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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| Published in: | Journal of applied phycology Vol. 32; no. 1; pp. 103 - 110 |
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| Main Authors: | , , , , , |
| Format: | Journal Article |
| Language: | English |
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01-02-2020
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| Abstract | 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. |
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| AbstractList | 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. 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. |
| Author | Porto, A. L. F. Brandão-Costa, R. M. P. Cavalcanti, V. L. R. Bezerra, Raquel Pedrosa Silva, A. J. Gama, W. A. |
| Author_xml | – sequence: 1 givenname: A. J. surname: Silva fullname: Silva, A. J. organization: Department of Animal Morphology and Physiology, Federal Rural University of Pernambuco – UFRPE – sequence: 2 givenname: V. L. R. surname: Cavalcanti fullname: Cavalcanti, V. L. R. organization: Department of Animal Morphology and Physiology, Federal Rural University of Pernambuco – UFRPE – sequence: 3 givenname: A. L. F. surname: Porto fullname: Porto, A. L. F. organization: Department of Animal Morphology and Physiology, Federal Rural University of Pernambuco – UFRPE – sequence: 4 givenname: W. A. surname: Gama fullname: Gama, W. A. organization: Department of Biology, Federal Rural University of Pernambuco – UFRPE – sequence: 5 givenname: R. M. P. surname: Brandão-Costa fullname: Brandão-Costa, R. M. P. organization: Department of Animal Morphology and Physiology, Federal Rural University of Pernambuco – UFRPE – sequence: 6 givenname: Raquel Pedrosa surname: Bezerra fullname: Bezerra, Raquel Pedrosa email: rpbezerra@yahoo.com.br organization: Department of Animal Morphology and Physiology, Federal Rural University of Pernambuco – UFRPE |
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| CitedBy_id | crossref_primary_10_1080_14786419_2023_2169688 crossref_primary_10_1016_j_biochi_2022_07_004 crossref_primary_10_1080_07391102_2023_2274519 crossref_primary_10_1080_21655979_2022_2061148 crossref_primary_10_14232_abs_2021_1_65_73 crossref_primary_10_1007_s11947_023_03194_y crossref_primary_10_3390_phycology3040029 crossref_primary_10_1016_j_algal_2021_102541 crossref_primary_10_1016_j_biotechadv_2023_108209 crossref_primary_10_3390_plants12010026 crossref_primary_10_1007_s11356_024_32143_1 crossref_primary_10_1016_j_algal_2021_102290 crossref_primary_10_3389_fenrg_2022_904014 crossref_primary_10_3390_ani13101589 |
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| Keywords | Hemagglutinins Biochemical characterization Isolation ABO type Chlorophyceae Protein |
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| SubjectTerms | 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 |
| Title | The green microalgae Tetradesmus obliquus (Scenedesmus acutus) as lectin source in the recognition of ABO blood type: purification and characterization |
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