Properties of L-arabinose isomerase from Escherichia coli as biocatalyst for tagatose production

Sang Hyun Yoon; Pil Kim; Deok Kun Oh

doi:10.1023/A:1022575601492

Properties of L-arabinose isomerase from Escherichia coli as biocatalyst for tagatose production

Sang Hyun Yoon
, Pil Kim
, Deok Kun Oh

Dept. of Biotechnology

Tong-Yang Confectionery Co.
Sejong University

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

58 Scopus citations

Abstract

L-arabinose isomerase (EC 5.3.1.4) mediates the isomerization of D-galactose into D-tagatose as well as the conversion of L-arabinose into L-ribulose. To investigate the properties of L-arabinose isomerase as a biocatalyst for the conversion of galactose to tagatose, the L-arabinose isomerase of Escherichia coli was characterized. The substrate specificity for L-arabinose was 166-fold higher than that for D-galactose. The optimal pH and temperature for the galactose isomerization reaction were 8.0 and 30°C, respectively. The enzyme activity was stable for 1 h at temperatures below 35°C and within a pH range of 8-10. The Michaelis constant, K_m, for galactose was 1480 mM, which is 25-fold higher than that for arabinose. The addition of Fe²⁺ and Mn²⁺ ions enhanced the conversion of galactose to tagatose, whereas the addition of Cu²⁺, Zn²⁺, Hg²⁺, and Fe³⁺ ions inhibited the reaction completely. In the presence of 1 mM Fe²⁺ ions, the K_m for galactose was found to be 300 mM.

Original language	English
Pages (from-to)	47-51
Number of pages	5
Journal	World Journal of Microbiology and Biotechnology
Volume	19
Issue number	1
DOIs	https://doi.org/10.1023/A:1022575601492
State	Published - Feb 2003

Bibliographical note

Funding Information:
This work was part of a National Research Project and funded by the Ministry of Health and Welfare, Korea (grant no. HMP-00-PT-22000-0034).

Keywords

Enzyme properties
Escherichia coli
Galactose
L-arabinose isomerase
Tagatose

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title = "Properties of L-arabinose isomerase from Escherichia coli as biocatalyst for tagatose production",

abstract = "L-arabinose isomerase (EC 5.3.1.4) mediates the isomerization of D-galactose into D-tagatose as well as the conversion of L-arabinose into L-ribulose. To investigate the properties of L-arabinose isomerase as a biocatalyst for the conversion of galactose to tagatose, the L-arabinose isomerase of Escherichia coli was characterized. The substrate specificity for L-arabinose was 166-fold higher than that for D-galactose. The optimal pH and temperature for the galactose isomerization reaction were 8.0 and 30°C, respectively. The enzyme activity was stable for 1 h at temperatures below 35°C and within a pH range of 8-10. The Michaelis constant, Km, for galactose was 1480 mM, which is 25-fold higher than that for arabinose. The addition of Fe2+ and Mn2+ ions enhanced the conversion of galactose to tagatose, whereas the addition of Cu2+, Zn2+, Hg2+, and Fe3+ ions inhibited the reaction completely. In the presence of 1 mM Fe2+ ions, the Km for galactose was found to be 300 mM.",

keywords = "Enzyme properties, Escherichia coli, Galactose, L-arabinose isomerase, Tagatose",

author = "Yoon, \{Sang Hyun\} and Pil Kim and Oh, \{Deok Kun\}",

note = "Funding Information: This work was part of a National Research Project and funded by the Ministry of Health and Welfare, Korea (grant no. HMP-00-PT-22000-0034).",

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AU - Yoon, Sang Hyun

AU - Kim, Pil

AU - Oh, Deok Kun

N1 - Funding Information: This work was part of a National Research Project and funded by the Ministry of Health and Welfare, Korea (grant no. HMP-00-PT-22000-0034).

PY - 2003/2

Y1 - 2003/2

N2 - L-arabinose isomerase (EC 5.3.1.4) mediates the isomerization of D-galactose into D-tagatose as well as the conversion of L-arabinose into L-ribulose. To investigate the properties of L-arabinose isomerase as a biocatalyst for the conversion of galactose to tagatose, the L-arabinose isomerase of Escherichia coli was characterized. The substrate specificity for L-arabinose was 166-fold higher than that for D-galactose. The optimal pH and temperature for the galactose isomerization reaction were 8.0 and 30°C, respectively. The enzyme activity was stable for 1 h at temperatures below 35°C and within a pH range of 8-10. The Michaelis constant, Km, for galactose was 1480 mM, which is 25-fold higher than that for arabinose. The addition of Fe2+ and Mn2+ ions enhanced the conversion of galactose to tagatose, whereas the addition of Cu2+, Zn2+, Hg2+, and Fe3+ ions inhibited the reaction completely. In the presence of 1 mM Fe2+ ions, the Km for galactose was found to be 300 mM.

AB - L-arabinose isomerase (EC 5.3.1.4) mediates the isomerization of D-galactose into D-tagatose as well as the conversion of L-arabinose into L-ribulose. To investigate the properties of L-arabinose isomerase as a biocatalyst for the conversion of galactose to tagatose, the L-arabinose isomerase of Escherichia coli was characterized. The substrate specificity for L-arabinose was 166-fold higher than that for D-galactose. The optimal pH and temperature for the galactose isomerization reaction were 8.0 and 30°C, respectively. The enzyme activity was stable for 1 h at temperatures below 35°C and within a pH range of 8-10. The Michaelis constant, Km, for galactose was 1480 mM, which is 25-fold higher than that for arabinose. The addition of Fe2+ and Mn2+ ions enhanced the conversion of galactose to tagatose, whereas the addition of Cu2+, Zn2+, Hg2+, and Fe3+ ions inhibited the reaction completely. In the presence of 1 mM Fe2+ ions, the Km for galactose was found to be 300 mM.

KW - Enzyme properties

KW - Escherichia coli

KW - Galactose

KW - L-arabinose isomerase

KW - Tagatose

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DO - 10.1023/A:1022575601492

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Properties of L-arabinose isomerase from Escherichia coli as biocatalyst for tagatose production

Abstract

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Keywords

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