Purification and Characterization of an Extracellular Laccase from<i>Phlebia radiata</i>Strain BP-11-2 That Decolorizes Fungal Melanin

Kaneko, Shuji; Cheng, Minyi; Murai, Hiroshi; Takenaka, Shinji; Murakami, Shinichiro; Aoki, Kenji

doi:10.1271/bbb.80740

Cited by 26 publications

(7 citation statements)

References 20 publications

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“…Thus, the presence of 1 mM Zn 2+ or Fe 2+ in the textile wastewater decreased level of T. hirsuta Lac activity in 20% and 35%, respectively, while inhibition was much intensive at concentration of 10 mM [17]. Inhibition of Lac activity in the presence of 1 mM Zn 2+ was also reported in L. edodes and G. lucidum [13,18], while the same concentration has not caused any effect in Phlebia radiata during melanin decolorization contrary to 1 mM Fe 2+ or Fe 3+ , which completely inhibited Lac activity [19].…”

Section: Resultsmentioning

confidence: 97%

Interaction of Trace Elements and Ligninolytic Enzymes in Pleurotus eryngii

Stajić

Vukojević

2010

Biol Trace Elem Res

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Considering the fact that some trace elements have influence on the growth and physiological processes in the fungi, the aim of this study was to resolve the question of whether Fe, Zn, and Se, added to the medium in the different forms, affect activity of selected Pleurotus eryngii ligninolytic enzymes participating in mandarine peels submerged fermentation. Compared with the control, Fe and Zn showed stimulatory effect on laccase activity. Reduction in the activity was emphasized with cultivation time, but it was slower in the presence of Zn than in the presence of Fe. Among studied Se forms, SeO2 was the most unfavorable Se source for laccase activity. All tested trace elements, independent on form, showed stimulatory effect on the activity of Mn-oxidizing peroxidases on the seventh day of cultivation. Based on the results, it could be concluded that the presence of the tested trace elements can advance various biotechnological processes among which is biodegradation of agricultural wastes, potential environmental pollutants.

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Section: Resultsmentioning

confidence: 97%

Interaction of Trace Elements and Ligninolytic Enzymes in Pleurotus eryngii

Stajić

Vukojević

2010

Biol Trace Elem Res

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“…The enzyme contains only one copper atom/molecule instead of the usual four, along with two zinc atoms and one iron atom in each protein molecule. Other so-called white laccases were purified from Pycnoporous sanguineus [135], from T. hirsuta [136], and from P. radiata BP-11-2 [137]. The analysis of metal ion contents of the laccase from T. hirsuta has shown the presence of copper and manganese in a 3:1 ratio.…”

Section: Laccases With Unusual Spectral Propertiesmentioning

confidence: 99%

Laccases: a never-ending story

Giardina¹,

Faraco²,

Pezzella³

et al. 2009

Cell. Mol. Life Sci.

866

638

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Laccases (benzenediol:oxygen oxidoreductases, EC 1.10.3.2) are blue multicopper oxidases that catalyze the oxidation of an array of aromatic substrates concomitantly with the reduction of molecular oxygen to water. In fungi, laccases carry out a variety of physiological roles during their life cycle. These enzymes are being increasingly evaluated for a variety of biotechnological applications due to their broad substrate range. In this review, the most recent studies on laccase structural features and catalytic mechanisms along with analyses of their expression are reported and examined with the aim of contributing to the discussion on their structure-function relationships. Attention has also been paid to the properties of enzymes endowed with unique characteristics and to fungal laccase multigene families and their organization.

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“…A colorless laccase, termed as "white laccase", purified from Pleurotus ostreatus was reported to contain only one copper atom/molecule with the other two coppers replaced by two zinc and one iron ions. [25] Other 'white' laccases were purified from Pycnoporous sanguineus [26], from Trametes hirsuta [27], and from Phlebia radiata BP-11-2 [28]. In the T. hirsuta white laccase, one copper atom was replaced by manganese.…”

Section: Introductionmentioning

confidence: 99%

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

et al. 2020

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Yellow laccases lack the typical blue type 1 Cu absorption band around 600 nm; however, multi-copper oxidases with laccase properties have been reported. We provide the first evidence that the yellow laccase isolated from Sclerotinia sclerotiorum is obtained from a blue form by covalent, but nevertheless reversible modification with a phenolic product. After separating the phenolics from the extracellular medium, a typical blue laccase is obtained. With ABTS as model substrate for this blue enzyme, a non-natural purple adduct is formed with a spectrum nearly identical to that of the 1:1 adduct of an ABTS radical and Tyr. This modification significantly increases the stability and substrate affinity of the enzyme, not by acting primarily as bound mediator, but by structural changes that also alters the type 1 Cu site. The HPLC-MS analyses of the ABTS adduct trypsin digests revealed a distinct tyrosine within a unique loop as site involved in the modification of the blue laccase form. Thus, S. sclerotiorum yellow laccase seems to be an intrinsically blue multi-copper oxidase that boosts its activity and stability with a radical-forming aromatic substrate. This particular case could, at least in part, explain the enigma of the yellow laccases.

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Purification and Characterization of an Extracellular Laccase fromPhlebia radiataStrain BP-11-2 That Decolorizes Fungal Melanin

Cited by 26 publications

References 20 publications

Interaction of Trace Elements and Ligninolytic Enzymes in Pleurotus eryngii

Interaction of Trace Elements and Ligninolytic Enzymes in Pleurotus eryngii

Laccases: a never-ending story

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

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