Optimization of Aqueous Two-Phase Partitioning of Aureobasidium pullulans α-Amylase via Response Surface Methodology and Investigation of its Thermodynamic and Kinetic Properties

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dc.contributor.authorAdemakinwa, Adedeji N.
dc.contributor.authorAgunbiade, Mayowa O.
dc.contributor.authorAyinla, Zainab A.
dc.contributor.authorAgboola, Femi K.
dc.date.accessioned2019-10-15T11:59:48Z
dc.date.available2019-10-15T11:59:48Z
dc.date.issued2019-08-29
dc.description.abstractIndustrial enzymes such as α-amylase must be thermostable and also easily purified/concentrated. Hence, aqueous two-phase partitioning systems (ATPS) was exploited for the partitioning of α-amylase from Aureobasidium pullulans due to its numerous advantages over conventional purification strategy. A. pullulans α-amylase was partially purified using ATPS via response surface methodology (RSM). The potentials of the ATPS-purified enzyme for possible industrial application such as resistance to thermal inactivation was investigated in comparison with the crude enzyme. PEG-6000 was the polymer of choice for ATPS as it resulted in higher purification factor (PF), %yield (Y), and partition coefficient (PC). At optimum levels (% w/v) of 20, 12 and 7.5 for PEG-6000, sodium citrate and sodium chloride respectively, maximum PF, Y and PC of 4.2, 88%, and 9.9 respectively were obtained. The response model validation and reliability were established based on the closeness between the experimented and predicted values. The kinetic and thermodynamic parameters such as Q10, t1/2, kd, D − value, Ed, of the ATPS-purified α-amylase indicated that it was thermostable at 50 to 60 °C compared to the crude α-amylase. A thermodynamically stable and ATPS-purified α-amylase from A. pullulans has properties easily applicable for most industrial processes.en_US
dc.identifier.uridoi.org/10.1016/j.ijbiomac.2019.08.159
dc.identifier.urihttp://repository.elizadeuniversity.edu.ng/handle/20.500.12398/532
dc.language.isoenen_US
dc.publisherElsevieren_US
dc.subjectAlpha amylaseen_US
dc.subjectAureobasidium pullulansen_US
dc.subjectOptimizationen_US
dc.subjectThermodynamicsen_US
dc.titleOptimization of Aqueous Two-Phase Partitioning of Aureobasidium pullulans α-Amylase via Response Surface Methodology and Investigation of its Thermodynamic and Kinetic Propertiesen_US
dc.typeArticleen_US
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