Evaluation of Higher Basidiomycetes Mushroom Lectin Activity in Submerged and Solid-State Fermentation of Agro-Industrial Residues

Davitashvili, Elene; Kapanadze, Ekaterine; Kachlishvili, Eva; Khardziani, Tamar; Elisashvili, Vladimir

doi:10.1615/intjmedmushr.v10.i2.80

Cited by 11 publications

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“…They have also been studied for biochemical reagents with valuable carbohydrate binding specificity (Horibe et al 2010). Owing to unique carbohydratebinding specificities of mushroom lectins, isolation of new lectins has been carried out by various workers (Mikiashvili et al 2006;Devitashvili et al 2008;Rouf et al 2011;Albores et al 2013). There are many reports on lectins from micromycetes and pathogenic fungi but their physiological role still remains uncertain (Tronchin et al 2002).…”

Section: Introductionmentioning

confidence: 99%

New lectins from aspergilli and their carbohydrate specificity

2013

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Lectin activity was assessed in sixteen Aspergillius species using human A, B, O, AB, rabbit, goat, pig and sheep erythrocytes. Neuraminidase and protease treated blood group O erythrocytes were also used to evaluate lectin activity from all the cultures unable to agglutinate native red blood cells. Lectin activity was revealed from Aspergillus acristatus, A. gorakhpurensis, A. panamensis and A. carbonarius extracts, while undiluted extract of A. fischeri showed weak haemagglutination. Lectin activity was expressed after 5 days of growth by A. acristatus, A. gorakhpurensis, A. panamensis and A. carbonarius and after 8 days of cultivation a sharp decline in lectin activity was observed. Higher titres were observed from these species with enzymatically modified blood type O erythrocytes. A variety of carbohydrates were used to study their minimum inhibitory concentration capable of inhibiting haemagglutination. Porcine stomach mucin was found to be the most potent inhibitor of all the lectins. A. gorakhpurensis lectin showed high specificity for chondroitin-6-sulphate and N-acetyl-D-galactosamine. Significant specificity for L-fucose, D-arabinose and 2-deoxy-D-ribose was identified with A. panamensis lectin. Low concentrations of 0.625 mM of D-galactosamine HCl and 0.12 mg/mL of chondroitin-6-sulphate were found optimal to prevent haemagglutination of A. carbonarius extract. A. carbonarius lectin was partially purified 2.75-fold using ammonium sulphate precipitation, dialysis and ultrafiltration. It was found to be stable upto 40• C and within the pH range of 7.0-8.0. Lectin activity was not affected by guanidine-HCl, while it was reduced to half after incubation with urea and thiourea after 24 h.

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Section: Introductionmentioning

confidence: 99%

New lectins from aspergilli and their carbohydrate specificity

2013

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“…This may indicate that changing of medium composition may affect the amount of lectin but did not affect the type of lectin. The ability to synthesize lectins is widespread among higher basidiomycetes and hemagglutinating activity is not only depending on species, but also is strain dependent (Mikiashvili et al, 2006;Davitashvili et al, 2008;Mikiashvili et al, 2009;Davitashvili et al, 2011;Davitashvili et al, 2015). P. ostreatus fruiting bodies exhibited the highest lectin specific activity.…”

Section: Screening Of Different Mushroom Species Belonging To Genus Pleurotus For Lectin Productionmentioning

confidence: 99%

Purification, Molecular and Biochemical Characterization and Biological Applications of Hemagglutinating Lectin With Anticancer Activities From Pleurotus Ostreatus

