Purification and Characterization of a Lectin Isolated from the Submerged Cultivated Mycelium of Grey Polypore Cerrena unicolor (Bull.) Murrill (Aphyllophoromycetideae)

Mikiashvili, Nona A.; Elisashvili, Vladimir; Worku, Mulumebet; Davitashvili, Elene; Isikhuemhen, Omoanghe S.

doi:10.1615/intjmedmushr.v11.i1.70

Cited by 5 publications

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“…Chromatofocusing was used to determine the isoelectric points for Cu CDH-FAD and Cu CDH, which were detected at pH 5.50 and 4.55, respectively. Many other intact CDHs from Basidiomycetes , such as P. chrysosporium , I. lacteus , T. versicolor , C. subvermispora , Phlebia lindtneri , and P. sanguineus , have acidic isoelectric points ranging from 3.0 to 5.1 [ 15 , 45 , 57 , 63 – 65 ]. The protein containing only the FAD domain has a higher pI (5.5–6.7) [ 45 , 63 , 64 ].…”

Section: Resultsmentioning

confidence: 99%

Characterization of Cellobiose Dehydrogenase from a Biotechnologically Important Cerrena unicolor Strain

Sulej

Janusz

Osińska-Jaroszuk

et al. 2015

Appl Biochem Biotechnol

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Cellobiose dehydrogenase (CDH), a secreted flavocytochrome produced by a number of wood-degrading fungi, was detected in the culture supernatant of a biotechnologically important strain of Cerrena unicolor grown in a modified cellulose-based liquid medium. The enzyme was purified as two active fractions: CuCDH-FAD (flavin domain) (1.51-fold) with recovery of 8.35 % and CuCDH (flavo-heme enzyme) (21.21-fold) with recovery of 73.41 %. As CDH from other wood-rotting fungi, the intact form of cellobiose dehydrogenase of C. unicolor is a monomeric protein containing one flavin and one heme b with molecular mass 97 kDa and pI = 4.55. The enzyme is glycosylated (8.2 %) mainly with mannose and glucosamine residues. Moreover, the cellobiose dehydrogenase gene cdh1 and its corresponding cDNA from the fungus C. unicolor were isolated, cloned, and characterized. The 2316-bp full-length cDNA of cdh1 encoded a mature CDH protein containing 771 amino acids preceded by a signal peptide consisting of 18 amino acids. Moreover, both active fractions were characterized in terms of kinetics, temperature and pH optima, and antioxidant properties.

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Section: Resultsmentioning

confidence: 99%

Characterization of Cellobiose Dehydrogenase from a Biotechnologically Important Cerrena unicolor Strain

Sulej

Janusz

Osińska-Jaroszuk

et al. 2015

Appl Biochem Biotechnol

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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%

“…Two N -acetyl- d -galactosamine-specific and one galactose-specific lectin fractions were isolated from the vegetative mycelium of Cerrena unicolor HAI 1095 and were characterized [ 7 ]. The ability of five strains of two Cerrena species ( C. maxima and C. unicolor ) to express hemagglutinating activity was evaluated in submerged fermentation of seven lignocellulosic materials of different chemical compositions [ 46 ].…”

Section: Intracellular Lectins From Mycelia Of Basidiomycetesmentioning

confidence: 99%

“…A variety of fungi, including members of the genera Armillaria , Agrocybe , Cerrena , Coprinus , Fomes , Funalia , Ganoderma , Grifola , Gymnopilus , Kuehneromyces , Lactarius , Lentinus , Laetipous , Panafolus , Pholiota , Pleurotus , Pseudotremella , Punctularia , Pycnoporus , Schizophyllum , Termitomyces , Trametes , Tricholoma , and Volvariella , can synthesize mycelial lectins. Most of these are intracellular [ 4 , 5 , 6 , 7 , 8 , 9 , 10 ], while others are associated with the surface of mycelial hyphae [ 11 , 12 , 13 ]. Some lectins are extracellular and are secreted into the growth medium during the fungal life cycle [ 4 , 14 , 15 , 16 ].…”

Section: Introductionmentioning

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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Purification and Characterization of a Lectin Isolated from the Submerged Cultivated Mycelium of Grey Polypore Cerrena unicolor (Bull.) Murrill (Aphyllophoromycetideae)

Cited by 5 publications

References 0 publications

Characterization of Cellobiose Dehydrogenase from a Biotechnologically Important Cerrena unicolor Strain

Characterization of Cellobiose Dehydrogenase from a Biotechnologically Important Cerrena unicolor Strain

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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