RESEARCH NOTE: HEMAGGLUTINATING ACTIVITY of LECTINS IN SELECTED VARIETIES of RAW and PROCESSED DRY BEANS (original) (raw)
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International Journal of Advanced Academic Research, 2016
Lectins was extracted from processed and unprocessed black-eyed peas, green beans, soybeans, peanuts, and red kidney beans by grinding using attrition mill and then soaked in distilled water. The proteins in the supernatant were precipitated by dissolving 10g of ammonium sulphate in 100ml of the supernatants. The lectin extracts were evaluated for hemagglutinin activity using human erythrocytes from blood group A + , B + , AB + , and O + , respectively. Result revealed that lectins from unprocessed soybean, black-eyed pea and green bean are blood group selective and may be classified as blood type specific lectins. While lectins from kidney beans and peanuts agglutinated all blood groups and may be classified as panhemagglutinin lectins, i.e. they agglutinated erythrocytes from all blood groups. Result shows that blood group O is less affected by hemagglutinin activity of lectin. Reduction/loss of hemagglutinin activity was observed with reduction in concentration of the crude lectin extracts in all unprocessed legumes. Boiling (at 100 0 C) for 30minutes completely inactivated hemagglutinin activity of lectin in Black eyed peas, soybeans, green beans and red kidney beans. Slight hemagglutinin activity was seen in lectin from roasted peanuts, indicating that dry heating may be very effective method to inactivate lectin completely. Also, in this study, lectins were extracted from rice (Oryza sativa), maize (Zea mays), sorghum (Sorghum bicolor), Acha (Digitaria excells), millet (Panicum maniceum); partial purification of the extract assayed from hemugglutinin activity using 4% of human erythrocyte in lectin buffer. Extract from these selected cereals showed positive and negative agglutination reaction with blood group A + , B + , O + and AB + depending on the concentration (dilution) and the blood group. Lectin extract from maize showed no agglutination reaction when diluted in blood group A + , B + , and AB + and even when processed and diluted. While crude lectin extract from rice showed no activity in blood group A + , B + , and AB + and when unprocessed and showed lectin agglutination activity when processed by boiling (cooking) showing that heat may encourage its activity. Blood group B + , and AB + showed no activity in all dilution. Also acha showed high agglutination activity in blood group A + , B + , AB + and O + but losses activity in dilution a 2 and a 3. Crude lectin extract from processed sorghum showed
Hemagglutinin Activities of Lectin Extracts from Selected Legumes
Researchgate, 2020
The legumes-Mucuna, Cowpea, Pigeon pea, African Yam Bean, Black-eyed pea, Soybean, Red kidney bean, Peanut, Green bean, and Bambara-were obtained from markets in Umuahia, ground in flour using Art's Way Roller Mill. Crude lectins were extracted from the milled legumes by soaking in distilled water for over 12 hours, followed by decanting; the proteins in the supernatant were precipitated by dissolving 10g of ammonium sulfate in 100ml of the supernatants. The crude lectin extracts were evaluated for hemagglutinin activity, using human erythrocytes. Mucuna lectins were specific for blood groups B + and AB +. Cowpea lectins agglutinated group A + and B +. African yam bean and Bambara lectins agglutinated all, while Pigeon pea was specific for groups A + , B + and O +. Mucuna cowpea, Pigeon pea, lectin was blood specific, while African yam bean and Bambara lectins were not. Lectins from Soybean, Black-eyed pea, and Green bean were blood group selective; while lectins from Kidney beans and Peanuts were pan-hemagglutinin lectins. Blood group O was less affected. Reduction in hemagglutinin activity was observed with a reduction in the concentration of the crude lectin extracts.
Biological Properties and Characterization of Lectin from Red Kidney Bean (Phaseolus Vulgaris)
Food Reviews International, 2008
Red kidney beans (Phaseolus vulgaris) contain significant amounts of lectins which have both beneficial and detrimental biological properties. Lectins are carbohydratebinding glycoproteins that can react specifically with human blood cells, preferentially agglutinate malignant cells, and undergo mitogenic stimulation of lymphocytes. Some lectins are resistant to heat and proteolytic enzymes and can enter the circulatory system intact. Phytohaemagglutinin (PHA)-a lectin isolated from the red kidney beanconsists of four subunits with a molecular weight of 125 kDa. This bioactive compound has been partially purified by affinity chromatography using Affi-gel Blue. PHA has been shown to inhibit the viral enzymes, immunodeficiency virus type 1 reverse transcriptase (HIV-1 RT), and aand b-glucosidases. This paper will review the chemical properties, biological activity, distribution, isolation, and heath benefits of red kidney bean lectin.
