Laccase-type phenoloxidase in salivary glands and watery saliva of the green rice leafhopper, Nephotettix cincticeps

Hattori, Makoto; Konishi, Hirosato; Tamura, Yasumori; Konno, Kotaro; Sogawa, Kazushige

doi:10.1016/j.jinsphys.2005.08.010

Cited by 68 publications

(74 citation statements)

References 32 publications

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“…Accordingly, we found that PO-like activity from plasma was inhibited by PTU, DETC, and, to a lesser extent, by SHAM and tropolone. PTU was previously described as an inhibitor of tyrosinases and catecholases [38] but also as an inhibitor of laccases [25,39]. It contains a sulphur compound that binds copper at the active site of catecholase [40].…”

Section: Discussionmentioning

confidence: 99%

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First evidence of laccase activity in the Pacific oyster Crassostrea gigas

Luna‐Acosta¹,

Rosenfeld²,

Amari³

et al. 2010

Fish & Shellfish Immunology

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Phenoloxidases (POs) are a family of enzymes including tyrosinases, catecholases and laccases, which play an important role in immune defence mechanisms in various invertebrates. The aim of this study was to thoroughly identify the PO-like activity present in the hemolymph of the Pacific oyster Crassostrea gigas, by using different substrates (i.e. dopamine and p-phenylenediamine, PPD) and different PO inhibitors. In order to go deeper in this analysis, we considered separately plasma and hemocyte lysate supernatant (HLS). In crude plasma, oxygraphic assays confirmed the presence of true oxidase activities. Moreover, the involvement of peroxidase(s) was excluded. In contrast to other molluscs, no tyrosinase-like activity was detected. With dopamine as substrate, PO-like activity was inhibited by the PO inhibitors tropolone, phenylthiourea (PTU), salicylhydroxamic acid and diethyldithio-carbamic acid, by a specific inhibitor of tyrosinases and catecholases, i.e. 4-hexylresorcinol (4-HR), and by a specific inhibitor of laccases, i.e. cetyltrimethylammonium bromide (CTAB). With PPD as substrate, PO-like activity was inhibited by PTU and CTAB. In precipitated protein fractions from plasma, and with dopamine and PPD as substrates, PTU and 4-HR, and PTU and CTAB inhibited PO-like activity, respectively. In precipitated protein fractions from hemocyte lysate supernatant, PTU and CTAB inhibited PO-like activity, independently of the substrate. Taken together, these results suggest the presence of both catecholase- and laccase-like activities in plasma, and the presence of a laccase-like activity in HLS. To the best of our knowledge, this is the first time that a laccase-like activity is identified in a mollusc by using specific substrates and inhibitors for laccase, opening new perspectives for studying the implication of this enzyme in immune defence mechanisms of molluscs of high economic value such as C. gigas.

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Section: Discussionmentioning

confidence: 99%

“…Plasma (10 ml) was preincubated at 25 C for 30 min in the presence of 10 ml of catalase from bovine liver at 1000 U/ml [25]. The total scavenging of H 2 O 2 was verified using the Catalase kit CAT-100 (Sigma) and specifications included (data not shown).…”

Section: Hydrogen Peroxide Scavenging By Exogenous Catalasementioning

confidence: 99%

First evidence of laccase activity in the Pacific oyster Crassostrea gigas

Luna‐Acosta¹,

Rosenfeld²,

Amari³

et al. 2010

Fish & Shellfish Immunology

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“…It was first isolated from the sap of Japanese lacquer tree Rhus vernicifera (Yoshida 1883) and are widely distributed in nature being found in plants, fungi, insects (Hattori et al 2005), and bacteria. First bacterial laccase was discovered in Azospirillum lipoferum (Givaudan et al 1993).…”

Section: Introductionmentioning

confidence: 99%

Fungal laccase discovered but yet undiscovered

Agrawal

Chaturvedi

Verma

2018

Bioresour. Bioprocess.

176

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Laccases belongs to multinuclear copper-containing oxidase and can act on a variety of aromatic and non-aromatic compounds. Due to their broad substrate specificity, they are considered as a promising candidate in various industrial and biotechnological sectors. They are regarded as a "Green Tool"/"Green Catalyst" in biotechnology. The present review focuses on structure, reaction mechanism, categories, applications, economic feasibility, limitations, and future prospects of fungal laccases. Thus, this review would help in understanding laccases along with the areas, which has not been focused and requires attention. Since past, immense work has been carried out on laccases: yet, new discoveries and application are ever increasing which includes bio-fuel, bio-sensor, fiber board synthesis, bioremediation, clinical, textile industry, food, cosmetics, and many more. Hence, it can be stated that fungal laccase is an enzyme which is "discovered but yet undiscovered".

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“…Laccases were Wrst detected in the juice of the lacquer tree, Rhus vernicifera, and were sequentially found in fungi, insects, and bacteria, whereas the most popular laccase producers were white-rot fungi [1,6,7,9,16]. In recent years, some other potential laccase producers were found, including diVerent genera of basidiomycetes, ascomycetes, and some deuteromycetes.…”

Section: Introductionmentioning

confidence: 99%

A newly isolated Paecilomyces sp. WSH-L07 for laccase production: isolation, identification, and production enhancement by complex inducement

Liu

Zhang

Hua

et al. 2009

J Ind Microbiol Biotechnol

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Laccase can catalyze the oxidation of a wide range of organic and inorganic substrates. In this study, an easily detectable method was employed for screening laccase-producing microorganisms by using 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonate) (ABTS) as laccase-secretion indicator. A novel laccase-producing strain was isolated and identified as Paecilomyces sp. WSH-L07 according to the morphological characteristics and the comparison of internal transcribed spacer (ITS) ribosomal DNA (rDNA) gene sequences. In further investigation, the production of laccase by Paecilomyces sp. WSH-L07 was greatly enhanced by the nontoxic inducers of copper sulphate and methylene blue. Under the induction of 50 microM copper sulphate and 20 microM methylene blue, the maximum laccase production was obtained. When these inducers were added into cultivation medium at 24 h and 12 h, respectively, an increment of about 100 times of laccase activity compared with that of in inducer-free medium and about two times of that of in single copper-supplemented medium was observed. Compared with other Paecilomyces species, Paecilomyces sp. WSH-L07 exhibit the better laccase-producing characteristics with an activity of 1,650 U/l on the eighth day, suggesting its potential ability for industrial application.

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Laccase-type phenoloxidase in salivary glands and watery saliva of the green rice leafhopper, Nephotettix cincticeps

Cited by 68 publications

References 32 publications

First evidence of laccase activity in the Pacific oyster Crassostrea gigas

First evidence of laccase activity in the Pacific oyster Crassostrea gigas

Fungal laccase discovered but yet undiscovered

A newly isolated Paecilomyces sp. WSH-L07 for laccase production: isolation, identification, and production enhancement by complex inducement

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