Stabilized glycerol dehydrogenase for the conversion of glycerol to dihydroxyacetone

Gudi Satheesh Kumar; Youngho Wee; Inseon Lee; Ho Jin Sun; Xueyan Zhao; Shunxiang Xia; Seongbeen Kim; Jinwoo Lee; Ping Wang; Jungbae Kim

doi:10.1016/j.cej.2015.04.039

Stabilized glycerol dehydrogenase for the conversion of glycerol to dihydroxyacetone

Gudi Satheesh Kumar, Youngho Wee, Inseon Lee, Ho Jin Sun, Xueyan Zhao, Shunxiang Xia, Seongbeen Kim, Jinwoo Lee, Ping Wang, Jungbae Kim

Department of Chemical and Biological Engineering

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

32 Citations (Scopus)

Abstract

The biodiesel industry generates glycerol as a main by-product, and the conversion of glycerol to value-added products is an important issue. Glycerol dehydrogenase (GDH) can catalyze the conversion of glycerol to dihydroxyacetone (DHA), which is used as a tanning agent in cosmetics and is much more expensive than glycerol. In this study, GDH was adsorbed into magnetically-separable mesoporous silica with 38. nm mesocellular pores connected via 18. nm window mesopores (adsorbed GDH, called ADS), and further crosslinked via a simple glutaraldehyde treatment to prepare nanoscale enzyme reactors of GDH (NERs of GDH, called NER). When the stabilities of free and immobilized GDH were monitored in an aqueous buffer under shaking (200. rpm), the residual activities of the free GDH and ADS could no longer be detected after 8. days and 22. days, respectively, while the NER maintained 64% of its initial activity even after 24-day incubation. The time-dependent conversion of glycerol to DHA was measured for both ADS and NER not only by analyzing the generation of NADH spectrophotometrically (340. nm) but also via the HPLC analysis measuring the increase of the DHA peak. Magnetically-separable NER maintained 39% of its initial activity after seven cycles of repeated use, while the residual activity of ADS dropped to 13% of its initial activity after only two recycled uses.

Original language	English
Pages (from-to)	283-288
Number of pages	6
Journal	Chemical Engineering Journal
Volume	276
DOIs	https://doi.org/10.1016/j.cej.2015.04.039
Publication status	Published - 2015 Sept 5

Bibliographical note

Funding Information:
This work was supported by the ‘ International Collaborative R&D Program ’ (No. 20118510020020 ) and ‘ Energy Efficiency & Resources Core Technology Program ’ (No. 20142020200980 ) of the Korea Institute of Energy Technology Evaluation and Planning (KETEP) grants, funded by the Korea government Ministry of Trade, Industry & Energy . This work was also supported by the Global Research Laboratory Program ( 2014K1A1A2043032 ), by the Nano Material Technology Development Program ( 2014M3A7B4052193 ), and by the ‘ 2015, University-Institute Cooperation Program ’, all of which are funded by the Korea government Ministry of Science, ICT & Future Planning . This work was also supported by a Korea University Grant.

Publisher Copyright:
© 2015 Elsevier B.V.

Keywords

Dihydroxyacetone
Enzyme immobilization and stabilization
Glycerol
Glycerol dehydrogenase
Magnetic separation
Nanoscale enzyme reactors

ASJC Scopus subject areas

Chemistry(all)
Environmental Chemistry
Chemical Engineering(all)
Industrial and Manufacturing Engineering

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10.1016/j.cej.2015.04.039

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title = "Stabilized glycerol dehydrogenase for the conversion of glycerol to dihydroxyacetone",

abstract = "The biodiesel industry generates glycerol as a main by-product, and the conversion of glycerol to value-added products is an important issue. Glycerol dehydrogenase (GDH) can catalyze the conversion of glycerol to dihydroxyacetone (DHA), which is used as a tanning agent in cosmetics and is much more expensive than glycerol. In this study, GDH was adsorbed into magnetically-separable mesoporous silica with 38. nm mesocellular pores connected via 18. nm window mesopores (adsorbed GDH, called ADS), and further crosslinked via a simple glutaraldehyde treatment to prepare nanoscale enzyme reactors of GDH (NERs of GDH, called NER). When the stabilities of free and immobilized GDH were monitored in an aqueous buffer under shaking (200. rpm), the residual activities of the free GDH and ADS could no longer be detected after 8. days and 22. days, respectively, while the NER maintained 64% of its initial activity even after 24-day incubation. The time-dependent conversion of glycerol to DHA was measured for both ADS and NER not only by analyzing the generation of NADH spectrophotometrically (340. nm) but also via the HPLC analysis measuring the increase of the DHA peak. Magnetically-separable NER maintained 39% of its initial activity after seven cycles of repeated use, while the residual activity of ADS dropped to 13% of its initial activity after only two recycled uses.",

keywords = "Dihydroxyacetone, Enzyme immobilization and stabilization, Glycerol, Glycerol dehydrogenase, Magnetic separation, Nanoscale enzyme reactors",

author = "Kumar, {Gudi Satheesh} and Youngho Wee and Inseon Lee and Sun, {Ho Jin} and Xueyan Zhao and Shunxiang Xia and Seongbeen Kim and Jinwoo Lee and Ping Wang and Jungbae Kim",

