Heterologous Expression of Thermogutta terrifontis Endo-Xanthanase in Penicillium verruculosum, Isolation and Primary Characterization of the Enzyme

Yury A. Denisenko; Olga G. Korotkova; Ivan N. Zorov; Alexandra M. Rozhkova; Margarita V. Semenova; Alexandr G. Elcheninov; Ilya V. Kublanov; Arkady P. Sinitsyn

doi:10.1134/s000629792104009x

Heterologous Expression of Thermogutta terrifontis Endo-Xanthanase in Penicillium verruculosum, Isolation and Primary Characterization of the Enzyme

Yury A. Denisenko^*, Olga G. Korotkova, Ivan N. Zorov, Alexandra M. Rozhkova, Margarita V. Semenova, Alexandr G. Elcheninov, Ilya V. Kublanov, Arkady P. Sinitsyn

^*Corresponding author for this work

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

5 Scopus citations

Abstract

Abstract: Heterologous endo-xanthanase (EX) from the thermophilic planktomycete Thermogutta terrifontis strain was obtained using Penicillium verruculosum 537 (ΔniaD) expression system with the cellobiohydrolase 1 gene promoter. Homogeneous EX with a molecular weight of 23.7 kDa (pI 6.5) was isolated using liquid chromatography methods. This xanthan degrading enzyme also possesses the enzymatic activity towards CM-cellulose, β-glucan, curdlan, lichenan, laminarin, galactomannan, xyloglucan but not towards p-nitrophenyl derivatives of β-D-glucose, mannose and cellobiose. The temperature and pH optima of EX were 55°C and 4.0, respectively; the enzyme exhibited 90% of its maximum activity in the temperature range 50-60°C and pH 3-5.

Original language	English
Pages (from-to)	489-495
Number of pages	7
Journal	Biochemistry (Moscow)
Volume	86
Issue number	4
DOIs	https://doi.org/10.1134/s000629792104009x
State	Published - Apr 2021
Externally published	Yes

Bibliographical note

Publisher Copyright:
© 2021, Pleiades Publishing, Ltd.

Keywords

Penicillium verruculosum
Thermogutta terrifontis
endo-xanthanase
heterologous expression
xanthan destruction

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10.1134/s000629792104009x

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Denisenko, Y. A., Korotkova, O. G., Zorov, I. N., Rozhkova, A. M., Semenova, M. V., Elcheninov, A. G., Kublanov, I. V., & Sinitsyn, A. P. (2021). Heterologous Expression of Thermogutta terrifontis Endo-Xanthanase in Penicillium verruculosum, Isolation and Primary Characterization of the Enzyme. Biochemistry (Moscow), 86(4), 489-495. https://doi.org/10.1134/s000629792104009x

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title = "Heterologous Expression of Thermogutta terrifontis Endo-Xanthanase in Penicillium verruculosum, Isolation and Primary Characterization of the Enzyme",

abstract = "Abstract: Heterologous endo-xanthanase (EX) from the thermophilic planktomycete Thermogutta terrifontis strain was obtained using Penicillium verruculosum 537 (ΔniaD) expression system with the cellobiohydrolase 1 gene promoter. Homogeneous EX with a molecular weight of 23.7 kDa (pI 6.5) was isolated using liquid chromatography methods. This xanthan degrading enzyme also possesses the enzymatic activity towards CM-cellulose, β-glucan, curdlan, lichenan, laminarin, galactomannan, xyloglucan but not towards p-nitrophenyl derivatives of β-D-glucose, mannose and cellobiose. The temperature and pH optima of EX were 55°C and 4.0, respectively; the enzyme exhibited 90% of its maximum activity in the temperature range 50-60°C and pH 3-5.",

keywords = "Penicillium verruculosum, Thermogutta terrifontis, endo-xanthanase, heterologous expression, xanthan destruction",

author = "Denisenko, {Yury A.} and Korotkova, {Olga G.} and Zorov, {Ivan N.} and Rozhkova, {Alexandra M.} and Semenova, {Margarita V.} and Elcheninov, {Alexandr G.} and Kublanov, {Ilya V.} and Sinitsyn, {Arkady P.}",

note = "Publisher Copyright: {\textcopyright} 2021, Pleiades Publishing, Ltd.",

year = "2021",

month = apr,

doi = "10.1134/s000629792104009x",

language = "אנגלית",

volume = "86",

pages = "489--495",

journal = "Biochemistry (Moscow)",

issn = "0006-2979",

publisher = "Pleiades Publishing",

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T1 - Heterologous Expression of Thermogutta terrifontis Endo-Xanthanase in Penicillium verruculosum, Isolation and Primary Characterization of the Enzyme

AU - Denisenko, Yury A.

AU - Korotkova, Olga G.

AU - Zorov, Ivan N.

AU - Rozhkova, Alexandra M.

AU - Semenova, Margarita V.

AU - Elcheninov, Alexandr G.

AU - Kublanov, Ilya V.

AU - Sinitsyn, Arkady P.

PY - 2021/4

Y1 - 2021/4

N2 - Abstract: Heterologous endo-xanthanase (EX) from the thermophilic planktomycete Thermogutta terrifontis strain was obtained using Penicillium verruculosum 537 (ΔniaD) expression system with the cellobiohydrolase 1 gene promoter. Homogeneous EX with a molecular weight of 23.7 kDa (pI 6.5) was isolated using liquid chromatography methods. This xanthan degrading enzyme also possesses the enzymatic activity towards CM-cellulose, β-glucan, curdlan, lichenan, laminarin, galactomannan, xyloglucan but not towards p-nitrophenyl derivatives of β-D-glucose, mannose and cellobiose. The temperature and pH optima of EX were 55°C and 4.0, respectively; the enzyme exhibited 90% of its maximum activity in the temperature range 50-60°C and pH 3-5.

AB - Abstract: Heterologous endo-xanthanase (EX) from the thermophilic planktomycete Thermogutta terrifontis strain was obtained using Penicillium verruculosum 537 (ΔniaD) expression system with the cellobiohydrolase 1 gene promoter. Homogeneous EX with a molecular weight of 23.7 kDa (pI 6.5) was isolated using liquid chromatography methods. This xanthan degrading enzyme also possesses the enzymatic activity towards CM-cellulose, β-glucan, curdlan, lichenan, laminarin, galactomannan, xyloglucan but not towards p-nitrophenyl derivatives of β-D-glucose, mannose and cellobiose. The temperature and pH optima of EX were 55°C and 4.0, respectively; the enzyme exhibited 90% of its maximum activity in the temperature range 50-60°C and pH 3-5.

KW - Penicillium verruculosum

KW - Thermogutta terrifontis

KW - endo-xanthanase

KW - heterologous expression

KW - xanthan destruction

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SN - 0006-2979

VL - 86

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EP - 495

JO - Biochemistry (Moscow)

JF - Biochemistry (Moscow)

IS - 4

ER -

Heterologous Expression of Thermogutta terrifontis Endo-Xanthanase in Penicillium verruculosum, Isolation and Primary Characterization of the Enzyme

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