Production and characterisation of AoSOX2 from Aspergillus oryzae, a novel flavin-dependent sulfhydryl oxidase with good pH and temperature stability

Greta Faccio (Corresponding Author), Kristiina Kruus, Johanna Buchert, Markku Saloheimo

Research output: Contribution to journalArticleScientificpeer-review

3 Citations (Scopus)

Abstract

Sulfhydryl oxidases have found application in the improvement of both dairy and baking products due to their ability to oxidise thiol groups in small molecules and cysteine residues in proteins. A genome mining study of the available fungal genomes had previously been performed by our group in order to identify novel sulfhydryl oxidases suitable for industrial applications and a representative enzyme was produced, AoSOX1 from Aspergillus oryzae (Faccio et al. BMC Biochem 11:31, 2010). As a result of the study, a second gene coding for a potentially secreted sulfhydryl oxidase, AoSOX2, was identified in the genome of A. oryzae. The protein AoSOX2 was heterologously expressed in Trichoderma reesei and characterised with regard to both biochemical properties as well as preliminary structural analysis. AoSOX2 showed activity on dithiothreitol and glutathione, and to a lesser extent on D/L-cysteine and beta-mercaptoethanol. AoSOX2 was a homodimeric flavin-dependent protein of approximately 78 kDa (monomer 42412 Da) and its secondary structure presents alpha-helical elements. A. oryzae AoSOX2 showed a significant stability to pH and temperature.
Original languageEnglish
Pages (from-to)941-949
Number of pages9
JournalApplied Microbiology and Biotechnology
Volume90
Issue number3
DOIs
Publication statusPublished - 2011
MoE publication typeA1 Journal article-refereed

Fingerprint

Aspergillus oryzae
Temperature
Cysteine
Fungal Genome
Genome
Proteins
Trichoderma
Dairy Products
Mercaptoethanol
Dithiothreitol
Sulfhydryl Compounds
Glutathione
Enzymes
Genes
sulfhydryl oxidase
4,6-dinitro-o-cresol

Keywords

  • Sulfhydryl oxidase
  • secreted
  • fungal
  • flavoenzyme
  • production
  • characterization

Cite this

@article{7294f7959347473895ec9a1ee93411a9,
title = "Production and characterisation of AoSOX2 from Aspergillus oryzae, a novel flavin-dependent sulfhydryl oxidase with good pH and temperature stability",
abstract = "Sulfhydryl oxidases have found application in the improvement of both dairy and baking products due to their ability to oxidise thiol groups in small molecules and cysteine residues in proteins. A genome mining study of the available fungal genomes had previously been performed by our group in order to identify novel sulfhydryl oxidases suitable for industrial applications and a representative enzyme was produced, AoSOX1 from Aspergillus oryzae (Faccio et al. BMC Biochem 11:31, 2010). As a result of the study, a second gene coding for a potentially secreted sulfhydryl oxidase, AoSOX2, was identified in the genome of A. oryzae. The protein AoSOX2 was heterologously expressed in Trichoderma reesei and characterised with regard to both biochemical properties as well as preliminary structural analysis. AoSOX2 showed activity on dithiothreitol and glutathione, and to a lesser extent on D/L-cysteine and beta-mercaptoethanol. AoSOX2 was a homodimeric flavin-dependent protein of approximately 78 kDa (monomer 42412 Da) and its secondary structure presents alpha-helical elements. A. oryzae AoSOX2 showed a significant stability to pH and temperature.",
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language = "English",
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Production and characterisation of AoSOX2 from Aspergillus oryzae, a novel flavin-dependent sulfhydryl oxidase with good pH and temperature stability. / Faccio, Greta (Corresponding Author); Kruus, Kristiina; Buchert, Johanna; Saloheimo, Markku.

In: Applied Microbiology and Biotechnology, Vol. 90, No. 3, 2011, p. 941-949.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Production and characterisation of AoSOX2 from Aspergillus oryzae, a novel flavin-dependent sulfhydryl oxidase with good pH and temperature stability

AU - Faccio, Greta

AU - Kruus, Kristiina

AU - Buchert, Johanna

AU - Saloheimo, Markku

PY - 2011

Y1 - 2011

N2 - Sulfhydryl oxidases have found application in the improvement of both dairy and baking products due to their ability to oxidise thiol groups in small molecules and cysteine residues in proteins. A genome mining study of the available fungal genomes had previously been performed by our group in order to identify novel sulfhydryl oxidases suitable for industrial applications and a representative enzyme was produced, AoSOX1 from Aspergillus oryzae (Faccio et al. BMC Biochem 11:31, 2010). As a result of the study, a second gene coding for a potentially secreted sulfhydryl oxidase, AoSOX2, was identified in the genome of A. oryzae. The protein AoSOX2 was heterologously expressed in Trichoderma reesei and characterised with regard to both biochemical properties as well as preliminary structural analysis. AoSOX2 showed activity on dithiothreitol and glutathione, and to a lesser extent on D/L-cysteine and beta-mercaptoethanol. AoSOX2 was a homodimeric flavin-dependent protein of approximately 78 kDa (monomer 42412 Da) and its secondary structure presents alpha-helical elements. A. oryzae AoSOX2 showed a significant stability to pH and temperature.

AB - Sulfhydryl oxidases have found application in the improvement of both dairy and baking products due to their ability to oxidise thiol groups in small molecules and cysteine residues in proteins. A genome mining study of the available fungal genomes had previously been performed by our group in order to identify novel sulfhydryl oxidases suitable for industrial applications and a representative enzyme was produced, AoSOX1 from Aspergillus oryzae (Faccio et al. BMC Biochem 11:31, 2010). As a result of the study, a second gene coding for a potentially secreted sulfhydryl oxidase, AoSOX2, was identified in the genome of A. oryzae. The protein AoSOX2 was heterologously expressed in Trichoderma reesei and characterised with regard to both biochemical properties as well as preliminary structural analysis. AoSOX2 showed activity on dithiothreitol and glutathione, and to a lesser extent on D/L-cysteine and beta-mercaptoethanol. AoSOX2 was a homodimeric flavin-dependent protein of approximately 78 kDa (monomer 42412 Da) and its secondary structure presents alpha-helical elements. A. oryzae AoSOX2 showed a significant stability to pH and temperature.

KW - Sulfhydryl oxidase

KW - secreted

KW - fungal

KW - flavoenzyme

KW - production

KW - characterization

U2 - 10.1007/s00253-011-3129-2

DO - 10.1007/s00253-011-3129-2

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JO - Applied Microbiology and Biotechnology

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