Solid-support immobilization of a "swing" fusion protein for enhanced glucose oxidase catalytic activity

Yoshiyuki Takatsuji, Ryota Yamasaki, Atsushi Iwanaga, Michael Lienemann, Markus Linder, Tetsuya Haruyama

Research output: Contribution to journalArticleScientificpeer-review

21 Citations (Scopus)

Abstract

The strategic surface immobilization of a protein can add new functionality to a solid substrate; however, protein activity, e.g., enzymatic activity, can be drastically decreased on immobilization onto a solid surface. The concept of a designed and optimized "molecular interface" is herein introduced in order to address this problem. In this study, molecular interface was designed and constructed with the aim of attaining high enzymatic activity of a solid-surface-immobilized a using the hydrophobin HFBI protein in conjunction with a fusion protein of HFBI attached to glucose oxidase (GOx). The ability of HFBI to form a self-organized membrane on a solid surface in addition to its adhesion properties makes it an ideal candidate for immobilization. The developed fusion protein was also able to form an organized membrane, and its structure and immobilized state on a solid surface were investigated using QCM-D measurements. This method of immobilization showed retention of high enzymatic activity and the ability to control the density of the immobilized enzyme. In this study, we demonstrated the importance of the design and construction of molecular interface for numerous purposes. This method of protein immobilization could be utilized for preparation of high throughput products requiring structurally ordered molecular interfaces, in addition to many other applications.
Original languageEnglish
Pages (from-to)186 - 191
JournalColloids and Surfaces B: Biointerfaces
Volume112
DOIs
Publication statusPublished - 2013
MoE publication typeA1 Journal article-refereed

Fingerprint

Glucose Oxidase
Glucose oxidase
oxidase
immobilization
glucose
Immobilization
catalytic activity
Catalyst activity
Fusion reactions
fusion
proteins
Proteins
solid surfaces
membranes
Membranes
Immobilized Enzymes
enzymes
adhesion
Adhesion
Enzymes

Keywords

  • glucose oxidase
  • hydorphobin
  • self-organized membrane
  • surface functionalization

Cite this

Takatsuji, Yoshiyuki ; Yamasaki, Ryota ; Iwanaga, Atsushi ; Lienemann, Michael ; Linder, Markus ; Haruyama, Tetsuya. / Solid-support immobilization of a "swing" fusion protein for enhanced glucose oxidase catalytic activity. In: Colloids and Surfaces B: Biointerfaces. 2013 ; Vol. 112. pp. 186 - 191.
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abstract = "The strategic surface immobilization of a protein can add new functionality to a solid substrate; however, protein activity, e.g., enzymatic activity, can be drastically decreased on immobilization onto a solid surface. The concept of a designed and optimized {"}molecular interface{"} is herein introduced in order to address this problem. In this study, molecular interface was designed and constructed with the aim of attaining high enzymatic activity of a solid-surface-immobilized a using the hydrophobin HFBI protein in conjunction with a fusion protein of HFBI attached to glucose oxidase (GOx). The ability of HFBI to form a self-organized membrane on a solid surface in addition to its adhesion properties makes it an ideal candidate for immobilization. The developed fusion protein was also able to form an organized membrane, and its structure and immobilized state on a solid surface were investigated using QCM-D measurements. This method of immobilization showed retention of high enzymatic activity and the ability to control the density of the immobilized enzyme. In this study, we demonstrated the importance of the design and construction of molecular interface for numerous purposes. This method of protein immobilization could be utilized for preparation of high throughput products requiring structurally ordered molecular interfaces, in addition to many other applications.",
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Solid-support immobilization of a "swing" fusion protein for enhanced glucose oxidase catalytic activity. / Takatsuji, Yoshiyuki; Yamasaki, Ryota; Iwanaga, Atsushi; Lienemann, Michael; Linder, Markus; Haruyama, Tetsuya.

In: Colloids and Surfaces B: Biointerfaces, Vol. 112, 2013, p. 186 - 191.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Solid-support immobilization of a "swing" fusion protein for enhanced glucose oxidase catalytic activity

AU - Takatsuji, Yoshiyuki

AU - Yamasaki, Ryota

AU - Iwanaga, Atsushi

AU - Lienemann, Michael

AU - Linder, Markus

AU - Haruyama, Tetsuya

PY - 2013

Y1 - 2013

N2 - The strategic surface immobilization of a protein can add new functionality to a solid substrate; however, protein activity, e.g., enzymatic activity, can be drastically decreased on immobilization onto a solid surface. The concept of a designed and optimized "molecular interface" is herein introduced in order to address this problem. In this study, molecular interface was designed and constructed with the aim of attaining high enzymatic activity of a solid-surface-immobilized a using the hydrophobin HFBI protein in conjunction with a fusion protein of HFBI attached to glucose oxidase (GOx). The ability of HFBI to form a self-organized membrane on a solid surface in addition to its adhesion properties makes it an ideal candidate for immobilization. The developed fusion protein was also able to form an organized membrane, and its structure and immobilized state on a solid surface were investigated using QCM-D measurements. This method of immobilization showed retention of high enzymatic activity and the ability to control the density of the immobilized enzyme. In this study, we demonstrated the importance of the design and construction of molecular interface for numerous purposes. This method of protein immobilization could be utilized for preparation of high throughput products requiring structurally ordered molecular interfaces, in addition to many other applications.

AB - The strategic surface immobilization of a protein can add new functionality to a solid substrate; however, protein activity, e.g., enzymatic activity, can be drastically decreased on immobilization onto a solid surface. The concept of a designed and optimized "molecular interface" is herein introduced in order to address this problem. In this study, molecular interface was designed and constructed with the aim of attaining high enzymatic activity of a solid-surface-immobilized a using the hydrophobin HFBI protein in conjunction with a fusion protein of HFBI attached to glucose oxidase (GOx). The ability of HFBI to form a self-organized membrane on a solid surface in addition to its adhesion properties makes it an ideal candidate for immobilization. The developed fusion protein was also able to form an organized membrane, and its structure and immobilized state on a solid surface were investigated using QCM-D measurements. This method of immobilization showed retention of high enzymatic activity and the ability to control the density of the immobilized enzyme. In this study, we demonstrated the importance of the design and construction of molecular interface for numerous purposes. This method of protein immobilization could be utilized for preparation of high throughput products requiring structurally ordered molecular interfaces, in addition to many other applications.

KW - glucose oxidase

KW - hydorphobin

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KW - surface functionalization

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