1994
DOI: 10.1128/aem.60.3.960-965.1994
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Lignin-Degrading Enzymes of the Commercial Button Mushroom, Agaricus bisporus

Abstract: Agaricus bisporus, grown under standard composting conditions, was evaluated for its ability to produce lignin-degrading peroxidases, which have been shown to have an integral role in lignin degradation by wood-rotting fungi. The activity of manganese peroxidase was monitored throughout the production cycle of the fungus, from the time of colonization of the compost through the development of fruit bodies. Characterization of the enzyme was done with a crude compost extract. Manganese peroxidase was found to h… Show more

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Cited by 127 publications
(48 citation statements)
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“…The conclusions drawn from this observation were that laccases and, veratryl alcohol too, played a role in the physiological development of the basidiocarp. A role for laccases during fruit body formation has also been observed in A. bisporus [18].…”
Section: Laccase Production During Mushroom Developmentmentioning
confidence: 72%
“…The conclusions drawn from this observation were that laccases and, veratryl alcohol too, played a role in the physiological development of the basidiocarp. A role for laccases during fruit body formation has also been observed in A. bisporus [18].…”
Section: Laccase Production During Mushroom Developmentmentioning
confidence: 72%
“…during the vegetative phase, appeared to be dependent on a moderate production of enzyme activities degrading lignocellulose and microbial products. The extracellular enzymes assayed in the present work are all known to be produced by commercial strains of A. bisporus in compost or in liquid media [25,26], but enzyme production in compost by newly isolated wild strains has not been reported before. A contribution to the definition of the adaptation to mushroom compost is presented here.…”
Section: Discussionmentioning
confidence: 91%
“…The enzyme activity was expressed in IU where one unit of Lignin Peroxidase corresponded to the amount of enzyme that oxidized one micromole of veratryl alcohol per min [33]. Manganese Peroxidase activity was quantified using a reaction mixture containing crude enzyme 1mM guaiacol, 10mM citrate phosphate buffer (pH 5.5), 1mM MnSO4, and 50 µM H 2 O 2 in a total volume of 1 ml [34]. The reaction was monitored by measuring the increase in absorbance of the reaction product at 465 nm.…”
Section: Enzyme Assaysmentioning
confidence: 99%