Biochemical characterization of an acid phosphatase from thermus thermophilus

Sy Jye Tham; Ching Dong Chang; Hao Jen Huang; Yueh Feng Lee; Tze Sing Huang; Ching Chun Chang

doi:10.1271/bbb.90773

Biochemical characterization of an acid phosphatase from thermus thermophilus

Sy Jye Tham, Ching Dong Chang, Hao Jen Huang, Yueh Feng Lee, Tze Sing Huang, Ching Chun Chang

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

17 Citations (Scopus)

Abstract

A recombinant putative acid phosphatase from Thermus thermophilus was expressed and purified from Escherichia coli. The recombinant phosphatase displayed activities in a broad range of temperature, from 40 to 90 °C, with optimal temperature at 70 °C. In addition, the recombinant enzyme had activities in a wide range of pH, from 3.6 to 9.1, with optimal pH at 6 in acetate buffer and with optimal pH at 6.5 in Hepes buffer. Furthermore, it showed significant thermal stability and still possessed 44% residual activity after 70 °C treatment for 15 min. Moreover, the recombinant phosphatase showed broad substrates specificities for monophosphate esters, p-nitrophenyl phosphate (pNPP) being the most preferred substrate, and it was able to resist inhibition by sodium tartrate. Additionally, the recombinant protein formed stable oligomer under partially denatured conditions and required calcium ions for enzymic activity.

Original language	English
Pages (from-to)	727-735
Number of pages	9
Journal	Bioscience, Biotechnology and Biochemistry
Volume	74
Issue number	4
DOIs	https://doi.org/10.1271/bbb.90773
Publication status	Published - 2010

All Science Journal Classification (ASJC) codes

Biotechnology
Analytical Chemistry
Biochemistry
Applied Microbiology and Biotechnology
Molecular Biology
Organic Chemistry

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10.1271/bbb.90773

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@article{38822a86f8db484fa7af4911e07fecba,

title = "Biochemical characterization of an acid phosphatase from thermus thermophilus",

abstract = "A recombinant putative acid phosphatase from Thermus thermophilus was expressed and purified from Escherichia coli. The recombinant phosphatase displayed activities in a broad range of temperature, from 40 to 90 °C, with optimal temperature at 70 °C. In addition, the recombinant enzyme had activities in a wide range of pH, from 3.6 to 9.1, with optimal pH at 6 in acetate buffer and with optimal pH at 6.5 in Hepes buffer. Furthermore, it showed significant thermal stability and still possessed 44% residual activity after 70 °C treatment for 15 min. Moreover, the recombinant phosphatase showed broad substrates specificities for monophosphate esters, p-nitrophenyl phosphate (pNPP) being the most preferred substrate, and it was able to resist inhibition by sodium tartrate. Additionally, the recombinant protein formed stable oligomer under partially denatured conditions and required calcium ions for enzymic activity.",

author = "Tham, {Sy Jye} and Chang, {Ching Dong} and Huang, {Hao Jen} and Lee, {Yueh Feng} and Huang, {Tze Sing} and Chang, {Ching Chun}",

note = "Funding Information: We thank Mr. Pin-Sheng Huang and Mr. Cheng-Shun Tsai for technical assistance. This work was financially supported in part by a grant (NSC96-2313-B-006-003-MY3) from the National Science Council of Taiwan to C.-C. Chang.",

year = "2010",

doi = "10.1271/bbb.90773",

language = "English",

volume = "74",

pages = "727--735",

journal = "Bioscience, Biotechnology and Biochemistry",

issn = "0916-8451",

publisher = "Japan Society for Bioscience Biotechnology and Agrochemistry",

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T1 - Biochemical characterization of an acid phosphatase from thermus thermophilus

AU - Tham, Sy Jye

AU - Chang, Ching Dong

AU - Huang, Hao Jen

AU - Lee, Yueh Feng

AU - Huang, Tze Sing

AU - Chang, Ching Chun

N1 - Funding Information: We thank Mr. Pin-Sheng Huang and Mr. Cheng-Shun Tsai for technical assistance. This work was financially supported in part by a grant (NSC96-2313-B-006-003-MY3) from the National Science Council of Taiwan to C.-C. Chang.

PY - 2010

Y1 - 2010

N2 - A recombinant putative acid phosphatase from Thermus thermophilus was expressed and purified from Escherichia coli. The recombinant phosphatase displayed activities in a broad range of temperature, from 40 to 90 °C, with optimal temperature at 70 °C. In addition, the recombinant enzyme had activities in a wide range of pH, from 3.6 to 9.1, with optimal pH at 6 in acetate buffer and with optimal pH at 6.5 in Hepes buffer. Furthermore, it showed significant thermal stability and still possessed 44% residual activity after 70 °C treatment for 15 min. Moreover, the recombinant phosphatase showed broad substrates specificities for monophosphate esters, p-nitrophenyl phosphate (pNPP) being the most preferred substrate, and it was able to resist inhibition by sodium tartrate. Additionally, the recombinant protein formed stable oligomer under partially denatured conditions and required calcium ions for enzymic activity.

AB - A recombinant putative acid phosphatase from Thermus thermophilus was expressed and purified from Escherichia coli. The recombinant phosphatase displayed activities in a broad range of temperature, from 40 to 90 °C, with optimal temperature at 70 °C. In addition, the recombinant enzyme had activities in a wide range of pH, from 3.6 to 9.1, with optimal pH at 6 in acetate buffer and with optimal pH at 6.5 in Hepes buffer. Furthermore, it showed significant thermal stability and still possessed 44% residual activity after 70 °C treatment for 15 min. Moreover, the recombinant phosphatase showed broad substrates specificities for monophosphate esters, p-nitrophenyl phosphate (pNPP) being the most preferred substrate, and it was able to resist inhibition by sodium tartrate. Additionally, the recombinant protein formed stable oligomer under partially denatured conditions and required calcium ions for enzymic activity.

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JO - Bioscience, Biotechnology and Biochemistry

JF - Bioscience, Biotechnology and Biochemistry

IS - 4

ER -

Biochemical characterization of an acid phosphatase from thermus thermophilus

Abstract

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