JOURNAL ARTICLE

Aryl alcohol oxidases from the white-rot basidiomycete Pleurotus ostreatus

Kenji OkamotoHideshi Yanase

Year: 2002 Journal:   Mycoscience Vol: 43 (5)Pages: 391-395   Publisher: Elsevier BV

Abstract

Three aryl alcohol oxidases (AAOs; EC 1.1.3.7) I, II, and III from the culture filtrate of a strain of white-rot fungus Pleurotus ostreatus were purified by multistep chromatography. Each of the purified AAOs I, II, and III had the same molecular masses of 70kDa and 72kDa on gel filtration chromatography and sodium dodecyl sulfatepolyacrylamide gel electrophoresis, respectively. Their optimum temperature was 40°C, but their optimum pHs differed slightly. The N-terminal amino acid sequence of AAOs I, II, and III was determined to be Ala-Asp-Lys- Asp-Tyr-Ile-Val-Val-Gly-Ala, which showed significant similarity to those of Pleurotus eryngii (80% identity) and Pleurotus ostreatus Florida (60% identity)

Keywords:
Pleurotus ostreatus Pleurotus eryngii Pleurotus Gel electrophoresis Size-exclusion chromatography Biology Chromatography Mycelium Biochemistry Chemistry Food science Botany Mushroom Enzyme

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Citation History

Topics

Fungal Biology and Applications
Health Sciences →  Medicine →  Pharmacology
Enzyme-mediated dye degradation
Life Sciences →  Agricultural and Biological Sciences →  Plant Science
Chemical synthesis and alkaloids
Physical Sciences →  Chemistry →  Organic Chemistry
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