Discovery and characterization of a novel Dyp-type peroxidase from a marine actinobacterium isolated from Trondheim fjord, Norway

Cristina M. Cordas; Giang Son Nguyen; Gabriel N. Valério; Malene Jønsson; Katharina Söllner; Ingvild H. Aune; Alexander Wentzel; José J. G. Moura

doi:10.1016/j.jinorgbio.2021.111651

Discovery and characterization of a novel Dyp-type peroxidase from a marine actinobacterium isolated from Trondheim fjord, Norway

Cristina M. Cordas, Giang Son Nguyen, Gabriel N. Valério, Malene Jønsson, Katharina Söllner, Ingvild H. Aune, Alexander Wentzel, José J. G. Moura

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

13 Citations (Scopus)

Abstract

A new dye-decolorizing peroxidase (DyP) was discovered through a data mining workflow based on HMMER software and profile Hidden Markov Model (HMM) using a dataset of 1200 genomes originated from a Actinobacteria strain collection isolated from Trondheim fjord. Instead of the conserved GXXDG motif known for Dyp-type peroxidases, the enzyme contains a new conserved motif EXXDG which has been not reported before. The enzyme can oxidize an anthraquinone dye Remazol Brilliant Blue R (Reactive Blue 19) and other phenolic compounds such as ferulic acid, sinapic acid, caffeic acid, 3-methylcatechol, dopamine hydrochloride, and tannic acid. The acidic pH optimum (3 to 4) and the low temperature optimum (25 °C) were confirmed using both biochemical and electrochemical assays. Kinetic and thermodynamic parameters associated with the catalytic redox center were attained by electrochemistry.

Original language	English
Article number	111651
Journal	Journal of Inorganic Biochemistry
Volume	226
DOIs	https://doi.org/10.1016/j.jinorgbio.2021.111651
Publication status	Published - Jan 2022

Keywords

Actinobacteria
Catalysis
Data mining
Dye-decolorizing peroxidase
Electrochemistry
Profile hidden Markov model

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1016/j.jinorgbio.2021.111651

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@article{51b1a198d4324ed79f933fa465b9a8c9,

title = "Discovery and characterization of a novel Dyp-type peroxidase from a marine actinobacterium isolated from Trondheim fjord, Norway",

abstract = "A new dye-decolorizing peroxidase (DyP) was discovered through a data mining workflow based on HMMER software and profile Hidden Markov Model (HMM) using a dataset of 1200 genomes originated from a Actinobacteria strain collection isolated from Trondheim fjord. Instead of the conserved GXXDG motif known for Dyp-type peroxidases, the enzyme contains a new conserved motif EXXDG which has been not reported before. The enzyme can oxidize an anthraquinone dye Remazol Brilliant Blue R (Reactive Blue 19) and other phenolic compounds such as ferulic acid, sinapic acid, caffeic acid, 3-methylcatechol, dopamine hydrochloride, and tannic acid. The acidic pH optimum (3 to 4) and the low temperature optimum (25 °C) were confirmed using both biochemical and electrochemical assays. Kinetic and thermodynamic parameters associated with the catalytic redox center were attained by electrochemistry.",

keywords = "Actinobacteria, Catalysis, Data mining, Dye-decolorizing peroxidase, Electrochemistry, Profile hidden Markov model",

author = "Cordas, {Cristina M.} and Nguyen, {Giang Son} and Val{\'e}rio, {Gabriel N.} and Malene J{\o}nsson and Katharina S{\"o}llner and Aune, {Ingvild H.} and Alexander Wentzel and Moura, {Jos{\'e} J. G.}",

note = "Funding Information: info:eu-repo/grantAgreement/FCT/6817 - DCRRNI ID/UIDB%2F50006%2F2020/PT# This work was supported by the project OXYMOD of the Centre for Digital Life Norway (DLN) under Research Council of Norway grant number 269408 as well as SINTEF internal funding. Also, this work was supported by the Associate Laboratory for Green Chemistry - LAQV which is financed by national funds from FCT/MCTES (UIDB/50006/2020), Portugal. ",

year = "2022",

month = jan,

doi = "10.1016/j.jinorgbio.2021.111651",

language = "English",

volume = "226",

journal = "Journal of Inorganic Biochemistry",

issn = "0162-0134",

publisher = "Elsevier",

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TY - JOUR

T1 - Discovery and characterization of a novel Dyp-type peroxidase from a marine actinobacterium isolated from Trondheim fjord, Norway

AU - Cordas, Cristina M.

AU - Nguyen, Giang Son

AU - Valério, Gabriel N.

AU - Jønsson, Malene

AU - Söllner, Katharina

AU - Aune, Ingvild H.

AU - Wentzel, Alexander

AU - Moura, José J. G.

N1 - Funding Information: info:eu-repo/grantAgreement/FCT/6817 - DCRRNI ID/UIDB%2F50006%2F2020/PT# This work was supported by the project OXYMOD of the Centre for Digital Life Norway (DLN) under Research Council of Norway grant number 269408 as well as SINTEF internal funding. Also, this work was supported by the Associate Laboratory for Green Chemistry - LAQV which is financed by national funds from FCT/MCTES (UIDB/50006/2020), Portugal.

PY - 2022/1

Y1 - 2022/1

N2 - A new dye-decolorizing peroxidase (DyP) was discovered through a data mining workflow based on HMMER software and profile Hidden Markov Model (HMM) using a dataset of 1200 genomes originated from a Actinobacteria strain collection isolated from Trondheim fjord. Instead of the conserved GXXDG motif known for Dyp-type peroxidases, the enzyme contains a new conserved motif EXXDG which has been not reported before. The enzyme can oxidize an anthraquinone dye Remazol Brilliant Blue R (Reactive Blue 19) and other phenolic compounds such as ferulic acid, sinapic acid, caffeic acid, 3-methylcatechol, dopamine hydrochloride, and tannic acid. The acidic pH optimum (3 to 4) and the low temperature optimum (25 °C) were confirmed using both biochemical and electrochemical assays. Kinetic and thermodynamic parameters associated with the catalytic redox center were attained by electrochemistry.

AB - A new dye-decolorizing peroxidase (DyP) was discovered through a data mining workflow based on HMMER software and profile Hidden Markov Model (HMM) using a dataset of 1200 genomes originated from a Actinobacteria strain collection isolated from Trondheim fjord. Instead of the conserved GXXDG motif known for Dyp-type peroxidases, the enzyme contains a new conserved motif EXXDG which has been not reported before. The enzyme can oxidize an anthraquinone dye Remazol Brilliant Blue R (Reactive Blue 19) and other phenolic compounds such as ferulic acid, sinapic acid, caffeic acid, 3-methylcatechol, dopamine hydrochloride, and tannic acid. The acidic pH optimum (3 to 4) and the low temperature optimum (25 °C) were confirmed using both biochemical and electrochemical assays. Kinetic and thermodynamic parameters associated with the catalytic redox center were attained by electrochemistry.

KW - Actinobacteria

KW - Catalysis

KW - Data mining

KW - Dye-decolorizing peroxidase

KW - Electrochemistry

KW - Profile hidden Markov model

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SN - 0162-0134

VL - 226

JO - Journal of Inorganic Biochemistry

JF - Journal of Inorganic Biochemistry

M1 - 111651

ER -

Discovery and characterization of a novel Dyp-type peroxidase from a marine actinobacterium isolated from Trondheim fjord, Norway

Abstract

Keywords

UN SDGs

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