Activity stabilization of Aspergillus niger and Escherichia coli phytases immobilized on allophanic synthetic compounds and montmorillonite nanoclays

Lancaster Environment Centre

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https://doi.org/10.1016/j.biortech.2011.07.054
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Keywords

6-Phytase, Aluminum Silicates, Aspergillus niger, Bentonite, Enzymes, Immobilized, Escherichia coli, Nanotechnology, Proteolysis, Temperature, Thermodynamics, X-Ray Diffraction

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Activity stabilization of Aspergillus niger and Escherichia coli phytases immobilized on allophanic synthetic compounds and montmorillonite nanoclays. / Menezes-Blackburn, Daniel; Jorquera, Milko; Gianfreda, Liliana et al.
In: Bioresource Technology, Vol. 102, No. 20, 10.2011, p. 9360-7.

Research output: Contribution to Journal/Magazine › Journal article › peer-review

Bibtex

@article{b9de800946a14841a8d91bbeaafc80ee,

title = "Activity stabilization of Aspergillus niger and Escherichia coli phytases immobilized on allophanic synthetic compounds and montmorillonite nanoclays",

abstract = "The aim of this work was to study the stabilization of the activity of two commercial microbial phytases (Aspergillus niger and Escherichia coli) after immobilization on nanoclays and to establish optimal conditions for their immobilization. Synthetic allophane, synthetic iron-coated allophanes and natural montmorillonite were chosen as solid supports for phytase immobilization. Phytase immobilization patterns at different pH values were strongly dependent on both enzyme and support characteristics. After immobilization, the residual activity of both phytases was higher under acidic conditions. Immobilization of phytases increased their thermal stability and improved resistance to proteolysis, particularly on iron-coated allophane (6% iron oxide), which showed activation energy (E(a)) and activation enthalpy (ΔH(#)) similar to free enzymes. Montmorillonite as well as allophanic synthetic compounds resulted in a good support for immobilization of E. coli phytase, but caused a severe reduction of A. niger phytase activity.",

keywords = "6-Phytase, Aluminum Silicates, Aspergillus niger, Bentonite, Enzymes, Immobilized, Escherichia coli, Nanotechnology, Proteolysis, Temperature, Thermodynamics, X-Ray Diffraction",

author = "Daniel Menezes-Blackburn and Milko Jorquera and Liliana Gianfreda and Maria Rao and Ralf Greiner and Elizabeth Garrido and {de la Luz Mora}, Mar{\'i}a",

note = "Copyright {\textcopyright} 2011. Published by Elsevier Ltd.",

year = "2011",

month = oct,

doi = "10.1016/j.biortech.2011.07.054",

language = "English",

volume = "102",

pages = "9360--7",

journal = "Bioresource Technology",

issn = "0960-8524",

publisher = "Elsevier Limited",

number = "20",

}

RIS

TY - JOUR

T1 - Activity stabilization of Aspergillus niger and Escherichia coli phytases immobilized on allophanic synthetic compounds and montmorillonite nanoclays

AU - Menezes-Blackburn, Daniel

AU - Jorquera, Milko

AU - Gianfreda, Liliana

AU - Rao, Maria

AU - Greiner, Ralf

AU - Garrido, Elizabeth

AU - de la Luz Mora, María

PY - 2011/10

Y1 - 2011/10

N2 - The aim of this work was to study the stabilization of the activity of two commercial microbial phytases (Aspergillus niger and Escherichia coli) after immobilization on nanoclays and to establish optimal conditions for their immobilization. Synthetic allophane, synthetic iron-coated allophanes and natural montmorillonite were chosen as solid supports for phytase immobilization. Phytase immobilization patterns at different pH values were strongly dependent on both enzyme and support characteristics. After immobilization, the residual activity of both phytases was higher under acidic conditions. Immobilization of phytases increased their thermal stability and improved resistance to proteolysis, particularly on iron-coated allophane (6% iron oxide), which showed activation energy (E(a)) and activation enthalpy (ΔH(#)) similar to free enzymes. Montmorillonite as well as allophanic synthetic compounds resulted in a good support for immobilization of E. coli phytase, but caused a severe reduction of A. niger phytase activity.

AB - The aim of this work was to study the stabilization of the activity of two commercial microbial phytases (Aspergillus niger and Escherichia coli) after immobilization on nanoclays and to establish optimal conditions for their immobilization. Synthetic allophane, synthetic iron-coated allophanes and natural montmorillonite were chosen as solid supports for phytase immobilization. Phytase immobilization patterns at different pH values were strongly dependent on both enzyme and support characteristics. After immobilization, the residual activity of both phytases was higher under acidic conditions. Immobilization of phytases increased their thermal stability and improved resistance to proteolysis, particularly on iron-coated allophane (6% iron oxide), which showed activation energy (E(a)) and activation enthalpy (ΔH(#)) similar to free enzymes. Montmorillonite as well as allophanic synthetic compounds resulted in a good support for immobilization of E. coli phytase, but caused a severe reduction of A. niger phytase activity.

KW - 6-Phytase

KW - Aluminum Silicates

KW - Aspergillus niger

KW - Bentonite

KW - Enzymes, Immobilized

KW - Escherichia coli

KW - Nanotechnology

KW - Proteolysis

KW - Temperature

KW - Thermodynamics

KW - X-Ray Diffraction

U2 - 10.1016/j.biortech.2011.07.054

DO - 10.1016/j.biortech.2011.07.054

M3 - Journal article

C2 - 21856150

VL - 102

SP - 9360

EP - 9367

JO - Bioresource Technology

JF - Bioresource Technology

SN - 0960-8524

IS - 20

ER -

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