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Literature DB >> 19352024

Purification and characterization of an extracellular laccase from Phlebia radiata strain BP-11-2 that decolorizes fungal melanin.

Shuji Kaneko¹, Minyi Cheng, Hiroshi Murai, Shinji Takenaka, Shuichiro Murakami, Kenji Aoki.

Abstract

Phlebia radiata strain BP-12-2, isolated from forest soil, decolorized fungal melanin and produced an extracellular laccase in culture. The enzyme was purified to homogeneity and characterized. It showed no absorption bands in the ultraviolet above 300 nm or visible regions. It differed from the reported laccases in substrate specificity, kinetic parameters, and NH2-terminal amino acid sequences.

Entities: Chemical Species

Mesh：

Substances：
Melanins
Laccase

Year: 2009 PMID： 19352024 DOI： 10.1271/bbb.80740

Source DB: PubMed Journal: Biosci Biotechnol Biochem ISSN： 0916-8451 Impact factor: 2.043

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Cited

5 in total

Review 1. Laccases: a never-ending story.

Authors: Paola Giardina; Vincenza Faraco; Cinzia Pezzella; Alessandra Piscitelli; Sophie Vanhulle; Giovanni Sannia
Journal: Cell Mol Life Sci Date: 2009-10-22 Impact factor: 9.261

5. "Yellow" laccase from Sclerotinia sclerotiorum is a blue laccase that enhances its substrate affinity by forming a reversible tyrosyl-product adduct.

Authors: Augustin C Mot; Cristina Coman; Niculina Hadade; Grigore Damian; Radu Silaghi-Dumitrescu; Hendrik Heering
Journal: PLoS One Date: 2020-01-21 Impact factor: 3.240

5 in total

Purification and characterization of an extracellular laccase from Phlebia radiata strain BP-11-2 that decolorizes fungal melanin.

Review 1. Laccases: a never-ending story.

2. Decolorization of synthetic melanins by crude laccases of Lentinus polychrous Lév.

3. Production and characterization of crude laccase from Irpex sp. JS7 that decolorizes synthetic and natural melanin.

4. A multicopper oxidase-related protein is essential for insect viability, longevity and ovary development.

5. "Yellow" laccase from Sclerotinia sclerotiorum is a blue laccase that enhances its substrate affinity by forming a reversible tyrosyl-product adduct.