Enzyme encapsulation using highly ordered mesoporous silica monoliths

Shun Ichi Matsuura; Sherif A. El-Safty; Manami Chiba; Emiko Tomon; Tatsuo Tsunoda; Taka Aki Hanaoka

doi:10.1016/j.matlet.2012.08.110

Enzyme encapsulation using highly ordered mesoporous silica monoliths

Shun Ichi Matsuura^*, Sherif A. El-Safty, Manami Chiba, Emiko Tomon, Tatsuo Tsunoda, Taka Aki Hanaoka

^*Corresponding author for this work

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

18 Citations (Scopus)

Abstract

Lipase encapsulation in 12 highly ordered mesoporous silica monoliths (HOMs) with different pore diameters (3-8 nm) and pore structures (2D and 3D mesostructures) was successfully achieved without leaching of the enzyme from the enzyme-HOM composite. The amount of lipase adsorbed on the HOMs was dependent on the pore diameter and pore structure. The 3D mesostructures had better enzyme adsorption capability than did the 2D mesostructures. Reaction kinetics showed that the lipase-HOM composites maintained high enzymatic activity during the hydrolysis of a triglyceride (80-85 of the activity of the free enzyme). Moreover, the thermal stability of the composites was greater than that of the free enzyme. These results strongly demonstrated the ability of HOM-n monoliths to act as supports for the stable immobilization of enzymes, with minimal loss of enzymatic activity.

Original language	English
Pages (from-to)	184-187
Number of pages	4
Journal	Materials Letters
Volume	89
DOIs	https://doi.org/10.1016/j.matlet.2012.08.110
Publication status	Published - 2012 Dec 15

Keywords

Enzyme activity
Enzyme encapsulation
Hydrolysis
Lipase
Mesoporous silica

ASJC Scopus subject areas

Materials Science(all)
Condensed Matter Physics
Mechanical Engineering
Mechanics of Materials

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10.1016/j.matlet.2012.08.110

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title = "Enzyme encapsulation using highly ordered mesoporous silica monoliths",

abstract = "Lipase encapsulation in 12 highly ordered mesoporous silica monoliths (HOMs) with different pore diameters (3-8 nm) and pore structures (2D and 3D mesostructures) was successfully achieved without leaching of the enzyme from the enzyme-HOM composite. The amount of lipase adsorbed on the HOMs was dependent on the pore diameter and pore structure. The 3D mesostructures had better enzyme adsorption capability than did the 2D mesostructures. Reaction kinetics showed that the lipase-HOM composites maintained high enzymatic activity during the hydrolysis of a triglyceride (80-85 of the activity of the free enzyme). Moreover, the thermal stability of the composites was greater than that of the free enzyme. These results strongly demonstrated the ability of HOM-n monoliths to act as supports for the stable immobilization of enzymes, with minimal loss of enzymatic activity.",

keywords = "Enzyme activity, Enzyme encapsulation, Hydrolysis, Lipase, Mesoporous silica",

author = "Matsuura, {Shun Ichi} and El-Safty, {Sherif A.} and Manami Chiba and Emiko Tomon and Tatsuo Tsunoda and Hanaoka, {Taka Aki}",

year = "2012",

month = dec,

day = "15",

doi = "10.1016/j.matlet.2012.08.110",

language = "English",

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journal = "Materials Letters",

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T1 - Enzyme encapsulation using highly ordered mesoporous silica monoliths

AU - Matsuura, Shun Ichi

AU - El-Safty, Sherif A.

AU - Chiba, Manami

AU - Tomon, Emiko

AU - Tsunoda, Tatsuo

AU - Hanaoka, Taka Aki

PY - 2012/12/15

Y1 - 2012/12/15

N2 - Lipase encapsulation in 12 highly ordered mesoporous silica monoliths (HOMs) with different pore diameters (3-8 nm) and pore structures (2D and 3D mesostructures) was successfully achieved without leaching of the enzyme from the enzyme-HOM composite. The amount of lipase adsorbed on the HOMs was dependent on the pore diameter and pore structure. The 3D mesostructures had better enzyme adsorption capability than did the 2D mesostructures. Reaction kinetics showed that the lipase-HOM composites maintained high enzymatic activity during the hydrolysis of a triglyceride (80-85 of the activity of the free enzyme). Moreover, the thermal stability of the composites was greater than that of the free enzyme. These results strongly demonstrated the ability of HOM-n monoliths to act as supports for the stable immobilization of enzymes, with minimal loss of enzymatic activity.

AB - Lipase encapsulation in 12 highly ordered mesoporous silica monoliths (HOMs) with different pore diameters (3-8 nm) and pore structures (2D and 3D mesostructures) was successfully achieved without leaching of the enzyme from the enzyme-HOM composite. The amount of lipase adsorbed on the HOMs was dependent on the pore diameter and pore structure. The 3D mesostructures had better enzyme adsorption capability than did the 2D mesostructures. Reaction kinetics showed that the lipase-HOM composites maintained high enzymatic activity during the hydrolysis of a triglyceride (80-85 of the activity of the free enzyme). Moreover, the thermal stability of the composites was greater than that of the free enzyme. These results strongly demonstrated the ability of HOM-n monoliths to act as supports for the stable immobilization of enzymes, with minimal loss of enzymatic activity.

KW - Enzyme activity

KW - Enzyme encapsulation

KW - Hydrolysis

KW - Lipase

KW - Mesoporous silica

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U2 - 10.1016/j.matlet.2012.08.110

DO - 10.1016/j.matlet.2012.08.110

M3 - Article

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SN - 0167-577X

VL - 89

SP - 184

EP - 187

JO - Materials Letters

JF - Materials Letters

ER -

Enzyme encapsulation using highly ordered mesoporous silica monoliths

Abstract

Keywords

ASJC Scopus subject areas

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