Thermophilic L-fucose isomerase from Thermanaeromonas toyohensis for L-fucose synthesis from L-fuculose

In Jung Kim; Kyoung Heon Kim

doi:10.1016/j.procbio.2020.05.017

Thermophilic L-fucose isomerase from Thermanaeromonas toyohensis for L-fucose synthesis from L-fuculose

In Jung Kim, Kyoung Heon Kim

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

6 Citations (Scopus)

Abstract

The beneficial biological properties of L-fucose have extended its commercial application potential in pharmaceutical, cosmetic, and food industries. Enzymatic production of L-fucose with L-fucose isomerase (L-FucI) is considered a selective, green, and efficient strategy. Efficient sugar production requires thermophilic enzymes with increased reaction rate, reduced risk of microbial contamination, and high sugar solubility. No study has evaluated the applicability of thermophilic L-FucI for L-fucose production. In this study, we explored the biochemical properties of a thermostable L-FucI from Thermanaeromonas toyohensis (TtFucI) using L-fuculose as a substrate. The recombinant TtFucI exhibited thermophilicity and optimum activity at 70 °C. The specific activity, K_m, and k_cat toward L-fuculose were 199.8 U/mg, 33.4 mM, and 901.7 s⁻¹, respectively. Mn²⁺ ions increased the activity of the enzyme by ∼10 times and enhanced its thermal stability. Our study, on L-fucose synthesis by thermostable L-FucI, suggests the potential application of this enzyme for the industrial production of L-fucose.

Original language	English
Pages (from-to)	131-137
Number of pages	7
Journal	Process Biochemistry
Volume	96
DOIs	https://doi.org/10.1016/j.procbio.2020.05.017
Publication status	Published - 2020 Sept

Bibliographical note

Funding Information:
This research was supported by the Mid-career Researcher Program (2020R1A2B5B02002631) and the Basic Research Laboratory Program (2018R1A4A1022589), both funded by the Korean Government (MSIT), through the National Research Foundation (NRF) of Korea. IJK acknowledges grant support from the Research Fellow Program through NRF (2017R1A6A3A11030496). Experiments were performed using the facilities of the Institute of Biomedical Science and Food Safety at the Food Safety Hall, Korea University.

Funding Information:
This research was supported by the Mid-career Researcher Program ( 2020R1A2B5B02002631 ) and the Basic Research Laboratory Program ( 2018R1A4A1022589 ), both funded by the Korean Government (MSIT) , through the National Research Foundation (NRF) of Korea . IJK acknowledges grant support from the Research Fellow Program through NRF ( 2017R1A6A3A11030496 ). Experiments were performed using the facilities of the Institute of Biomedical Science and Food Safety at the Food Safety Hall, Korea University.

Publisher Copyright:
© 2020

Keywords

L-
L-Fucose
L-fucose isomerase
Thermanaeromonas toyohensis
Thermophilic

ASJC Scopus subject areas

Bioengineering
Biochemistry
Applied Microbiology and Biotechnology

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10.1016/j.procbio.2020.05.017

Cite this

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title = "Thermophilic L-fucose isomerase from Thermanaeromonas toyohensis for L-fucose synthesis from L-fuculose",

abstract = "The beneficial biological properties of L-fucose have extended its commercial application potential in pharmaceutical, cosmetic, and food industries. Enzymatic production of L-fucose with L-fucose isomerase (L-FucI) is considered a selective, green, and efficient strategy. Efficient sugar production requires thermophilic enzymes with increased reaction rate, reduced risk of microbial contamination, and high sugar solubility. No study has evaluated the applicability of thermophilic L-FucI for L-fucose production. In this study, we explored the biochemical properties of a thermostable L-FucI from Thermanaeromonas toyohensis (TtFucI) using L-fuculose as a substrate. The recombinant TtFucI exhibited thermophilicity and optimum activity at 70 °C. The specific activity, Km, and kcat toward L-fuculose were 199.8 U/mg, 33.4 mM, and 901.7 s−1, respectively. Mn2+ ions increased the activity of the enzyme by ∼10 times and enhanced its thermal stability. Our study, on L-fucose synthesis by thermostable L-FucI, suggests the potential application of this enzyme for the industrial production of L-fucose.",

keywords = "L-, L-Fucose, L-fucose isomerase, Thermanaeromonas toyohensis, Thermophilic",

