Please use this identifier to cite or link to this item: http://repository.elizadeuniversity.edu.ng/jspui/handle/20.500.12398/532
Title: Optimization of Aqueous Two-Phase Partitioning of Aureobasidium pullulans α-Amylase via Response Surface Methodology and Investigation of its Thermodynamic and Kinetic Properties
Authors: Ademakinwa, Adedeji N.
Agunbiade, Mayowa O.
Ayinla, Zainab A.
Agboola, Femi K.
Keywords: Alpha amylase
Aureobasidium pullulans
Optimization
Thermodynamics
Issue Date: 29-Aug-2019
Publisher: Elsevier
Abstract: Industrial 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.
URI: doi.org/10.1016/j.ijbiomac.2019.08.159
http://repository.elizadeuniversity.edu.ng/jspui/handle/20.500.12398/532
Appears in Collections:Research Articles

Files in This Item:
File Description SizeFormat 
Alpha amylase Ademakinwa et al 2019.pdf907.32 kBAdobe PDFThumbnail
View/Open


Items in EUSpace are protected by copyright, with all rights reserved, unless otherwise indicated.