Extraction and determination of enzymes produced by Ceriporiopsis subvermispora during biopulping of Pinus taeda wood chips

Priscila Brasil de Souza-Cruz, Juanita Freer, Matti Siika-aho, Andre Ferraz (Corresponding Author)

Research output: Contribution to journalArticleScientificpeer-review

88 Citations (Scopus)

Abstract

Ceriporiopsis subvermispora is a white-rot basidiomycete that degrades lignin selectively and often is used in biopulping. Development of appropriate experimental procedures for recovery and determination of enzymes produced by C. subvermispora during biopulping is necessary to evaluate the role of each enzyme in this process. In this work, enzymes produced during biopulping were extracted and determined by using a series of substrates. Manganese-dependent peroxidases (MnP) predominated over laccases, which were of minor significance. The lack of laccases was further confirmed by assaying several substrates such as syrindaldazine, o-dianisidine and ABTS. A basal oxidation of syringaldazine and phenol red in the absence of exogenous Mn2+ led to the assumption that the extracts contained some Mn-independent peroxidase or enough Mn2+ to initiate MnP catalyzed reactions. The presence of Mn2+ was evidenced since phenol red was not oxidized by a 16-h-dialysed extract. Addition of 111 μM of Mn2+ to the reaction medium restored the oxidative activity. Lignin peroxidase activity was not detected in the extracts based on the Azure B assay. Cellulase activities were very low while xylanases predominated. The xylanolytic complex was deficient in beta-xylosidase. Successive extractions were performed for a quantitative recovery of the enzymes adsorbed on wood chips. The first 4-h extraction recovered an average of 50% of the total enzymatic activities.

Original languageEnglish
Pages (from-to)228 - 234
Number of pages7
JournalEnzyme and Microbial Technology
Volume34
Issue number3-4
DOIs
Publication statusPublished - 2004
MoE publication typeA1 Journal article-refereed

Fingerprint

manganese peroxidase
Biopulping
Pinus taeda
Coriolaceae
Wood
Enzymes
Phenolsulfonphthalein
Laccase
Lignin
Phenols
Manganese
Dianisidine
Recovery
Basidiomycota
Cellulase
Substrates
Peroxidase
Assays
Oxidation

Keywords

  • Ceriporiopsis subvermispora
  • Oxidative enzymes
  • Biopulping
  • White-rot fungi

Cite this

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title = "Extraction and determination of enzymes produced by Ceriporiopsis subvermispora during biopulping of Pinus taeda wood chips",
abstract = "Ceriporiopsis subvermispora is a white-rot basidiomycete that degrades lignin selectively and often is used in biopulping. Development of appropriate experimental procedures for recovery and determination of enzymes produced by C. subvermispora during biopulping is necessary to evaluate the role of each enzyme in this process. In this work, enzymes produced during biopulping were extracted and determined by using a series of substrates. Manganese-dependent peroxidases (MnP) predominated over laccases, which were of minor significance. The lack of laccases was further confirmed by assaying several substrates such as syrindaldazine, o-dianisidine and ABTS. A basal oxidation of syringaldazine and phenol red in the absence of exogenous Mn2+ led to the assumption that the extracts contained some Mn-independent peroxidase or enough Mn2+ to initiate MnP catalyzed reactions. The presence of Mn2+ was evidenced since phenol red was not oxidized by a 16-h-dialysed extract. Addition of 111 μM of Mn2+ to the reaction medium restored the oxidative activity. Lignin peroxidase activity was not detected in the extracts based on the Azure B assay. Cellulase activities were very low while xylanases predominated. The xylanolytic complex was deficient in beta-xylosidase. Successive extractions were performed for a quantitative recovery of the enzymes adsorbed on wood chips. The first 4-h extraction recovered an average of 50{\%} of the total enzymatic activities.",
keywords = "Ceriporiopsis subvermispora, Oxidative enzymes, Biopulping, White-rot fungi",
author = "{Brasil de Souza-Cruz}, Priscila and Juanita Freer and Matti Siika-aho and Andre Ferraz",
year = "2004",
doi = "10.1016/j.enzmictec.2003.10.005",
language = "English",
volume = "34",
pages = "228 -- 234",
journal = "Enzyme and Microbial Technology",
issn = "0141-0229",
publisher = "Elsevier",
number = "3-4",

}

Extraction and determination of enzymes produced by Ceriporiopsis subvermispora during biopulping of Pinus taeda wood chips. / Brasil de Souza-Cruz, Priscila; Freer, Juanita; Siika-aho, Matti; Ferraz, Andre (Corresponding Author).

