PhanerochaeteV1, Main, Exploration, bibRecord, 000F05

Overproduction of lignin-degrading enzymes by an isolate of Phanerochaete chrysosporium.

Identifieur interne : 000F05 ( Main/Exploration ); précédent : 000F04; suivant : 000F06

Overproduction of lignin-degrading enzymes by an isolate of Phanerochaete chrysosporium.

Auteurs : A B Orth [États-Unis] ; M. Denny ; M. Tien

Source :

Applied and environmental microbiology [ 0099-2240 ] ; 1991.

RBID : pubmed:1768132

Descripteurs français

KwdFr :
- Alcohol oxidoreductases (biosynthèse), Alcools benzyliques (pharmacologie), Chrysosporium (enzymologie), Chrysosporium (génétique), Chrysosporium (isolement et purification), Lignine (métabolisme), Manganèse (pharmacologie), Milieux de culture (MeSH), Peroxidases (biosynthèse), Protéines fongiques (biosynthèse).
MESH :
- biosynthèse : Alcohol oxidoreductases, Peroxidases, Protéines fongiques.
- enzymologie : Chrysosporium.
- génétique : Chrysosporium.
- isolement et purification : Chrysosporium.
- métabolisme : Lignine.
- pharmacologie : Alcools benzyliques, Manganèse.
- Milieux de culture.

English descriptors

KwdEn :
- Alcohol Oxidoreductases (biosynthesis), Benzyl Alcohols (pharmacology), Chrysosporium (enzymology), Chrysosporium (genetics), Chrysosporium (isolation & purification), Culture Media (MeSH), Fungal Proteins (biosynthesis), Lignin (metabolism), Manganese (pharmacology), Peroxidases (biosynthesis).
MESH :
- chemical , biosynthesis : Alcohol Oxidoreductases, Fungal Proteins, Peroxidases.
- chemical , metabolism : Lignin.
- chemical , pharmacology : Benzyl Alcohols, Manganese.
- enzymology : Chrysosporium.
- genetics : Chrysosporium.
- isolation & purification : Chrysosporium.
- chemical : Culture Media.

Abstract

Phanerochaete chrysosporium is a white rot fungus which secretes a family of lignin-degrading enzymes under nutrient limitation. PSBL-1 is a mutant of this organism that generates the ligninolytic system under nonlimiting conditions during primary metabolism. Lignin peroxidase, manganese peroxidase, and glyoxal oxidase activities for PSBL-1 under nonlimiting conditions were 4- to 10-fold higher than those of the wild type (WT) under nitrogen-limiting conditions. PSBL-1 was still in the log phase of growth while secreting the enzymes, whereas the WT had ceased to grow by this time. As in the WT, manganese(II) increased manganese peroxidase activity in the mutant. However, manganese also caused an increase in lignin peroxidase and glyoxal oxidase activities in PSBL-1. Addition of veratryl alcohol to the culture medium stimulated lignin peroxidase activity, inhibited glyoxal oxidase activity, and had little effect on manganese peroxidase activity in PSBL-1, as in the WT. Fast protein liquid chromatography (FPLC) analysis shows production of larger amounts of isozyme H2 in PSBL-1 than in the WT. These properties make PSBL-1 very useful for isolation of large amounts of all ligninolytic enzymes for biochemical study, and they open the possibility of scale-up production for pratical use.

DOI: 10.1128/AEM.57.9.2591-2596.1991
PubMed: 1768132
PubMed Central: PMC183625

Affiliations:

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Le document en format XML

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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Alcohol Oxidoreductases (biosynthesis)</term>
<term>Benzyl Alcohols (pharmacology)</term>
<term>Chrysosporium (enzymology)</term>
<term>Chrysosporium (genetics)</term>
<term>Chrysosporium (isolation & purification)</term>
<term>Culture Media (MeSH)</term>
<term>Fungal Proteins (biosynthesis)</term>
<term>Lignin (metabolism)</term>
<term>Manganese (pharmacology)</term>
<term>Peroxidases (biosynthesis)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Alcohol oxidoreductases (biosynthèse)</term>
<term>Alcools benzyliques (pharmacologie)</term>
<term>Chrysosporium (enzymologie)</term>
<term>Chrysosporium (génétique)</term>
<term>Chrysosporium (isolement et purification)</term>
<term>Lignine (métabolisme)</term>
<term>Manganèse (pharmacologie)</term>
<term>Milieux de culture (MeSH)</term>
<term>Peroxidases (biosynthèse)</term>
<term>Protéines fongiques (biosynthèse)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Alcohol Oxidoreductases</term>
<term>Fungal Proteins</term>
<term>Peroxidases</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Lignin</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Benzyl Alcohols</term>
<term>Manganese</term>
</keywords>
<keywords scheme="MESH" qualifier="biosynthèse" xml:lang="fr"><term>Alcohol oxidoreductases</term>
<term>Peroxidases</term>
<term>Protéines fongiques</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Chrysosporium</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Chrysosporium</term>
</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Chrysosporium</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Chrysosporium</term>
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<keywords scheme="MESH" qualifier="isolation & purification" xml:lang="en"><term>Chrysosporium</term>
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<keywords scheme="MESH" qualifier="isolement et purification" xml:lang="fr"><term>Chrysosporium</term>
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<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Lignine</term>
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<keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Alcools benzyliques</term>
<term>Manganèse</term>
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<front><div type="abstract" xml:lang="en">Phanerochaete chrysosporium is a white rot fungus which secretes a family of lignin-degrading enzymes under nutrient limitation. PSBL-1 is a mutant of this organism that generates the ligninolytic system under nonlimiting conditions during primary metabolism. Lignin peroxidase, manganese peroxidase, and glyoxal oxidase activities for PSBL-1 under nonlimiting conditions were 4- to 10-fold higher than those of the wild type (WT) under nitrogen-limiting conditions. PSBL-1 was still in the log phase of growth while secreting the enzymes, whereas the WT had ceased to grow by this time. As in the WT, manganese(II) increased manganese peroxidase activity in the mutant. However, manganese also caused an increase in lignin peroxidase and glyoxal oxidase activities in PSBL-1. Addition of veratryl alcohol to the culture medium stimulated lignin peroxidase activity, inhibited glyoxal oxidase activity, and had little effect on manganese peroxidase activity in PSBL-1, as in the WT. Fast protein liquid chromatography (FPLC) analysis shows production of larger amounts of isozyme H2 in PSBL-1 than in the WT. These properties make PSBL-1 very useful for isolation of large amounts of all ligninolytic enzymes for biochemical study, and they open the possibility of scale-up production for pratical use.</div>
</front>
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<Month>02</Month>
<Day>18</Day>
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<Title>Applied and environmental microbiology</Title>
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<Abstract><AbstractText>Phanerochaete chrysosporium is a white rot fungus which secretes a family of lignin-degrading enzymes under nutrient limitation. PSBL-1 is a mutant of this organism that generates the ligninolytic system under nonlimiting conditions during primary metabolism. Lignin peroxidase, manganese peroxidase, and glyoxal oxidase activities for PSBL-1 under nonlimiting conditions were 4- to 10-fold higher than those of the wild type (WT) under nitrogen-limiting conditions. PSBL-1 was still in the log phase of growth while secreting the enzymes, whereas the WT had ceased to grow by this time. As in the WT, manganese(II) increased manganese peroxidase activity in the mutant. However, manganese also caused an increase in lignin peroxidase and glyoxal oxidase activities in PSBL-1. Addition of veratryl alcohol to the culture medium stimulated lignin peroxidase activity, inhibited glyoxal oxidase activity, and had little effect on manganese peroxidase activity in PSBL-1, as in the WT. Fast protein liquid chromatography (FPLC) analysis shows production of larger amounts of isozyme H2 in PSBL-1 than in the WT. These properties make PSBL-1 very useful for isolation of large amounts of all ligninolytic enzymes for biochemical study, and they open the possibility of scale-up production for pratical use.</AbstractText>
</Abstract>
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<Country>United States</Country>
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Overproduction of lignin-degrading enzymes by an isolate of Phanerochaete chrysosporium.

Overproduction of lignin-degrading enzymes by an isolate of Phanerochaete chrysosporium.

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