author = "Kim, {In Jung} and Kim, {Kyoung Heon}",

note = "Funding Information: This research was supported by the Mid-career Researcher Program (2020R1A2B5B02002631) and the Basic Research Laboratory Program (2018R1A4A1022589), both funded by the Korean Government (MSIT), through the National Research Foundation (NRF) of Korea. IJK acknowledges grant support from the Research Fellow Program through NRF (2017R1A6A3A11030496). Experiments were performed using the facilities of the Institute of Biomedical Science and Food Safety at the Food Safety Hall, Korea University. Funding Information: This research was supported by the Mid-career Researcher Program ( 2020R1A2B5B02002631 ) and the Basic Research Laboratory Program ( 2018R1A4A1022589 ), both funded by the Korean Government (MSIT) , through the National Research Foundation (NRF) of Korea . IJK acknowledges grant support from the Research Fellow Program through NRF ( 2017R1A6A3A11030496 ). Experiments were performed using the facilities of the Institute of Biomedical Science and Food Safety at the Food Safety Hall, Korea University. Publisher Copyright: {\textcopyright} 2020",

year = "2020",

month = sep,

doi = "10.1016/j.procbio.2020.05.017",

language = "English",

volume = "96",

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journal = "Process Biochemistry",

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AU - Kim, In Jung

AU - Kim, Kyoung Heon

N1 - Funding Information: This research was supported by the Mid-career Researcher Program (2020R1A2B5B02002631) and the Basic Research Laboratory Program (2018R1A4A1022589), both funded by the Korean Government (MSIT), through the National Research Foundation (NRF) of Korea. IJK acknowledges grant support from the Research Fellow Program through NRF (2017R1A6A3A11030496). Experiments were performed using the facilities of the Institute of Biomedical Science and Food Safety at the Food Safety Hall, Korea University. Funding Information: This research was supported by the Mid-career Researcher Program ( 2020R1A2B5B02002631 ) and the Basic Research Laboratory Program ( 2018R1A4A1022589 ), both funded by the Korean Government (MSIT) , through the National Research Foundation (NRF) of Korea . IJK acknowledges grant support from the Research Fellow Program through NRF ( 2017R1A6A3A11030496 ). Experiments were performed using the facilities of the Institute of Biomedical Science and Food Safety at the Food Safety Hall, Korea University. Publisher Copyright: © 2020

PY - 2020/9

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N2 - The beneficial biological properties of L-fucose have extended its commercial application potential in pharmaceutical, cosmetic, and food industries. Enzymatic production of L-fucose with L-fucose isomerase (L-FucI) is considered a selective, green, and efficient strategy. Efficient sugar production requires thermophilic enzymes with increased reaction rate, reduced risk of microbial contamination, and high sugar solubility. No study has evaluated the applicability of thermophilic L-FucI for L-fucose production. In this study, we explored the biochemical properties of a thermostable L-FucI from Thermanaeromonas toyohensis (TtFucI) using L-fuculose as a substrate. The recombinant TtFucI exhibited thermophilicity and optimum activity at 70 °C. The specific activity, Km, and kcat toward L-fuculose were 199.8 U/mg, 33.4 mM, and 901.7 s−1, respectively. Mn2+ ions increased the activity of the enzyme by ∼10 times and enhanced its thermal stability. Our study, on L-fucose synthesis by thermostable L-FucI, suggests the potential application of this enzyme for the industrial production of L-fucose.

AB - The beneficial biological properties of L-fucose have extended its commercial application potential in pharmaceutical, cosmetic, and food industries. Enzymatic production of L-fucose with L-fucose isomerase (L-FucI) is considered a selective, green, and efficient strategy. Efficient sugar production requires thermophilic enzymes with increased reaction rate, reduced risk of microbial contamination, and high sugar solubility. No study has evaluated the applicability of thermophilic L-FucI for L-fucose production. In this study, we explored the biochemical properties of a thermostable L-FucI from Thermanaeromonas toyohensis (TtFucI) using L-fuculose as a substrate. The recombinant TtFucI exhibited thermophilicity and optimum activity at 70 °C. The specific activity, Km, and kcat toward L-fuculose were 199.8 U/mg, 33.4 mM, and 901.7 s−1, respectively. Mn2+ ions increased the activity of the enzyme by ∼10 times and enhanced its thermal stability. Our study, on L-fucose synthesis by thermostable L-FucI, suggests the potential application of this enzyme for the industrial production of L-fucose.

KW - L-

KW - L-Fucose

KW - L-fucose isomerase

KW - Thermanaeromonas toyohensis

KW - Thermophilic

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M3 - Article

AN - SCOPUS:85086499933

SN - 1359-5113

VL - 96

SP - 131

EP - 137

JO - Process Biochemistry

JF - Process Biochemistry

ER -

Thermophilic L-fucose isomerase from Thermanaeromonas toyohensis for L-fucose synthesis from L-fuculose

Abstract

Bibliographical note

Keywords

ASJC Scopus subject areas

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