Scientific Bulletin. Series F. Biotechnologies, 2013
The purpose of the research was to study the purification and characterization of lectin from Phaseolus vulgaris L. cv.white seeds. The lectin was purified by sequence of steps , namly , first with ammonium sulfate precipitation followed by ion exchange (DEAE cellulose) and gel filtration (sephadex G-200) chromatographies , and finally by polyacrylamide electrophoresis (PAGE). Single band was observed in native PAGE. The lectin was shown to have molecular weight of 33 kDa in SDS PAGE and about 35 kDa in gel filtration and purified about 9.01 fold to final specific activity of 64 titer/mg of protein. The hemagglutination activity of the lectin was stable within the pH range from 4-11 and temperature range from 0°-50°C. Chemical modification results indicate that lysine and tryptophan were crucial for the hemagglutination activity of lectin. The results of carbohydrates specificity showed that the lectin was had complex sugar specifities, but not specific to xylose and mannose.
Biosynthesis of lectins in developing seeds of common bean
Food Chemistry, 1990
Two cultivars of Phaseolus vulgaris L., )qor de mayo FM-RMC, showing resistance to common mosaic virus and to bean rust (Uromyces phaseoli), and FM-C, without such resistance, were used to study the synthesis of lectins during seed development as measured by affinity chromatography of protein fr~ctions. Seeds at different stages of development were sorted out by size from 4-12mm length, in addition to mature samples. The spec([ic haemagglutinating activity ( SHA ) of isolated protein fractions from mature seeds', expressed as haemagglutinating units/mg protein, and the theoretical agglutination capacity (TA C). calculated from the SHA and the total protein fr~ction, were also assessed. The peak lectin level as measured by affinity chromatography was reached at a seed size of lOmm and decreased thereafter. The lec tin con ten t and TA C of all samples of the disease-resistan t cultivar were superior to that of the non-resistant variety.
International Journal of Research and Analytical Reviews (IJRAR) , 2024
A protein fraction exhibiting lectin activity was identified in the extract of local Roman bean (Phaseolus vulgaris) sprouts. The galactose-specific lectins demonstrated the highest activity. The galactose-specific lectin (BS-Gal) was purified using affinity chromatography on an ES-2100-100 column. Gel electrophoresis revealed that BS-Gal consists of two protein subunits with molecular weights of 60 and 54 kDa, respectively. Various physicochemical properties of the lectin were investigated, showing optimal activity within a pH range of 7-9 and temperatures from 0 to 75 °C, beyond which its hemagglutinating activity diminishes. The lectin displayed high sensitivity to divalent ions and certain amino acids. Calcium and magnesium ions significantly contribute to the structural integrity of the lectin, as indicated by changes in hemagglutinating activity in the presence of EDTA and EGTA. Additionally, BS-Gal was found to bind to human erythrocytes expressing A and B antigens.
Journal of the Science of Food and Agriculture, 1982
The toxic lectins present in red, white and black kidney beans (Phaseolus vulgaris) are sensitive to heat treatment and the efficiency of that treatment is greatly improved by pre-soaking of the seeds. Heating of pre-soaked seeds at all temperatures above 75°C caused a continuous reduction in both their haemagglutinating activity and toxicity. However, the only safe method of eliminating toxicity was to heat the fully hydrated seeds to 100°C for a minimum of 10 min.
Purification and Characterization of a Lectin fromPhaseolus vulgaris cv.(Anasazi Beans)
Journal of Biomedicine and Biotechnology, 2009
A lectin has been isolated from seeds of the Phaseolus vulgaris cv. "Anasazi beans" using a procedure that involved affinity chromatography on Affi-gel blue gel, fast protein liquid chromatography (FPLC)-ion exchange chromatography on Mono S, and FPLC-gel filtration on Superdex 200. The lectin was comprised of two 30-kDa subunits with substantial N-terminal sequence similarity to other Phaseolus lectins. The hemagglutinating activity of the lectin was stable within the pH range of 1-14 and the temperature range of 0-80 • C. The lectin potently suppressed proliferation of MCF-7 (breast cancer) cells with an IC 50 of 1.3 μM, and inhibited the activity of HIV-1 reverse transcriptase with an IC 50 of 7.6 μM. The lectin evoked a mitogenic response from murine splenocytes as evidenced by an increase in [ 3 H-methyl]-thymidine incorporation. The lectin had no antifungal activity. It did not stimulate nitric oxide production by murine peritoneal macrophages. Chemical modification results indicated that tryptophan was crucial for the hemagglutinating activity of the lectin.
Journal of Food Biochemistry, 1990
High levels of lectin activity were found in sixty cultivated and ten wild tepary (Phaseolus acutifolius) accessions. No lectin deficient varieties were observed and all examples studied contained both the phytohemagglutinin-E and L-like lectins previously described . There appeared to be no obvious differences between the wild and cultivated forms of the tepary lectins and all teparies studied contained lectin-like proteins in addition to the tepary lectins. One of the lectin related proteins (40 Kdalton subunit) was present in all teparies and may be comparable to arcelin, a lectin found in certain wild accessions of Phaselus vulgaris. All wild teparies contained a lectin related polypeptide of about 34 Kdaltons which appears to distinguish the wild teparies from the cultivated forms. Three tepary-common bean hybrids were examined and one hybrid was found to be expressing both tepary and common bean lectin genes.