2013
DOI: 10.5504/bbeq.2013.0010
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Excellent Stability and Synthetic Activity of Lipase fromB. StearothermophilusMC7 Immobilized on Tin Dioxide in Environmentally Friendly Medium

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Cited by 6 publications
(1 citation statement)
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“…All studied additives slowed down the process of thermal denaturation; an increased enzyme stability was observed for a large number of modifiers applied within a broad concentration range with the highest degree of activation when PEG 6000 was applied (up to 2.3-fold increase) [43]. A beneficial effect on the operational and thermal stability of lipase MC7 immobilized on nanostructured tin dioxide was observed in two ionic liquids [44]. Stearyl stearate production was achieved at a much higher reaction rate in the presence of 3methyl-1-octyl imidazolium chloride compared to solvent-free medium and 95% conversion of the substrates was achieved for 5 h at 65°C.…”
Section: Lipase Produced By G Stearothermophilus Mc7mentioning
confidence: 92%
“…All studied additives slowed down the process of thermal denaturation; an increased enzyme stability was observed for a large number of modifiers applied within a broad concentration range with the highest degree of activation when PEG 6000 was applied (up to 2.3-fold increase) [43]. A beneficial effect on the operational and thermal stability of lipase MC7 immobilized on nanostructured tin dioxide was observed in two ionic liquids [44]. Stearyl stearate production was achieved at a much higher reaction rate in the presence of 3methyl-1-octyl imidazolium chloride compared to solvent-free medium and 95% conversion of the substrates was achieved for 5 h at 65°C.…”
Section: Lipase Produced By G Stearothermophilus Mc7mentioning
confidence: 92%