Candida antartica lipase (CAL) B with 2% water content at 50°C and showed enhanced synthetic activity. …”

Section: Ohmentioning

confidence: 99%