The adsorption characteristics, activity and stability of trypsin onto mesoporous silicates

D. Goradia; J. Cooney; B. K. Hodnett; E. Magner

doi:10.1016/j.molcatb.2004.12.007

The adsorption characteristics, activity and stability of trypsin onto mesoporous silicates

D. Goradia, J. Cooney, B. K. Hodnett, E. Magner

University of Limerick

Research output: Contribution to journal › Article › peer-review

Abstract

The immobilization of the hydrolytic enzyme trypsin onto various mesoporous silicates (MPS) was studied. MPS were prepared using cationic or non-ionic surfactants (average pore diameters were in the range of 28-300 Å). All MPS were characterised by X-ray diffraction, scanning electron microscopy and nitrogen porosimetry. Enzyme purity strongly influenced loading. Trypsin adsorbed on MPS was found to be desorbed more readily by polyethylene glycol than by ammonium sulphate, suggesting that hydrophobic-hydrophilic interactions were important. Immobilized trypsin showed 10-20 times higher activity than the free trypsin and was stable for 4-6 weeks when stored at 4 or 25°C. The trypsin-MPS catalyst was successfully reused for up to 6 cycles

Original language	English
Pages (from-to)	231-239
Number of pages	9
Journal	Journal of Molecular Catalysis B: Enzymatic
Volume	32
Issue number	5-6
DOIs	https://doi.org/10.1016/j.molcatb.2004.12.007
Publication status	Published - 1 Mar 2005

Keywords

Adsorption
Desorption
Immobilization
Mesoporous silicates
Stability
Trypsin

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10.1016/j.molcatb.2004.12.007

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title = "The adsorption characteristics, activity and stability of trypsin onto mesoporous silicates",

abstract = "The immobilization of the hydrolytic enzyme trypsin onto various mesoporous silicates (MPS) was studied. MPS were prepared using cationic or non-ionic surfactants (average pore diameters were in the range of 28-300 {\AA}). All MPS were characterised by X-ray diffraction, scanning electron microscopy and nitrogen porosimetry. Enzyme purity strongly influenced loading. Trypsin adsorbed on MPS was found to be desorbed more readily by polyethylene glycol than by ammonium sulphate, suggesting that hydrophobic-hydrophilic interactions were important. Immobilized trypsin showed 10-20 times higher activity than the free trypsin and was stable for 4-6 weeks when stored at 4 or 25°C. The trypsin-MPS catalyst was successfully reused for up to 6 cycles",

keywords = "Adsorption, Desorption, Immobilization, Mesoporous silicates, Stability, Trypsin",

author = "D. Goradia and J. Cooney and Hodnett, {B. K.} and E. Magner",

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T1 - The adsorption characteristics, activity and stability of trypsin onto mesoporous silicates

AU - Goradia, D.

AU - Cooney, J.

AU - Hodnett, B. K.

AU - Magner, E.

PY - 2005/3/1

Y1 - 2005/3/1

N2 - The immobilization of the hydrolytic enzyme trypsin onto various mesoporous silicates (MPS) was studied. MPS were prepared using cationic or non-ionic surfactants (average pore diameters were in the range of 28-300 Å). All MPS were characterised by X-ray diffraction, scanning electron microscopy and nitrogen porosimetry. Enzyme purity strongly influenced loading. Trypsin adsorbed on MPS was found to be desorbed more readily by polyethylene glycol than by ammonium sulphate, suggesting that hydrophobic-hydrophilic interactions were important. Immobilized trypsin showed 10-20 times higher activity than the free trypsin and was stable for 4-6 weeks when stored at 4 or 25°C. The trypsin-MPS catalyst was successfully reused for up to 6 cycles

AB - The immobilization of the hydrolytic enzyme trypsin onto various mesoporous silicates (MPS) was studied. MPS were prepared using cationic or non-ionic surfactants (average pore diameters were in the range of 28-300 Å). All MPS were characterised by X-ray diffraction, scanning electron microscopy and nitrogen porosimetry. Enzyme purity strongly influenced loading. Trypsin adsorbed on MPS was found to be desorbed more readily by polyethylene glycol than by ammonium sulphate, suggesting that hydrophobic-hydrophilic interactions were important. Immobilized trypsin showed 10-20 times higher activity than the free trypsin and was stable for 4-6 weeks when stored at 4 or 25°C. The trypsin-MPS catalyst was successfully reused for up to 6 cycles

KW - Adsorption

KW - Desorption

KW - Immobilization

KW - Mesoporous silicates

KW - Stability

KW - Trypsin

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U2 - 10.1016/j.molcatb.2004.12.007

DO - 10.1016/j.molcatb.2004.12.007

M3 - Article

AN - SCOPUS:13844272253

SN - 1381-1177

VL - 32

SP - 231

EP - 239

JO - Journal of Molecular Catalysis B: Enzymatic

JF - Journal of Molecular Catalysis B: Enzymatic

IS - 5-6

ER -

The adsorption characteristics, activity and stability of trypsin onto mesoporous silicates

Abstract

Keywords

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