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Production of partially phosphorylated myo-inositol phosphates using phytases immobilised on magnetic nanoparticles

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Production of partially phosphorylated myo-inositol phosphates using phytases immobilised on magnetic nanoparticles. / Greiner, Ralf; Konietzny, Ursula; Blackburn, Daniel Menezes; Jorquera, Milko A.

In: Bioresource Technology, Vol. 142, 08.2013, p. 375-383.

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Greiner, Ralf ; Konietzny, Ursula ; Blackburn, Daniel Menezes ; Jorquera, Milko A. / Production of partially phosphorylated myo-inositol phosphates using phytases immobilised on magnetic nanoparticles. In: Bioresource Technology. 2013 ; Vol. 142. pp. 375-383.

Bibtex

@article{f5ae25cc263e41cea5d7bfce1b9758a9,
title = "Production of partially phosphorylated myo-inositol phosphates using phytases immobilised on magnetic nanoparticles",
abstract = "Phytases of different origin were covalently bound onto Fe3O4 magnetic nanoparticles (12 nm). Binding efficiencies of all three phytases were well above 70% relative to the number of aldehyde groups available on the surface of the magnetic nanoparticles. Temperature stability for all three phytases was enhanced as a consequence of immobilisation, whereas pH dependence of enzyme activity was not affected. Maximum catalytic activity of the immobilised phytases was found at 60°C (rye), 65°C (Aspergillus niger) and 70°C (Escherichia albertii). The immobilised enzymes exhibited the same excellent substrate specificities and unique myo-inositol phosphate phosphatase activities as their soluble counterparts. However, the catalytic turnover number dropped drastically for the immobilised phytases. The amount of the desired partially phosphorylated myo-inositol phosphate isomer could be easily controlled by the contact time of substrate solution and immobilised enzymes. The immobilised phytases showed a high operational stability by retaining almost full activity even after fifty uses.",
keywords = "6-Phytase, Enzymes, Immobilized, Hydrogen-Ion Concentration, Hydrolysis, Inositol Phosphates, Kinetics, Magnetics, Nanoparticles, Phosphorylation, Substrate Specificity, Temperature",
author = "Ralf Greiner and Ursula Konietzny and Blackburn, {Daniel Menezes} and Jorquera, {Milko A.}",
note = "Copyright {\textcopyright} 2013 Elsevier Ltd. All rights reserved.",
year = "2013",
month = aug,
doi = "10.1016/j.biortech.2013.05.056",
language = "English",
volume = "142",
pages = "375--383",
journal = "Bioresource Technology",
issn = "0960-8524",
publisher = "Elsevier Limited",

}

RIS

TY - JOUR

T1 - Production of partially phosphorylated myo-inositol phosphates using phytases immobilised on magnetic nanoparticles

AU - Greiner, Ralf

AU - Konietzny, Ursula

AU - Blackburn, Daniel Menezes

AU - Jorquera, Milko A.

N1 - Copyright © 2013 Elsevier Ltd. All rights reserved.

PY - 2013/8

Y1 - 2013/8

N2 - Phytases of different origin were covalently bound onto Fe3O4 magnetic nanoparticles (12 nm). Binding efficiencies of all three phytases were well above 70% relative to the number of aldehyde groups available on the surface of the magnetic nanoparticles. Temperature stability for all three phytases was enhanced as a consequence of immobilisation, whereas pH dependence of enzyme activity was not affected. Maximum catalytic activity of the immobilised phytases was found at 60°C (rye), 65°C (Aspergillus niger) and 70°C (Escherichia albertii). The immobilised enzymes exhibited the same excellent substrate specificities and unique myo-inositol phosphate phosphatase activities as their soluble counterparts. However, the catalytic turnover number dropped drastically for the immobilised phytases. The amount of the desired partially phosphorylated myo-inositol phosphate isomer could be easily controlled by the contact time of substrate solution and immobilised enzymes. The immobilised phytases showed a high operational stability by retaining almost full activity even after fifty uses.

AB - Phytases of different origin were covalently bound onto Fe3O4 magnetic nanoparticles (12 nm). Binding efficiencies of all three phytases were well above 70% relative to the number of aldehyde groups available on the surface of the magnetic nanoparticles. Temperature stability for all three phytases was enhanced as a consequence of immobilisation, whereas pH dependence of enzyme activity was not affected. Maximum catalytic activity of the immobilised phytases was found at 60°C (rye), 65°C (Aspergillus niger) and 70°C (Escherichia albertii). The immobilised enzymes exhibited the same excellent substrate specificities and unique myo-inositol phosphate phosphatase activities as their soluble counterparts. However, the catalytic turnover number dropped drastically for the immobilised phytases. The amount of the desired partially phosphorylated myo-inositol phosphate isomer could be easily controlled by the contact time of substrate solution and immobilised enzymes. The immobilised phytases showed a high operational stability by retaining almost full activity even after fifty uses.

KW - 6-Phytase

KW - Enzymes, Immobilized

KW - Hydrogen-Ion Concentration

KW - Hydrolysis

KW - Inositol Phosphates

KW - Kinetics

KW - Magnetics

KW - Nanoparticles

KW - Phosphorylation

KW - Substrate Specificity

KW - Temperature

U2 - 10.1016/j.biortech.2013.05.056

DO - 10.1016/j.biortech.2013.05.056

M3 - Journal article

C2 - 23747448

VL - 142

SP - 375

EP - 383

JO - Bioresource Technology

JF - Bioresource Technology

SN - 0960-8524

ER -