note = "Funding Information: This work was supported by the {\textquoteleft} International Collaborative R&D Program {\textquoteright} (No. 20118510020020 ) and {\textquoteleft} Energy Efficiency & Resources Core Technology Program {\textquoteright} (No. 20142020200980 ) of the Korea Institute of Energy Technology Evaluation and Planning (KETEP) grants, funded by the Korea government Ministry of Trade, Industry & Energy . This work was also supported by the Global Research Laboratory Program ( 2014K1A1A2043032 ), by the Nano Material Technology Development Program ( 2014M3A7B4052193 ), and by the {\textquoteleft} 2015, University-Institute Cooperation Program {\textquoteright}, all of which are funded by the Korea government Ministry of Science, ICT & Future Planning . This work was also supported by a Korea University Grant. Publisher Copyright: {\textcopyright} 2015 Elsevier B.V.",

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doi = "10.1016/j.cej.2015.04.039",

language = "English",

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pages = "283--288",

journal = "Chemical Engineering Journal",

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T1 - Stabilized glycerol dehydrogenase for the conversion of glycerol to dihydroxyacetone

AU - Kumar, Gudi Satheesh

AU - Wee, Youngho

AU - Lee, Inseon

AU - Sun, Ho Jin

AU - Zhao, Xueyan

AU - Xia, Shunxiang

AU - Kim, Seongbeen

AU - Lee, Jinwoo

AU - Wang, Ping

AU - Kim, Jungbae

N1 - Funding Information: This work was supported by the ‘ International Collaborative R&D Program ’ (No. 20118510020020 ) and ‘ Energy Efficiency & Resources Core Technology Program ’ (No. 20142020200980 ) of the Korea Institute of Energy Technology Evaluation and Planning (KETEP) grants, funded by the Korea government Ministry of Trade, Industry & Energy . This work was also supported by the Global Research Laboratory Program ( 2014K1A1A2043032 ), by the Nano Material Technology Development Program ( 2014M3A7B4052193 ), and by the ‘ 2015, University-Institute Cooperation Program ’, all of which are funded by the Korea government Ministry of Science, ICT & Future Planning . This work was also supported by a Korea University Grant. Publisher Copyright: © 2015 Elsevier B.V.

PY - 2015/9/5

Y1 - 2015/9/5

N2 - The biodiesel industry generates glycerol as a main by-product, and the conversion of glycerol to value-added products is an important issue. Glycerol dehydrogenase (GDH) can catalyze the conversion of glycerol to dihydroxyacetone (DHA), which is used as a tanning agent in cosmetics and is much more expensive than glycerol. In this study, GDH was adsorbed into magnetically-separable mesoporous silica with 38. nm mesocellular pores connected via 18. nm window mesopores (adsorbed GDH, called ADS), and further crosslinked via a simple glutaraldehyde treatment to prepare nanoscale enzyme reactors of GDH (NERs of GDH, called NER). When the stabilities of free and immobilized GDH were monitored in an aqueous buffer under shaking (200. rpm), the residual activities of the free GDH and ADS could no longer be detected after 8. days and 22. days, respectively, while the NER maintained 64% of its initial activity even after 24-day incubation. The time-dependent conversion of glycerol to DHA was measured for both ADS and NER not only by analyzing the generation of NADH spectrophotometrically (340. nm) but also via the HPLC analysis measuring the increase of the DHA peak. Magnetically-separable NER maintained 39% of its initial activity after seven cycles of repeated use, while the residual activity of ADS dropped to 13% of its initial activity after only two recycled uses.

AB - The biodiesel industry generates glycerol as a main by-product, and the conversion of glycerol to value-added products is an important issue. Glycerol dehydrogenase (GDH) can catalyze the conversion of glycerol to dihydroxyacetone (DHA), which is used as a tanning agent in cosmetics and is much more expensive than glycerol. In this study, GDH was adsorbed into magnetically-separable mesoporous silica with 38. nm mesocellular pores connected via 18. nm window mesopores (adsorbed GDH, called ADS), and further crosslinked via a simple glutaraldehyde treatment to prepare nanoscale enzyme reactors of GDH (NERs of GDH, called NER). When the stabilities of free and immobilized GDH were monitored in an aqueous buffer under shaking (200. rpm), the residual activities of the free GDH and ADS could no longer be detected after 8. days and 22. days, respectively, while the NER maintained 64% of its initial activity even after 24-day incubation. The time-dependent conversion of glycerol to DHA was measured for both ADS and NER not only by analyzing the generation of NADH spectrophotometrically (340. nm) but also via the HPLC analysis measuring the increase of the DHA peak. Magnetically-separable NER maintained 39% of its initial activity after seven cycles of repeated use, while the residual activity of ADS dropped to 13% of its initial activity after only two recycled uses.

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KW - Enzyme immobilization and stabilization

KW - Glycerol

KW - Glycerol dehydrogenase

KW - Magnetic separation

KW - Nanoscale enzyme reactors

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ER -

Stabilized glycerol dehydrogenase for the conversion of glycerol to dihydroxyacetone

Abstract

Bibliographical note

Keywords

ASJC Scopus subject areas

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