scholarly journals Purification of Extracellular Laccase from Rhizoctonia praticola

10.5109/19530 ◽  
2011 ◽  
Vol 56 (1) ◽  
pp. 1-7
Author(s):  
Jerzy Rogalski ◽  
Grzegorz Janusz ◽  
Dorota Legiec ◽  
Soo-Jeong Shin ◽  
Shoji Ohga
Keyword(s):  
Extracellular Laccase ◽  
Rhizoctonia Praticola

Production of induced laccase by the fungus Rhizoctonia praticola

1986 ◽  
Vol 32 (11) ◽  
pp. 867-870 ◽  
Author(s):  
Kay L. Shuttleworth ◽  
Lori Postie ◽  
Jean-Marc Bollag
Keyword(s):  
Gel Electrophoresis ◽  
Inductive Effect ◽  
Laccase Production ◽  
Growth Media ◽  
Benzoic Acids ◽  
Substituted Phenols ◽  
Ph Optimum ◽  
Extracellular Laccase ◽  
Rhizoctonia Praticola

The ability of the fungus Rhizoctonia praticola to produce an induced extracellular laccase was examined. Potential inducers, including substituted phenols, anilines, and benzoic acids, were added at a concentration of 1 mM to the growth media of fungal cultures. Of the 11 compounds tested, 5 were found to have an inductive effect. The most effective inducer, p-anisidine (p-methoxyaniline), stimulated laccase production by a factor of 30. Other parameters which influenced the production of laccase were temperature, condition of the mycelia at the time of the induction, and the concentration of the inducer. A comparison of the p-anisidine induced laccase with the constitutive laccase showed noticeable similarities in Km, pH optimum, and mobility in gel electrophoresis, suggesting that the two enzymes may be similar.

scholarly journals Laccase Immobilisation on Mesostructured Silicas

2012 ◽  
Vol 33 (4) ◽  
pp. 611-620 ◽  
Author(s):  
Jolanta Bryjak ◽  
Katarzyna Szymańska ◽  
Andrzej B. Jarzębski
Keyword(s):  
Thermal Inactivation ◽  
Mesoporous Silicas ◽  
Native Enzyme ◽  
Covalent Attachment ◽  
Initial Activity ◽  
Ordered Mesoporous ◽  
Extracellular Laccase ◽  
Activity Loss ◽  
Activity Decay ◽  
Hexagonally Ordered

Extracellular laccase produced by the wood-rotting fungus Cerrena unicolor was immobilised covalently on the mesostructured siliceous foam (MCF) and three hexagonally ordered mesoporous silicas (SBA-15) with different pore sizes. The enzyme was attached covalently via glutaraldehyde (GLA) or by simple adsorption and additionally crosslinked with GLA. The experiments indicated that laccase bound by covalent attachment remains very active and stable. The best biocatalysts were MCF and SBA-15 with Si-F moieties on their surface. Thermal inactivation of immobilised and native laccase at 80°C showed a biphasic-type activity decay, that could be modelled with 3- parameter isoenzyme model. It appeared that immobilisation did not significantly change the mechanism of activity loss but stabilised a fraction of a stable isoform. Examination of time needed for 90% initial activity loss revealed that immobilisation prolonged that time from 8 min (native enzyme) up to 155 min (SBA-15SF).

Enhanced Formation of Extracellular Laccase Activity by the White-Rot Fungus Trametes multicolor

2002 ◽  
pp. 229-241 ◽  
Author(s):  
Johann Hess ◽  
Christian Leitner ◽  
Christiane Galhaup ◽  
Klaus D. Kulbe ◽  
Barbara Hinterstoisser ◽  
...  
Keyword(s):  
Laccase Activity ◽  
White Rot ◽  
White Rot Fungus ◽  
Extracellular Laccase ◽  
Trametes Multicolor

scholarly journals Temporal profiles of intra- and extracellular laccase isoenzymes from Pleurotus ostreatus produced in submerged and solid-state cultures

2016 ◽  
Vol 15 (22) ◽  
pp. 1069-1077 ◽  
Author(s):  
Armas Tizapantzi Anah iacute ◽  
Cuatecontzi Cuautle Elizet ◽  
J Fern aacute ndez Francisco ◽  
Estrada Torres Arturo ◽  
oacute nica Montiel Gonz Alba
Keyword(s):  
Solid State ◽  
Pleurotus Ostreatus ◽  
Extracellular Laccase ◽  
Temporal Profiles

Purification and characterization of extracellular laccase from Pleurotus ostreatus

Mycoscience ◽  
2000 ◽  
Vol 41 (1) ◽  
pp. 7-13 ◽  
Author(s):  
Kenji Okamoto ◽  
Sonoe O. Yanagi ◽  
Takuo Sakai
Keyword(s):  
Pleurotus Ostreatus ◽  
Purification And Characterization ◽  
Extracellular Laccase

scholarly journals Cyclic Dipeptides Mediating Quorum Sensing and Their Biological Effects in Hypsizygus Marmoreus

Biomolecules ◽  
2020 ◽  
Vol 10 (2) ◽  
pp. 298
Author(s):  
Shu-Jing Sun ◽  
Yun-Chao Liu ◽  
Cai-Hong Weng ◽  
Shi-Wei Sun ◽  
Fan Li ◽  
...  
Keyword(s):  
Quorum Sensing ◽  
Biological Effects ◽  
Fruit Body ◽  
Symbiotic Bacterium ◽  
Hyphal Growth ◽  
Hypsizygus Marmoreus ◽  
Cyclic Dipeptides ◽  
Body Development ◽  
Extracellular Laccase ◽  
Peptide Synthetase

A novel quorum sensing (QS) system was discovered in Serratia odorifera, the symbiotic bacterium of Hypsizygus marmoreus. This system uses cyclo(Pro-Phe), cyclo(Pro-Tyr), cyclo(Pro-Val), cyclo(Pro-Leu), cyclo(Tyr-Leu), and cyclo(Tyr-Ile) as autoinducers. This discovery is the first attempt to characterize cyclic dipeptides as QS signaling molecules in S. odorifera and improves the classical QS theory. Significantly, except for cyclo(Tyr-Leu), these QS autoinducers can increase the transcription level of lignin-degrading enzyme genes of H. marmoreus. The cyclo(Pro-Phe) can increase the activity of extracellular laccase (1.32-fold) and manganese peroxidase (20%), which may explain why QS potentially regulates the hyphal growth, primordium formation, and fruit body development of H. marmoreus. Furthermore, it was demonstrated that the cyclo(Tyr-Ile) biosynthesis in S. odorifera was catalyzed by the nonribosomal peptide synthetase (NRPS). This study supports exploring the growth and development of H. marmoreus promoted by its symbiotic bacteria at QS signal transduction level.

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