Differential production of extracellular laccase in the Dutch elm disease pathogens Ophiostoma ulmi and O. novo-ulmi

Binz, Thomas; Canevascini, Giorgio

doi:10.1016/s0953-7562(96)80213-9

Cited by 30 publications

(14 citation statements)

References 30 publications

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“…The extracel1ular cyanobacterial laccase exhibit strong binding with DEAE cellulose column and elution was done at 0.2 M NaCI gradient. Laccases show variable binding and many studies have also reported the elution from 0.1 M to 0.3 M NaCl gradient [26]. Previously laccase purification was reported from fungi Pleurotus sajor - caju MTCC 141 with 10.71 fold and 3.46% yield while in bacteria 28.46 fold purification of laccase from Bacillus tequilensis SN4 with 13.34% yield was reported [27, 28].…”

Section: Resultsmentioning

confidence: 99%

A novel multicopper oxidase (laccase) from cyanobacteria: Purification, characterization with potential in the decolorization of anthraquinonic dye

et al. 2017

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A novel extracellular laccase enzyme produced from Spirulina platensis CFTRI was purified by ultrafiltration, cold acetone precipitation, anion exchange and size exclusion chromatography with 51.5% recovery and 5.8 purification fold. The purified laccase was a monomeric protein with molecular mass of ~66 kDa that was confirmed by zymogram analysis and peptide mass fingerprinting. The optimum pH and temperature of the enzyme activity was found at 3.0 and 30°C using ABTS as substrate but the enzyme was quite stable at high temperature and alkaline pH. The laccase activity was enhanced by Cu+2, Zn+2 and Mn+2. In addition, the dye decolorization potential of purified laccase was much higher in terms of extent as well as time. The purified laccase decolorized (96%) of anthraquinonic dye Reactive blue- 4 within 4 h and its biodegradation studies was monitored by UV visible spectra, FTIR and HPLC which concluded that cyanobacterial laccase can be efficiently used to decolorize synthetic dye and help in waste water treatment.

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Section: Resultsmentioning

confidence: 99%

A novel multicopper oxidase (laccase) from cyanobacteria: Purification, characterization with potential in the decolorization of anthraquinonic dye

et al. 2017

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“…Laccase from Cryphonectria parasitica, which causes chestnut blight, is thought to be responsible for the detoxification of tannins in chestnut bark [101,102]. It has been reported that Ophiostoma ulmi and Ophiostoma novo ulmi, both vascular wilt pathogens and causative agents of Dutch elm disease, can be differentiated by their potential to produce extracellular laccase [103]. O. novo ulmi is a strong pathogen on native North American and European elm [104] and produce high amount of laccase.…”

Section: Morphogenesismentioning

confidence: 99%

Ligninolytic Fungal Laccases and Their Biotechnological Applications

Arora

Sharma

2009

Appl Biochem Biotechnol

321

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Lignin is amorphous in nature, lacks stereoregularity, and is not susceptible to hydrolytic attack. Despite its resistant nature, it is however degraded by various microorganisms, particularly, white-rot fungi. Such fungi are capable of extracellular production of lignin peroxidase, manganese peroxidase, and laccase, the three major enzymes associated with ligninolysis. Though all white-rot fungi do not produce all the three enzymes, laccase occupies an important place in ligninolysis. Laccase belongs to a diverse group of enzymes called oxidoreductases and is also known as benzenediol: oxygen oxidoreductase. They have low substrate specificity. The copper-containing enzyme laccase has been detected in a variety of organisms such as bacteria, fungi, plants, and insects. Mostly, these are extracellular proteins, although intracellular laccases have also been detected in some fungi and insects. Fungal laccases are believed to play a variety of roles, such as, morphogenesis, pathogenesis, and lignin degradation. As an oxidase, laccase is used in many agricultural, industrial, and medicinal applications. Current investigations are focused on laccase-based biooxidation, biotransformation, biosensor, and enzymatic synthesis of organic compounds. By enhancing laccase production using different physiochemical parameters, better understanding of the mechanism for the reactions of interest, and optimizing the catalytic activity of laccase, it can be used in a better way in diverse fields of biotechnology.

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“…The use of pheromone traps for vector control has great attraction from an environmental point of view. However, it did not gain the expected momentum because the results were not as anticipated (Birch et al 1981, Sticklen et al 1991. Lanier (1989) reported on the usefulness of elm bark beetle trap trees for control of DED.…”

Section: Reduction Of Vector Populationsmentioning

confidence: 99%

“…Assumptions (based on circumstantial evidence) have been made that toxins, such as cerato ulmin (CU) (Takai 1980, Richards 1993, peptidorhamno-mannan (Claydon et al 1980, Nordin and Strobel 1981, Scheffer 1983, Scheffer et al 1987, glycopeptides and glycoprotein elicitors (Yang et al 1989) may function as factors of virulence. Binz and Canevascini (1996) stated that production of extra-cellular laccase may be important for the survival of the fungus in its host. Confirmation of these compounds as factors of virulence is still waiting.…”

Section: Fungal Metabolites As Factors Of Virulencementioning

confidence: 99%

The American elm and Dutch elm disease

Hubbes¹

1999

The Forestry Chronicle

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Shortly after World War I, a new disease previously unknown among elms emerged in Holland. It spread rapidly from Europe to Great Britain (1927), United States (1930), and Canada (1945), killing millions of elms. The disease known, as Dutch elm disease (DED) is a wilt disease, caused by the fungus Ophiostoma ulmi. It is transmitted from tree to tree by elm bark beetles (scolytid) vectors. Numerous attempts to control the disease have concentrated on the reduction of insect vector populations, exploitation of natural host resistance, extensive application of fungicides and integrated pest management. In spite of these efforts in Canada, the disease continues to migrate westwards threatening the elm populations in Saskatchewan and Alberta. Today there are approximately 700 000 elm shade trees in cities and towns across Canada and their value exceeds $2.5 billion dollars.With the advance of molecular biology new, powerful tools are now available to study, in greater detail, the molecular and biochemical mechanisms of the DED pathogen, with particular reference to the mechanisms that induce host defenses. A glycoprotein has been isolated and identified such that when injected either in liquid or pellet form into the elm tree, significantly reduced the wilting symptoms of both five-year old elm seedlings and 10 cm diameter trees. The elicitor induces a chain of defensive reactions that prevent the rapid spread of the fungus within the vascular system of the host. Key words: Ophiostoma ulmi, elm bark beetle vectors, induced resistance, chemical control, RFLP, mitochondrial DNA, ribosomal DNA, virus-like DNA, resistance breeding

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Differential production of extracellular laccase in the Dutch elm disease pathogens Ophiostoma ulmi and O. novo-ulmi

Cited by 30 publications

References 30 publications

A novel multicopper oxidase (laccase) from cyanobacteria: Purification, characterization with potential in the decolorization of anthraquinonic dye

A novel multicopper oxidase (laccase) from cyanobacteria: Purification, characterization with potential in the decolorization of anthraquinonic dye

Ligninolytic Fungal Laccases and Their Biotechnological Applications

The American elm and Dutch elm disease

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