Production of a chimeric enzyme tool associating the Trichoderma reesei swollenin with the Aspergillus niger feruloyl esterase A for release of ferulic acid

Anthony Levasseur, Markku Saloheimo, David Navarro, Martina Andberg, Frédéric Monot, Tiina Nakari-Setälä, Marcel Asther, Eric Record

Research output: Contribution to journalArticleScientificpeer-review

36 Citations (Scopus)

Abstract

The main goals of this work were to produce the fusion protein of the Trichoderma reesei swollenin I (SWOI) and Aspergillus niger feruloyl esterase A (FAEA) and to study the effect of the physical association of the fusion partners on the efficiency of the enzyme. The fusion protein was produced up to 25 mg l−1 in the T. reesei strains Rut-C30 and CL847. In parallel, FAEA alone was produced for use as a control protein in application tests. Recombinant FAEA and SWOI–FAEA were purified to homogeneity and characterized. The biochemical and kinetic characteristics of the two recombinant proteins were found to be similar to those of native FAEA, except for the temperature stability and specific activity of the SWOI–FAEA. Finally, the SWOI–FAEA protein was tested for release of ferulic acid from wheat bran. A period of 24 h of enzymatic hydrolysis with the SWOI–FAEA improved the efficiency of ferulic acid release by 50% compared with the results obtained using the free FAEA and SWOI. Ferulic acid is used as an antioxidant and flavor precursor in the food and pharmaceutical industries. This is the first report of a potential application of the SWOI protein fused with an enzyme of industrial interest.
Original languageEnglish
Pages (from-to)872 - 880
JournalApplied Microbiology and Biotechnology
Volume73
Issue number4
DOIs
Publication statusPublished - 2006
MoE publication typeA1 Journal article-refereed

Fingerprint

ferulic acid
Trichoderma
Aspergillus niger
Enzymes
Proteins
Food Industry
Dietary Fiber
Drug Industry
Recombinant Proteins
Hydrolysis
Antioxidants
feruloyl esterase

Keywords

  • Trichoderma reesei
  • Chimeric protein
  • Swollenin
  • Feruloyl esterase
  • Biotechnology
  • Fungus

Cite this

@article{7a670cb11ae84f1ebe82bcf573d370c9,
title = "Production of a chimeric enzyme tool associating the Trichoderma reesei swollenin with the Aspergillus niger feruloyl esterase A for release of ferulic acid",
abstract = "The main goals of this work were to produce the fusion protein of the Trichoderma reesei swollenin I (SWOI) and Aspergillus niger feruloyl esterase A (FAEA) and to study the effect of the physical association of the fusion partners on the efficiency of the enzyme. The fusion protein was produced up to 25 mg l−1 in the T. reesei strains Rut-C30 and CL847. In parallel, FAEA alone was produced for use as a control protein in application tests. Recombinant FAEA and SWOI–FAEA were purified to homogeneity and characterized. The biochemical and kinetic characteristics of the two recombinant proteins were found to be similar to those of native FAEA, except for the temperature stability and specific activity of the SWOI–FAEA. Finally, the SWOI–FAEA protein was tested for release of ferulic acid from wheat bran. A period of 24 h of enzymatic hydrolysis with the SWOI–FAEA improved the efficiency of ferulic acid release by 50{\%} compared with the results obtained using the free FAEA and SWOI. Ferulic acid is used as an antioxidant and flavor precursor in the food and pharmaceutical industries. This is the first report of a potential application of the SWOI protein fused with an enzyme of industrial interest.",
keywords = "Trichoderma reesei, Chimeric protein, Swollenin, Feruloyl esterase, Biotechnology, Fungus",
author = "Anthony Levasseur and Markku Saloheimo and David Navarro and Martina Andberg and Fr{\'e}d{\'e}ric Monot and Tiina Nakari-Set{\"a}l{\"a} and Marcel Asther and Eric Record",
year = "2006",
doi = "10.1007/s00253-006-0546-8",
language = "English",
volume = "73",
pages = "872 -- 880",
journal = "Applied Microbiology and Biotechnology",
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}

Production of a chimeric enzyme tool associating the Trichoderma reesei swollenin with the Aspergillus niger feruloyl esterase A for release of ferulic acid. / Levasseur, Anthony; Saloheimo, Markku; Navarro, David; Andberg, Martina; Monot, Frédéric; Nakari-Setälä, Tiina; Asther, Marcel; Record, Eric.

In: Applied Microbiology and Biotechnology, Vol. 73, No. 4, 2006, p. 872 - 880.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Production of a chimeric enzyme tool associating the Trichoderma reesei swollenin with the Aspergillus niger feruloyl esterase A for release of ferulic acid

AU - Levasseur, Anthony

AU - Saloheimo, Markku

AU - Navarro, David

AU - Andberg, Martina

AU - Monot, Frédéric

AU - Nakari-Setälä, Tiina

AU - Asther, Marcel

AU - Record, Eric

PY - 2006

Y1 - 2006

N2 - The main goals of this work were to produce the fusion protein of the Trichoderma reesei swollenin I (SWOI) and Aspergillus niger feruloyl esterase A (FAEA) and to study the effect of the physical association of the fusion partners on the efficiency of the enzyme. The fusion protein was produced up to 25 mg l−1 in the T. reesei strains Rut-C30 and CL847. In parallel, FAEA alone was produced for use as a control protein in application tests. Recombinant FAEA and SWOI–FAEA were purified to homogeneity and characterized. The biochemical and kinetic characteristics of the two recombinant proteins were found to be similar to those of native FAEA, except for the temperature stability and specific activity of the SWOI–FAEA. Finally, the SWOI–FAEA protein was tested for release of ferulic acid from wheat bran. A period of 24 h of enzymatic hydrolysis with the SWOI–FAEA improved the efficiency of ferulic acid release by 50% compared with the results obtained using the free FAEA and SWOI. Ferulic acid is used as an antioxidant and flavor precursor in the food and pharmaceutical industries. This is the first report of a potential application of the SWOI protein fused with an enzyme of industrial interest.

AB - The main goals of this work were to produce the fusion protein of the Trichoderma reesei swollenin I (SWOI) and Aspergillus niger feruloyl esterase A (FAEA) and to study the effect of the physical association of the fusion partners on the efficiency of the enzyme. The fusion protein was produced up to 25 mg l−1 in the T. reesei strains Rut-C30 and CL847. In parallel, FAEA alone was produced for use as a control protein in application tests. Recombinant FAEA and SWOI–FAEA were purified to homogeneity and characterized. The biochemical and kinetic characteristics of the two recombinant proteins were found to be similar to those of native FAEA, except for the temperature stability and specific activity of the SWOI–FAEA. Finally, the SWOI–FAEA protein was tested for release of ferulic acid from wheat bran. A period of 24 h of enzymatic hydrolysis with the SWOI–FAEA improved the efficiency of ferulic acid release by 50% compared with the results obtained using the free FAEA and SWOI. Ferulic acid is used as an antioxidant and flavor precursor in the food and pharmaceutical industries. This is the first report of a potential application of the SWOI protein fused with an enzyme of industrial interest.

KW - Trichoderma reesei

KW - Chimeric protein

KW - Swollenin

KW - Feruloyl esterase

KW - Biotechnology

KW - Fungus

U2 - 10.1007/s00253-006-0546-8

DO - 10.1007/s00253-006-0546-8

M3 - Article

VL - 73

SP - 872

EP - 880

JO - Applied Microbiology and Biotechnology

JF - Applied Microbiology and Biotechnology

SN - 0175-7598

IS - 4

ER -