Protein-inorganic hybrid system for efficient his-tagged enzymes immobilization and its application in l-xylulose production

Sanjay K.S. Patel; Sachin V. Otari; Yun Chan Kang; Jung Kul Lee

doi:10.1039/c6ra24404a

Protein-inorganic hybrid system for efficient his-tagged enzymes immobilization and its application in l-xylulose production

Sanjay K.S. Patel, Sachin V. Otari, Yun Chan Kang, Jung Kul Lee

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

94 Citations (Scopus)

Abstract

The facile synthesis of protein-inorganic hybrid nanoflowers was evaluated for the efficient immobilization of recombinant his-tagged enzymes, which have a broad range of potential applications. In this study, we report the preparation of a metal-protein hybrid nanoflower system for efficient immobilization of the recombinant enzymes l-arabinitol 4-dehydrogenase from Hypocrea jecorina (HjLAD) and NADH oxidase from Streptococcus pyogenes (SpNox). Compared with free enzymes, synthesized hybrid nanoflowers exhibited enhanced enzymatic activities of 246 and 144% for HjLAD and SpNox, respectively. We have demonstrated that immobilized enzymes retained high catalytic activity and improved the tolerance towards pH and temperature changes. Synthesized nanoflowers also retained high storage stability and reusability. In addition, the immobilized enzymes exhibited significantly enhanced l-xylulose production under co-factor regeneration conditions than the free enzyme combination. These results demonstrate that variations in the concentration of metals and synthesis conditions of nanoflowers can be extended to efficiently immobilize recombinant his-tagged enzymes.

Original language	English
Pages (from-to)	3488-3494
Number of pages	7
Journal	RSC Advances
Volume	7
Issue number	6
DOIs	https://doi.org/10.1039/c6ra24404a
Publication status	Published - 2017

Bibliographical note

Funding Information:
This work was supported by the Energy Efficiency & Resources Core Technology Program of the Korea Institute of Energy Technology Evaluation and Planning (KETEP), granted financial resource from the Ministry of Trade, Industry & Energy, Republic of Korea (20153030091450). This research was also supported by a grant from the Intelligent Synthetic Biology Center of Global Frontier Project (2013M3A6A8073184) funded by the Ministry of Science, ICT and Future Planning, Republic of Korea. This research was supported by the 2015 KU Brain Pool of Konkuk University.

Publisher Copyright:
© The Royal Society of Chemistry.

ASJC Scopus subject areas

General Chemistry
General Chemical Engineering

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title = "Protein-inorganic hybrid system for efficient his-tagged enzymes immobilization and its application in l-xylulose production",

abstract = "The facile synthesis of protein-inorganic hybrid nanoflowers was evaluated for the efficient immobilization of recombinant his-tagged enzymes, which have a broad range of potential applications. In this study, we report the preparation of a metal-protein hybrid nanoflower system for efficient immobilization of the recombinant enzymes l-arabinitol 4-dehydrogenase from Hypocrea jecorina (HjLAD) and NADH oxidase from Streptococcus pyogenes (SpNox). Compared with free enzymes, synthesized hybrid nanoflowers exhibited enhanced enzymatic activities of 246 and 144% for HjLAD and SpNox, respectively. We have demonstrated that immobilized enzymes retained high catalytic activity and improved the tolerance towards pH and temperature changes. Synthesized nanoflowers also retained high storage stability and reusability. In addition, the immobilized enzymes exhibited significantly enhanced l-xylulose production under co-factor regeneration conditions than the free enzyme combination. These results demonstrate that variations in the concentration of metals and synthesis conditions of nanoflowers can be extended to efficiently immobilize recombinant his-tagged enzymes.",

author = "Patel, {Sanjay K.S.} and Otari, {Sachin V.} and {Chan Kang}, Yun and Lee, {Jung Kul}",

note = "Funding Information: This work was supported by the Energy Efficiency & Resources Core Technology Program of the Korea Institute of Energy Technology Evaluation and Planning (KETEP), granted financial resource from the Ministry of Trade, Industry & Energy, Republic of Korea (20153030091450). This research was also supported by a grant from the Intelligent Synthetic Biology Center of Global Frontier Project (2013M3A6A8073184) funded by the Ministry of Science, ICT and Future Planning, Republic of Korea. This research was supported by the 2015 KU Brain Pool of Konkuk University. Publisher Copyright: {\textcopyright} The Royal Society of Chemistry.",

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AU - Lee, Jung Kul

N1 - Funding Information: This work was supported by the Energy Efficiency & Resources Core Technology Program of the Korea Institute of Energy Technology Evaluation and Planning (KETEP), granted financial resource from the Ministry of Trade, Industry & Energy, Republic of Korea (20153030091450). This research was also supported by a grant from the Intelligent Synthetic Biology Center of Global Frontier Project (2013M3A6A8073184) funded by the Ministry of Science, ICT and Future Planning, Republic of Korea. This research was supported by the 2015 KU Brain Pool of Konkuk University. Publisher Copyright: © The Royal Society of Chemistry.

PY - 2017

Y1 - 2017

N2 - The facile synthesis of protein-inorganic hybrid nanoflowers was evaluated for the efficient immobilization of recombinant his-tagged enzymes, which have a broad range of potential applications. In this study, we report the preparation of a metal-protein hybrid nanoflower system for efficient immobilization of the recombinant enzymes l-arabinitol 4-dehydrogenase from Hypocrea jecorina (HjLAD) and NADH oxidase from Streptococcus pyogenes (SpNox). Compared with free enzymes, synthesized hybrid nanoflowers exhibited enhanced enzymatic activities of 246 and 144% for HjLAD and SpNox, respectively. We have demonstrated that immobilized enzymes retained high catalytic activity and improved the tolerance towards pH and temperature changes. Synthesized nanoflowers also retained high storage stability and reusability. In addition, the immobilized enzymes exhibited significantly enhanced l-xylulose production under co-factor regeneration conditions than the free enzyme combination. These results demonstrate that variations in the concentration of metals and synthesis conditions of nanoflowers can be extended to efficiently immobilize recombinant his-tagged enzymes.

AB - The facile synthesis of protein-inorganic hybrid nanoflowers was evaluated for the efficient immobilization of recombinant his-tagged enzymes, which have a broad range of potential applications. In this study, we report the preparation of a metal-protein hybrid nanoflower system for efficient immobilization of the recombinant enzymes l-arabinitol 4-dehydrogenase from Hypocrea jecorina (HjLAD) and NADH oxidase from Streptococcus pyogenes (SpNox). Compared with free enzymes, synthesized hybrid nanoflowers exhibited enhanced enzymatic activities of 246 and 144% for HjLAD and SpNox, respectively. We have demonstrated that immobilized enzymes retained high catalytic activity and improved the tolerance towards pH and temperature changes. Synthesized nanoflowers also retained high storage stability and reusability. In addition, the immobilized enzymes exhibited significantly enhanced l-xylulose production under co-factor regeneration conditions than the free enzyme combination. These results demonstrate that variations in the concentration of metals and synthesis conditions of nanoflowers can be extended to efficiently immobilize recombinant his-tagged enzymes.

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Protein-inorganic hybrid system for efficient his-tagged enzymes immobilization and its application in l-xylulose production

Abstract

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