Kamel¹,

Khalil²,

Atalla³

et al. 2021

PLANT ARCHIVES

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Three Pleurotus species were screened for their ability to synthesize mycelial, culture filtrate and fruiting bodies lectins. All tested Pleurotus species were able to synthesize mycelial and fruiting bodies lectins but with different degree of activity, while no extracellular lectin was detected. P. ostreatus Lectin (POL) from its fruiting bodies recorded the highest activity, so it was selected for further studies. Partial sequencing of lectin gene and partial amino acid sequencing were performed, resulting in 267 amino acids. POL purification involved a combination of (NH 4 ) 2 SO 4 precipitation along with two anion-chromatographic steps using Q-Sepharose column and Mono Q column. POL appeared as a single band with a molecular mass of 29 kDa on SDS-PAGE. Biochemical and biological activities of pure POL were compared with crude extract from the same organism. POL activity was inhibited by xylose with a MIC of 0.1 M. It was active up to 70ºC and pH 11 then its activity completely disappeared. POL activity was inhibited by different concentrations of Hg 2+ , Zn 2+ , Cu 2+ , Mn 2+ , Ca 2+ , Na + and K + ions. POL manifested antibacterial activity, but showed no antifungal activity. It exhibited anticancer activity toward human hepatocellular and colorectal carcinoma with IC 50 of 424 and 270 µg/ml, respectively.

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“…Several large-scale studies of lectin activity in mycelia and fruit bodies of various basidiomycete species and strains grown by different methods have been made by Davitashvili, Mikiashvili, and their coauthors [ 7 , 8 , 44 , 45 , 46 , 47 ]. The lectin activity of extracts from the fruit bodies of medicinal and edible mushrooms (13 species), as well as from mycelia grown in liquid culture (6 species, 9 strains) and on malt extract agar (11 species, 23 strains) was evaluated by hemagglutination with rabbit erythrocytes [ 44 ].…”

Section: Intracellular Lectins From Mycelia Of Basidiomycetesmentioning

confidence: 99%

“…In another study, 21 strains of higher basidiomycetes belonging to 16 species of different taxonomic and ecological groups were compared for their lectin activity in submerged and solid-state fermentation of agroindustrial wastes or byproducts [ 45 ]. Absent or very low hemagglutinating activity was found in Bjerkandera adusta , Lentinus edodes , Lenzites varnieri , Postia tephroleuca , Trametes ochracea , and T. versicolor .…”

Section: Intracellular Lectins From Mycelia Of Basidiomycetesmentioning

confidence: 99%

“…In a study involving 21 strains of 16 basidiomycete species grown by different methods, several species were found to accumulate proteins with hemagglutinating activity in both culture liquids and mycelial extracts [ 45 ]. Moreover, during submerged fermentation of lignocellulose by Cerrena unicolor IBB 301 and Trametes versicolor IBB 775, the specific hemagglutinating activity was much higher in the culture liquid than it was in the fungal biomass.…”

Section: Extracellular Lectinsmentioning

confidence: 99%

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Lectins from Mycelia of Basidiomycetes

Никитина

Loshchinina

Ветчинкина

2017

IJMS

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Lectins are proteins of a nonimmunoglobulin nature that are capable of specific recognition of and reversible binding to the carbohydrate moieties of complex carbohydrates, without altering the covalent structure of any of the recognized glycosyl ligands. They have a broad range of biological activities important for the functioning of the cell and the whole organism and, owing to the high specificity of reversible binding to carbohydrates, are valuable tools used widely in biology and medicine. Lectins can be produced by many living organisms, including basidiomycetes. Whereas lectins from the fruit bodies of basidiomycetes have been studied sufficiently well, mycelial lectins remain relatively unexplored. Here, we review and comparatively analyze what is currently known about lectins isolated from the vegetative mycelium of macrobasidiomycetes, including their localization, properties, and carbohydrate specificities. Particular attention is given to the physiological role of mycelial lectins in fungal growth and development.

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Evaluation of Higher Basidiomycetes Mushroom Lectin Activity in Submerged and Solid-State Fermentation of Agro-Industrial Residues

Cited by 11 publications

References 0 publications

New lectins from aspergilli and their carbohydrate specificity

New lectins from aspergilli and their carbohydrate specificity

Purification, Molecular and Biochemical Characterization and Biological Applications of Hemagglutinating Lectin With Anticancer Activities From Pleurotus Ostreatus

Lectins from Mycelia of Basidiomycetes

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