Alcohol dehydrogenase on inorganic powders: Zeta potential and particle agglomeration as main factors determining activity during immobilization

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Abstract

Alcohol dehydrogenase from Saccharomyces cerevisiae was immobilized on different inorganic support materials, i.e. powders of Al2O3, SiC, TiO2 and YSZ-8, by covalent bonding and physical adsorption. The raw powders were characterized by scanning electron microscopy, BET surface area, particle size distribution and ζ-potential measurements. Enzyme activity retention, storage stability and recyclability were evaluated on the basis of the measured support material properties. Preliminary experiments showed that the buffer selection was a critical factor. The properties of both the enzyme and the powders varied considerably between the buffers used; namely Tris-HCl (100 mM, pH 7) and MES (40 mM, pH 6.5) buffers. The enzyme activity was higher and more stable in the MES buffer, whereas the commonly used Tris buffer was problematic due to apparent incompatibility with formaldehyde. In MES, the order of decreasing activity of covalently bonded enzyme was on SiC > YSZ-8 > Al2O3 > TiO2. The lower performance of TiO2 was ascribed to the negative ζ-potential of the material, which impeded an efficient immobilization. Particle agglomeration, caused by low colloidal stability of the particles in MES buffer, hampered the storage stability of the immobilized systems. The results from this study show the advantages and limitations of using nanoparticles as immobilization supports, and highlight which properties of nanoparticles must be considered to ensure an efficient immobilization.
Original languageEnglish
JournalColloids and Surfaces B: Biointerfaces
Volume175
Pages (from-to)136-142
ISSN0927-7765
DOIs
Publication statusPublished - 2018

Keywords

  • Enzyme immobilization
  • Inorganic powders
  • Alcohol dehydrogenase
  • Colloid stability

Cite this

@article{38bd7e95214348439f1557da465d31d3,
title = "Alcohol dehydrogenase on inorganic powders: Zeta potential and particle agglomeration as main factors determining activity during immobilization",
abstract = "Alcohol dehydrogenase from Saccharomyces cerevisiae was immobilized on different inorganic support materials, i.e. powders of Al2O3, SiC, TiO2 and YSZ-8, by covalent bonding and physical adsorption. The raw powders were characterized by scanning electron microscopy, BET surface area, particle size distribution and ζ-potential measurements. Enzyme activity retention, storage stability and recyclability were evaluated on the basis of the measured support material properties. Preliminary experiments showed that the buffer selection was a critical factor. The properties of both the enzyme and the powders varied considerably between the buffers used; namely Tris-HCl (100 mM, pH 7) and MES (40 mM, pH 6.5) buffers. The enzyme activity was higher and more stable in the MES buffer, whereas the commonly used Tris buffer was problematic due to apparent incompatibility with formaldehyde. In MES, the order of decreasing activity of covalently bonded enzyme was on SiC > YSZ-8 > Al2O3 > TiO2. The lower performance of TiO2 was ascribed to the negative ζ-potential of the material, which impeded an efficient immobilization. Particle agglomeration, caused by low colloidal stability of the particles in MES buffer, hampered the storage stability of the immobilized systems. The results from this study show the advantages and limitations of using nanoparticles as immobilization supports, and highlight which properties of nanoparticles must be considered to ensure an efficient immobilization.",
keywords = "Enzyme immobilization, Inorganic powders, Alcohol dehydrogenase, Colloid stability",
author = "Sigurdard{\'o}ttir, {Sigyn Bj{\"o}rk} and Jonas Lehmann and Jean‐Claude Grivel and Zhang, {Wenjing (Angela)} and Andreas Kaiser and Manuel Pinelo",
year = "2018",
doi = "10.1016/j.colsurfb.2018.11.080",
language = "English",
volume = "175",
pages = "136--142",
journal = "Colloids and Surfaces B: Biointerfaces",
issn = "0927-7765",
publisher = "Elsevier",

}

TY - JOUR

T1 - Alcohol dehydrogenase on inorganic powders: Zeta potential and particle agglomeration as main factors determining activity during immobilization

AU - Sigurdardóttir, Sigyn Björk

AU - Lehmann, Jonas

AU - Grivel, Jean‐Claude

AU - Zhang, Wenjing (Angela)

AU - Kaiser, Andreas

AU - Pinelo, Manuel

PY - 2018

Y1 - 2018

N2 - Alcohol dehydrogenase from Saccharomyces cerevisiae was immobilized on different inorganic support materials, i.e. powders of Al2O3, SiC, TiO2 and YSZ-8, by covalent bonding and physical adsorption. The raw powders were characterized by scanning electron microscopy, BET surface area, particle size distribution and ζ-potential measurements. Enzyme activity retention, storage stability and recyclability were evaluated on the basis of the measured support material properties. Preliminary experiments showed that the buffer selection was a critical factor. The properties of both the enzyme and the powders varied considerably between the buffers used; namely Tris-HCl (100 mM, pH 7) and MES (40 mM, pH 6.5) buffers. The enzyme activity was higher and more stable in the MES buffer, whereas the commonly used Tris buffer was problematic due to apparent incompatibility with formaldehyde. In MES, the order of decreasing activity of covalently bonded enzyme was on SiC > YSZ-8 > Al2O3 > TiO2. The lower performance of TiO2 was ascribed to the negative ζ-potential of the material, which impeded an efficient immobilization. Particle agglomeration, caused by low colloidal stability of the particles in MES buffer, hampered the storage stability of the immobilized systems. The results from this study show the advantages and limitations of using nanoparticles as immobilization supports, and highlight which properties of nanoparticles must be considered to ensure an efficient immobilization.

AB - Alcohol dehydrogenase from Saccharomyces cerevisiae was immobilized on different inorganic support materials, i.e. powders of Al2O3, SiC, TiO2 and YSZ-8, by covalent bonding and physical adsorption. The raw powders were characterized by scanning electron microscopy, BET surface area, particle size distribution and ζ-potential measurements. Enzyme activity retention, storage stability and recyclability were evaluated on the basis of the measured support material properties. Preliminary experiments showed that the buffer selection was a critical factor. The properties of both the enzyme and the powders varied considerably between the buffers used; namely Tris-HCl (100 mM, pH 7) and MES (40 mM, pH 6.5) buffers. The enzyme activity was higher and more stable in the MES buffer, whereas the commonly used Tris buffer was problematic due to apparent incompatibility with formaldehyde. In MES, the order of decreasing activity of covalently bonded enzyme was on SiC > YSZ-8 > Al2O3 > TiO2. The lower performance of TiO2 was ascribed to the negative ζ-potential of the material, which impeded an efficient immobilization. Particle agglomeration, caused by low colloidal stability of the particles in MES buffer, hampered the storage stability of the immobilized systems. The results from this study show the advantages and limitations of using nanoparticles as immobilization supports, and highlight which properties of nanoparticles must be considered to ensure an efficient immobilization.

KW - Enzyme immobilization

KW - Inorganic powders

KW - Alcohol dehydrogenase

KW - Colloid stability

U2 - 10.1016/j.colsurfb.2018.11.080

DO - 10.1016/j.colsurfb.2018.11.080

M3 - Journal article

C2 - 30529819

VL - 175

SP - 136

EP - 142

JO - Colloids and Surfaces B: Biointerfaces

JF - Colloids and Surfaces B: Biointerfaces

SN - 0927-7765

ER -