The green microalgae Tetradesmus obliquus (Scenedesmus acutus) as lectin source in the recognition of ABO blood type: purification and characterization

The green microalgae Tetradesmus obliquus (Scenedesmus acutus) as lectin source in the recognition of ABO blood type: purification and characterization

Lectins have potential applications in agriculture, medicine, and biotechnological research and have become an important tool in the identification of different blood groups. Lectins can be obtained from different sources, such as microalgae. Tetradesmus obliquus is a green microalga that produces b...

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Bibliographic Details
Published in:Journal of applied phycology Vol. 32; no. 1; pp. 103 - 110
Main Authors: Silva, A. J., Cavalcanti, V. L. R., Porto, A. L. F., Gama, W. A., Brandão-Costa, R. M. P., Bezerra, Raquel Pedrosa
Format: Journal Article
Language:English
Published: Dordrecht Springer Netherlands 01-02-2020
Springer Nature B.V
Subjects:
ABO system
Albumins
Algae
Azocasein
Biomedical and Life Sciences
Biotechnology
Blood groups
Carbohydrates
Ecology
Erythrocytes
Filtration
Freshwater & Marine Ecology
Gel filtration
Gels
Glycoproteins
Horses
Ion exchange
Lectins
Life Sciences
Medical sciences
Microalgae
Molecular weight
pH effects
Phytoplankton
Plant Physiology
Plant Sciences
Purification
Recognition
Temperature effects
Tetradesmus obliquus
Thermal stability
Water purification
Hemagglutinins
Biochemical characterization
Isolation
ABO type
Chlorophyceae
Protein
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Summary:Lectins have potential applications in agriculture, medicine, and biotechnological research and have become an important tool in the identification of different blood groups. Lectins can be obtained from different sources, such as microalgae. Tetradesmus obliquus is a green microalga that produces bioactives with high added value. A novel lectin was purified from microalgae T. obliquus by ion exchange and gel filtration chromatographies and characterized by molecular mass determination; carbohydrate contents; recognition of the rabbit, bovine, horse, and ABO blood type; inhibition by carbohydrate and glycoprotein; optimum pH and temperature; and their stability. Lectin was purified with a purification factor of 4.2-fold and yield of 3.13 in a two-step using ion exchange and gel filtration. It agglutinated human type O and rabbit erythrocytes but not bovine, horse, human erythrocytes types A1, A2, B, and AB. Lectin showed optimum pH at 7.0–7.5 and stability for 90 min, while the optimum temperature of 20–50 °C showed fairly good thermostability. The lectin is a glycoprotein with 5.37% of carbohydrate, an apparent molecular mass of 78 kDa as determined by gel filtration, and the activity was decreasing in the presence of ions and inhibited only by glycoprotein azoalbumin, azocasein, and albumin, characteristics that indicate the lectin from T. obliquus as unique among microalgal lectins.
ISSN:0921-8971
1573-5176
DOI:10.1007/s10811-019-01923-5