Discovery and Characterization of a Novel Thermostable β-Amino Acid Transaminase from a Meiothermus Strain Isolated in an Icelandic Hot Spring

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Standard

Discovery and Characterization of a Novel Thermostable β-Amino Acid Transaminase from a Meiothermus Strain Isolated in an Icelandic Hot Spring. / Ferrandi, Erica E.; Bassanini, Ivan; Sechi, Barbara; Vanoni, Marta; Tessaro, Davide; Gudbergsdóttir, Sóley Ruth; Riva, Sergio; Peng, Xu; Monti, Daniela.

I: Biotechnology Journal, Bind 15, Nr. 11, 2000125, 2020.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Ferrandi, EE, Bassanini, I, Sechi, B, Vanoni, M, Tessaro, D, Gudbergsdóttir, SR, Riva, S, Peng, X & Monti, D 2020, 'Discovery and Characterization of a Novel Thermostable β-Amino Acid Transaminase from a Meiothermus Strain Isolated in an Icelandic Hot Spring', Biotechnology Journal, bind 15, nr. 11, 2000125. https://doi.org/10.1002/biot.202000125

APA

Ferrandi, E. E., Bassanini, I., Sechi, B., Vanoni, M., Tessaro, D., Gudbergsdóttir, S. R., Riva, S., Peng, X., & Monti, D. (2020). Discovery and Characterization of a Novel Thermostable β-Amino Acid Transaminase from a Meiothermus Strain Isolated in an Icelandic Hot Spring. Biotechnology Journal, 15(11), [2000125]. https://doi.org/10.1002/biot.202000125

Vancouver

Ferrandi EE, Bassanini I, Sechi B, Vanoni M, Tessaro D, Gudbergsdóttir SR o.a. Discovery and Characterization of a Novel Thermostable β-Amino Acid Transaminase from a Meiothermus Strain Isolated in an Icelandic Hot Spring. Biotechnology Journal. 2020;15(11). 2000125. https://doi.org/10.1002/biot.202000125

Author

Ferrandi, Erica E. ; Bassanini, Ivan ; Sechi, Barbara ; Vanoni, Marta ; Tessaro, Davide ; Gudbergsdóttir, Sóley Ruth ; Riva, Sergio ; Peng, Xu ; Monti, Daniela. / Discovery and Characterization of a Novel Thermostable β-Amino Acid Transaminase from a Meiothermus Strain Isolated in an Icelandic Hot Spring. I: Biotechnology Journal. 2020 ; Bind 15, Nr. 11.

Bibtex

@article{953a382a1d674320b3d0a70636a112b9,
title = "Discovery and Characterization of a Novel Thermostable β-Amino Acid Transaminase from a Meiothermus Strain Isolated in an Icelandic Hot Spring",
abstract = "AMeiothermusstrain capable of using beta-phenylalanine for growth is isolated by culture enrichment of samples collected in hot environments and the genome is sequenced showing the presence of 22 putative transaminase (TA) sequences. On the basis of phylogenetic and sequence analysis, a TA termed Ms-TA2 is selected for further studies. The enzyme is successfully produced inEscherichia coliRosetta(DE3) cells, with 70 mg of pure protein obtained from 1 L culture after purification by affinity chromatography. Ms-TA2 shows high activity toward (S)-beta-phenylalanine and other (S)-beta-amino acids, as well as a preference for alpha-ketoglutarate and aromatic aldehydes as amino acceptors. Moreover, Ms-TA2 is shown to be a thermostable enzyme by maintaining about 60% of the starting activity after 3 h incubation at 50 degrees C and showing a melting temperature of about 73 degrees C. Finally, a homology-based structural model of Ms-TA2 is built and key active site interactions for substrate and cofactor binding are analyzed.",
keywords = "amine transferases, biocatalysis, culture enrichment, thermostability, beta-amino acids, PYRUVATE TRANSAMINASE, OMEGA-TRANSAMINASE, IDENTIFICATION, ALGORITHM, SEQUENCE",
author = "Ferrandi, {Erica E.} and Ivan Bassanini and Barbara Sechi and Marta Vanoni and Davide Tessaro and Gudbergsd{\'o}ttir, {S{\'o}ley Ruth} and Sergio Riva and Xu Peng and Daniela Monti",
year = "2020",
doi = "10.1002/biot.202000125",
language = "English",
volume = "15",
journal = "Biotechnology Journal",
issn = "1860-6768",
publisher = "Wiley - V C H Verlag GmbH & Co. KGaA",
number = "11",

}

RIS

TY - JOUR

T1 - Discovery and Characterization of a Novel Thermostable β-Amino Acid Transaminase from a Meiothermus Strain Isolated in an Icelandic Hot Spring

AU - Ferrandi, Erica E.

AU - Bassanini, Ivan

AU - Sechi, Barbara

AU - Vanoni, Marta

AU - Tessaro, Davide

AU - Gudbergsdóttir, Sóley Ruth

AU - Riva, Sergio

AU - Peng, Xu

AU - Monti, Daniela

PY - 2020

Y1 - 2020

N2 - AMeiothermusstrain capable of using beta-phenylalanine for growth is isolated by culture enrichment of samples collected in hot environments and the genome is sequenced showing the presence of 22 putative transaminase (TA) sequences. On the basis of phylogenetic and sequence analysis, a TA termed Ms-TA2 is selected for further studies. The enzyme is successfully produced inEscherichia coliRosetta(DE3) cells, with 70 mg of pure protein obtained from 1 L culture after purification by affinity chromatography. Ms-TA2 shows high activity toward (S)-beta-phenylalanine and other (S)-beta-amino acids, as well as a preference for alpha-ketoglutarate and aromatic aldehydes as amino acceptors. Moreover, Ms-TA2 is shown to be a thermostable enzyme by maintaining about 60% of the starting activity after 3 h incubation at 50 degrees C and showing a melting temperature of about 73 degrees C. Finally, a homology-based structural model of Ms-TA2 is built and key active site interactions for substrate and cofactor binding are analyzed.

AB - AMeiothermusstrain capable of using beta-phenylalanine for growth is isolated by culture enrichment of samples collected in hot environments and the genome is sequenced showing the presence of 22 putative transaminase (TA) sequences. On the basis of phylogenetic and sequence analysis, a TA termed Ms-TA2 is selected for further studies. The enzyme is successfully produced inEscherichia coliRosetta(DE3) cells, with 70 mg of pure protein obtained from 1 L culture after purification by affinity chromatography. Ms-TA2 shows high activity toward (S)-beta-phenylalanine and other (S)-beta-amino acids, as well as a preference for alpha-ketoglutarate and aromatic aldehydes as amino acceptors. Moreover, Ms-TA2 is shown to be a thermostable enzyme by maintaining about 60% of the starting activity after 3 h incubation at 50 degrees C and showing a melting temperature of about 73 degrees C. Finally, a homology-based structural model of Ms-TA2 is built and key active site interactions for substrate and cofactor binding are analyzed.

KW - amine transferases

KW - biocatalysis

KW - culture enrichment

KW - thermostability

KW - beta-amino acids

KW - PYRUVATE TRANSAMINASE

KW - OMEGA-TRANSAMINASE

KW - IDENTIFICATION

KW - ALGORITHM

KW - SEQUENCE

U2 - 10.1002/biot.202000125

DO - 10.1002/biot.202000125

M3 - Journal article

C2 - 32893504

VL - 15

JO - Biotechnology Journal

JF - Biotechnology Journal

SN - 1860-6768

IS - 11

M1 - 2000125

ER -

ID: 248891897