In: Enzyme and Microbial Technology, Vol. 34, No. 3-4, 2004, p. 228 - 234.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Extraction and determination of enzymes produced by Ceriporiopsis subvermispora during biopulping of Pinus taeda wood chips

AU - Brasil de Souza-Cruz, Priscila

AU - Freer, Juanita

AU - Siika-aho, Matti

AU - Ferraz, Andre

PY - 2004

Y1 - 2004

N2 - Ceriporiopsis subvermispora is a white-rot basidiomycete that degrades lignin selectively and often is used in biopulping. Development of appropriate experimental procedures for recovery and determination of enzymes produced by C. subvermispora during biopulping is necessary to evaluate the role of each enzyme in this process. In this work, enzymes produced during biopulping were extracted and determined by using a series of substrates. Manganese-dependent peroxidases (MnP) predominated over laccases, which were of minor significance. The lack of laccases was further confirmed by assaying several substrates such as syrindaldazine, o-dianisidine and ABTS. A basal oxidation of syringaldazine and phenol red in the absence of exogenous Mn2+ led to the assumption that the extracts contained some Mn-independent peroxidase or enough Mn2+ to initiate MnP catalyzed reactions. The presence of Mn2+ was evidenced since phenol red was not oxidized by a 16-h-dialysed extract. Addition of 111 μM of Mn2+ to the reaction medium restored the oxidative activity. Lignin peroxidase activity was not detected in the extracts based on the Azure B assay. Cellulase activities were very low while xylanases predominated. The xylanolytic complex was deficient in beta-xylosidase. Successive extractions were performed for a quantitative recovery of the enzymes adsorbed on wood chips. The first 4-h extraction recovered an average of 50% of the total enzymatic activities.

AB - Ceriporiopsis subvermispora is a white-rot basidiomycete that degrades lignin selectively and often is used in biopulping. Development of appropriate experimental procedures for recovery and determination of enzymes produced by C. subvermispora during biopulping is necessary to evaluate the role of each enzyme in this process. In this work, enzymes produced during biopulping were extracted and determined by using a series of substrates. Manganese-dependent peroxidases (MnP) predominated over laccases, which were of minor significance. The lack of laccases was further confirmed by assaying several substrates such as syrindaldazine, o-dianisidine and ABTS. A basal oxidation of syringaldazine and phenol red in the absence of exogenous Mn2+ led to the assumption that the extracts contained some Mn-independent peroxidase or enough Mn2+ to initiate MnP catalyzed reactions. The presence of Mn2+ was evidenced since phenol red was not oxidized by a 16-h-dialysed extract. Addition of 111 μM of Mn2+ to the reaction medium restored the oxidative activity. Lignin peroxidase activity was not detected in the extracts based on the Azure B assay. Cellulase activities were very low while xylanases predominated. The xylanolytic complex was deficient in beta-xylosidase. Successive extractions were performed for a quantitative recovery of the enzymes adsorbed on wood chips. The first 4-h extraction recovered an average of 50% of the total enzymatic activities.

KW - Ceriporiopsis subvermispora

KW - Oxidative enzymes

KW - Biopulping

KW - White-rot fungi

U2 - 10.1016/j.enzmictec.2003.10.005

DO - 10.1016/j.enzmictec.2003.10.005

M3 - Article

VL - 34

SP - 228

EP - 234

JO - Enzyme and Microbial Technology

JF - Enzyme and Microbial Technology

SN - 0141-0229

IS - 3-4

ER -