2012
DOI: 10.1016/j.bej.2011.10.005
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Primary recovery of lipase derived from Burkholderia cenocepacia strain ST8 and recycling of phase components in an aqueous two-phase system

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Cited by 49 publications
(24 citation statements)
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“…In general, their results showed successful partitioning of the desired product (laccase) towards the top phase (PEG), while the contaminants were partitioned to the bottom phase (phosphate buffer solution) with the highest recovery percentage (up to 60%) with PEG 1000 and PEG 1450. Although studies on the recovery of laccases using ATPS are scarce there are several reports of the recovery of other proteins …”
Section: Resultsmentioning
confidence: 99%
“…In general, their results showed successful partitioning of the desired product (laccase) towards the top phase (PEG), while the contaminants were partitioned to the bottom phase (phosphate buffer solution) with the highest recovery percentage (up to 60%) with PEG 1000 and PEG 1450. Although studies on the recovery of laccases using ATPS are scarce there are several reports of the recovery of other proteins …”
Section: Resultsmentioning
confidence: 99%
“…The concentrated EOPO solution from the secondary ATPS can be reused to further extract proteins from the salt solution in the primary ATPS (Fig. 2) [40].…”
Section: Novel Lipase Purification Methodsmentioning
confidence: 99%
“… An illustration of an extractive fermentation process using the recycling ATPS developed by Show et al [40] (*Reproduced with permission from Elsevier). …”
Section: Novel Lipase Purification Methodsmentioning
confidence: 99%
“…The impact of the loaded mass on the partition of enzymes is important, as the loaded feed stock can alter the phase volume ratio [44] and the partition behavior of target protein [45]. The increasing amounts of both polygalacturonase and contaminants in the systems could result in a decrease of the liquid/liquid extraction process performance.…”
Section: The Effect Of Crude Feedstock Concentration and Total Volumementioning
confidence: 99%