Optimization of aqueous two-phase partitioning of Aureobasidium pullulans α-amylase via response surface methodology and investigation of its thermodynamic and kinetic properties

Ademakinwa, Adedeji Nelson; Agunbiade, Mayowa Oladele; Ayinla, Zainab Adenike; Agboola, Femi Kayode

doi:10.1016/j.ijbiomac.2019.08.159

Cited by 21 publications

(14 citation statements)

References 26 publications

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“…Both enzyme form's enzymatic activity decayed in a typical first-order heat inactivation pattern. This inactivation pattern is similar to other enzymes produced by this fungus [15,[23][24][25].…”

Section: Ph and Temperature Stabilitysupporting

confidence: 82%

“…It was concluded that the laccase CLEA was more thermostable than the free enzyme. The thermostability of CLEA or other immobilized enzymes over their free enzyme has been reported in recent literature [17,21,[23][24][25] Heat inactivation studies Table 2 shows the summary of the kinetic and thermodynamic parameters for both the free and immobilized laccase. Both enzyme form's enzymatic activity decayed in a typical first-order heat inactivation pattern.…”

Section: Ph and Temperature Stabilitymentioning

confidence: 99%

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Laccase immobilization via cross-linked aggregate preparation: Characterization, thermodynamic/kinetic properties and application in removal of bisphenol A from solutions

Ademakinwa

2021

Preprint

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Fungal laccase from Aureobasidium pullulans was immobilized via cross-linked enzyme aggregate (CLEA) preparation under statistically optimized conditions. The stability of the CLEA to heat inactivation was studied via investigation of its thermodynamic and kinetic parameters. The immobilized enzyme was then deployed in the biodegradation of a bisphenol-A (BPA). The optimum conditions for CLEA preparation resulting in the highest immobilization yield were ammonium sulphate (60% v/v), glutaraldehyde (30 mM), pH (4.5), time (6 h) and temperature (55ºC). The CLEA retained about 51% of its activity after eight catalytic cycles. The optimum pH and temperature of the laccase CLEA were 5.5 and 60ºC respectively. The SEM indicated that the laccase CLEA was type II (unstructured). The data obtained from the heat inactivation kinetics and thermodynamic characterization indicated that the CLEA was stable to heat denaturation than the free enzyme. The kinetic parameters obtained for the CLEA with ABTS as substrate were 101.3 µM, 2.94 µmols-1mg-1 and 0.03 dm3s-1mg-1 for the Km, Kcat and Kcat/Km respectively. The optimum conditions for BPA biodegradation using the CLEA were temperature (55ºC), time (2 h), CLEA (1.0 mg) and BPA concentration (40 mg/L). After the 7th cycle, laccase CLEA retained about 63 ± 2.3% biodegradation efficiency. A heat-resistant laccase CLEA was able to remove BPA from solutions under statistically optimized conditions. The laccase CLEA has properties for other futuristic applications.

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Section: Ph and Temperature Stabilitysupporting

confidence: 82%

Section: Ph and Temperature Stabilitymentioning

confidence: 99%

Laccase immobilization via cross-linked aggregate preparation: Characterization, thermodynamic/kinetic properties and application in removal of bisphenol A from solutions

Ademakinwa

2021

Preprint

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“…The change in α-amylase dimensionless activity a is also described by the first-order kinetics [26,27] with the following equation…”

Section: The Effect Of Temperature On α-Amylase Activitymentioning

confidence: 99%

Determination of Activation Energies and the Optimum Temperatures of Hydrolysis of Starch by α-Amylase from Porcine Pancreas

Miłek

2021

Molecules

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The present paper reports the determination of the activation energies and the optimum temperatures of starch hydrolysis by porcine pancreas α-amylase. The parameters were estimated based on the literature data on the activity curves versus temperature for starch hydrolysis by α-amylase from porcine pancreas. It was assumed that both the hydrolysis reaction process and the deactivation process of α-amylase were first-order reactions by the enzyme concentration. A mathematical model describing the effect of temperature on porcine pancreas α-amylase activity was used. The determine deactivation energies Ea were from 19.82 ± 7.22 kJ/mol to 128.80 ± 9.27 kJ/mol, the obtained optimum temperatures Topt were in the range from 311.06 ± 1.10 K to 326.52 ± 1.75 K. In turn, the values of deactivation energies Ed has been noted in the range from 123.57 ± 14.17 kJ/mol to 209.37 ± 5.17 kJ/mol. The present study is related to the starch hydrolysis by α-amylase. In the industry, the obtained results the values Ea, Ed, Topt can be used to design and optimize starch hydrolysis by α-amylase porcine pancreas. The obtained results might also find application in research on the pharmaceutical preparations used to treat pancreatic insufficiency or prognosis of pancreatic cancer.

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“…Enzymes are known as biological catalysts that facilitate complex chemical processes within optimum conditions. α-amylase (EC 3.2.1.1) is a significant enzyme, especally in textile [1], food processing [2], paper pulping [3] and pharmaceutical industries [4]. Amylases have been a source of inspiration for some research areas regarding their applications in the food and fermentation business lines.…”

Section: Introductionmentioning

confidence: 99%

α-Amylase Immobilized Composite Cryogels: Some Studies on Kinetic and Adsorption Factors

Acet

Inanan

Acet

et al. 2021

Appl Biochem Biotechnol

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Stability of enzymes is significant factor for their industrial feasibility. α-amylase is an important enzyme for some industries i.e., textile, food, paper and pharmaceutics.. Pumice particles (PPa) are non-toxic, natural, low-cost alternative adsorbents with high adsorption capacity. In this study, Cu 2+ ions were attached onto pumice particles (Cu 2+ -APPa). Then, Cu 2+ -APPa embedded composite cryogel was synthesized (Cu 2+ -APPaC) via polymerization of gelforming agents at minus temperatures. Characterization studies of the Cu 2+ -APPaC cryogel column was performed by X-ray fluorescence spectrometer (XRF), scanning electron microscopy (SEM), and Brunauer, Emmett, Teller (BET) apparatus. The experiments were carried out in a continuous column system. α-amylase was adsorbed onto Cu 2+ -APPaC cryogel with maximum amount of 858.7 mg/g particles at pH 4.0. Effects of pH and temperature on the activity profiles of the free and the immobilized α-amylase were investigated, and results indicate that immobilization did not alter the optimum pH and temperature values. kcat value of the immobilized α-amylase is higher than that of the free α-amylase while KM value increases by immobilization. Storage and operational stabilities of the free and the immobilized αamylase were determined for 35 days and for 20 runs, respectively.

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Optimization of aqueous two-phase partitioning of Aureobasidium pullulans α-amylase via response surface methodology and investigation of its thermodynamic and kinetic properties

Cited by 21 publications

References 26 publications

Laccase immobilization via cross-linked aggregate preparation: Characterization, thermodynamic/kinetic properties and application in removal of bisphenol A from solutions

Laccase immobilization via cross-linked aggregate preparation: Characterization, thermodynamic/kinetic properties and application in removal of bisphenol A from solutions

Determination of Activation Energies and the Optimum Temperatures of Hydrolysis of Starch by α-Amylase from Porcine Pancreas

α-Amylase Immobilized Composite Cryogels: Some Studies on Kinetic and Adsorption Factors

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