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

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

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

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
State	Published - Apr 2021
Externally published	Yes

Keywords

Penicillium verruculosum
Thermogutta terrifontis
endo-xanthanase
heterologous expression
xanthan destruction

All Science Journal Classification (ASJC) codes

Biochemistry

Cite this

@article{03c8864af15246b5aa2efec32aca025c,

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,

language = "الإنجليزيّة",

volume = "86",

pages = "489--495",

journal = "Biochemistry (Moscow)",

issn = "0006-2979",

publisher = "Pleiades Publishing",

number = "4",

}

TY - JOUR

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

UR - http://www.scopus.com/inward/record.url?scp=85104139167&partnerID=8YFLogxK

M3 - مقالة

C2 - 33941069

SN - 0006-2979

VL - 86

SP - 489

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

Abstract

Keywords

All Science Journal Classification (ASJC) codes

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