Physicochemical properties of micromycetes Alternaria alternate 4 lectin

The physicochemical properties of the lectin of the lower fungus, micromycetes Alternaria alternate 4 have been studied. It was found that the lectin of the micromycetes Alternaria alternate 4 is stable over a wide range of temperatures and pH values (5-70oC and pH 6.0-9.0). The greatest activity of lectin was observed at a temperature of 5-50 °C and a pH of 6.5-8.5. The increased activity of Alternaria alternate 4 lectin was facilitated by the presence of divalent Ca2+, Mn2+, and Zn2+ ions in the reaction mixture, which indicates that Alternaria alternate 4 lectin is a metal-dependent glycoprotein. Alternaria alternate 4 lectin had the ability to bind simple carbohydrates. The activity of Alternaria alternate 4 lectin was inhibited to a greater extent by galactose, which indicates that Alternaria alternate 4 lectin belongs to the group of galactose-binding lectins.

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Publication Details

Journal
GSC Advanced Research and Reviews
Published
2025-06-21
DOI
https://doi.org/10.30574/gscarr.2025.23.3.0168
Primary Topic
Glycosylation and Glycoproteins Research
Type
article
Field-Weighted Citation Impact
0.00

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article

Physicochemical properties of micromycetes Alternaria alternate 4 lectin

A. Salomy Monica Diyya, Zinurova E.E, Bagaeva T.V, Zinurov M.R
GSC Advanced Research and Reviews
Glycosylation and Glycoproteins Research
article

Physicochemical properties of micromycetes Alternaria alternate 4 lectin

A. Salomy Monica Diyya, Zinurova E.E, Bagaeva T.V, Zinurov M.R
article en

Abstract

The physicochemical properties of the lectin of the lower fungus, micromycetes Alternaria alternate 4 have been studied. It was found that the lectin of the micromycetes Alternaria alternate 4 is stable over a wide range of temperatures and pH values (5-70oC and pH 6.0-9.0). The greatest activity of lectin was observed at a temperature of 5-50 °C and a pH of 6.5-8.5. The increased activity of Alternaria alternate 4 lectin was facilitated by the presence of divalent Ca2+, Mn2+, and Zn2+ ions in the reaction mixture, which indicates that Alternaria alternate 4 lectin is a metal-dependent glycoprotein. Alternaria alternate 4 lectin had the ability to bind simple carbohydrates. The activity of Alternaria alternate 4 lectin was inhibited to a greater extent by galactose, which indicates that Alternaria alternate 4 lectin belongs to the group of galactose-binding lectins.

GSC Advanced Research and ReviewsVol. 23(3)
Kazan Federal University
Openalex Percentile: Top 87%
Glycosylation and Glycoproteins Research
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