Strategies for improving ligninolytic enzyme activities in semi-solid-state bioreactors

Susana Rodríguez Couto, Marjaana Rättö, Alberto Domínguez, Angeles Sanromán (Corresponding Author)

Research output: Contribution to journalArticleScientificpeer-review

13 Citations (Scopus)

Abstract

The production of ligninolytic enzymes by Phanerochaete chrysosporium BKM-F-1767 (ATCC 24725) was studied in laboratory-scale bioreactors, operating under semi-solid-state conditions. The bioreactors were filled with inert support (polypropylene sponges) and cultivation was carried out in batch. Veratryl alcohol (2 mM) and Tween 80 (0.05% v/v) were added at the beginning of the fermentation to stimulate the production of ligninolytic enzymes. A modification in the design of a bioreactor, which operates in semi-solid-state conditions, lead to a significant improvement in the ligninolytic enzyme activities obtained. Thus, by modifying the design of the bioreactor employed in the current study, it was possible to increase about tenfold manganese-dependent peroxidase (MnP) activities and around 40% lignin peroxidase (LiP) activities. Moreover, both MnP and LiP profiles were more regular in the modified bioreactor.
Original languageEnglish
Pages (from-to)995-999
JournalProcess Biochemistry
Volume36
Issue number10
DOIs
Publication statusPublished - 2001
MoE publication typeA1 Journal article-refereed

Fingerprint

Enzyme activity
Bioreactors
manganese peroxidase
Enzymes
Lignin
Manganese
Phanerochaete
Polysorbates
Polypropylenes
Porifera
Fermentation
Alcohols
lignin peroxidase

Cite this

Rodríguez Couto, Susana ; Rättö, Marjaana ; Domínguez, Alberto ; Sanromán, Angeles. / Strategies for improving ligninolytic enzyme activities in semi-solid-state bioreactors. In: Process Biochemistry. 2001 ; Vol. 36, No. 10. pp. 995-999.
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title = "Strategies for improving ligninolytic enzyme activities in semi-solid-state bioreactors",
abstract = "The production of ligninolytic enzymes by Phanerochaete chrysosporium BKM-F-1767 (ATCC 24725) was studied in laboratory-scale bioreactors, operating under semi-solid-state conditions. The bioreactors were filled with inert support (polypropylene sponges) and cultivation was carried out in batch. Veratryl alcohol (2 mM) and Tween 80 (0.05{\%} v/v) were added at the beginning of the fermentation to stimulate the production of ligninolytic enzymes. A modification in the design of a bioreactor, which operates in semi-solid-state conditions, lead to a significant improvement in the ligninolytic enzyme activities obtained. Thus, by modifying the design of the bioreactor employed in the current study, it was possible to increase about tenfold manganese-dependent peroxidase (MnP) activities and around 40{\%} lignin peroxidase (LiP) activities. Moreover, both MnP and LiP profiles were more regular in the modified bioreactor.",
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Rodríguez Couto, S, Rättö, M, Domínguez, A & Sanromán, A 2001, 'Strategies for improving ligninolytic enzyme activities in semi-solid-state bioreactors', Process Biochemistry, vol. 36, no. 10, pp. 995-999. https://doi.org/10.1016/S0032-9592(01)00139-X

Strategies for improving ligninolytic enzyme activities in semi-solid-state bioreactors. / Rodríguez Couto, Susana; Rättö, Marjaana; Domínguez, Alberto; Sanromán, Angeles (Corresponding Author).

In: Process Biochemistry, Vol. 36, No. 10, 2001, p. 995-999.

Research output: Contribution to journalArticleScientificpeer-review

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AB - The production of ligninolytic enzymes by Phanerochaete chrysosporium BKM-F-1767 (ATCC 24725) was studied in laboratory-scale bioreactors, operating under semi-solid-state conditions. The bioreactors were filled with inert support (polypropylene sponges) and cultivation was carried out in batch. Veratryl alcohol (2 mM) and Tween 80 (0.05% v/v) were added at the beginning of the fermentation to stimulate the production of ligninolytic enzymes. A modification in the design of a bioreactor, which operates in semi-solid-state conditions, lead to a significant improvement in the ligninolytic enzyme activities obtained. Thus, by modifying the design of the bioreactor employed in the current study, it was possible to increase about tenfold manganese-dependent peroxidase (MnP) activities and around 40% lignin peroxidase (LiP) activities. Moreover, both MnP and LiP profiles were more regular in the modified bioreactor.

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