Explorando a versatilidade estrutural das lectinas de plantas para o isolamento e

Simpósio - Lectinas vegetais: purificação e aplicaçõesbiotecnológica

Histochemical Evaluation of Human Prostatic Tissues with Cratylia mollis Seed Lectin

Lectins, proteins which selectively recognize carbohydrates, have been used in histochemistry for the evaluation of changes in glycosylation in processes of cellular differentiation and/or dedifferentiation. Cratylia mollis seed lectins (Cramoll 1,4 and Cramoll 3), conjugated to horseradish peroxidase, were used as histochemical probes in human prostate tissues: normal (NP), hyperplasia (BPH), and prostate carcinoma (PCa). The staining pattern of Con-A and Cramoll 1,4 in BPH was more intense than in NP. These lectins also showed staining differences between BPH and PCa; the latter showing decreased staining intensity with an increased degree of malignancy. PNA and Cramoll 3 stained epithelial cells similarly in all diagnoses although they did present intense staining of PCa glands lumen. Corpora amylacea were not differentially recognized by any of the lectins. Cramoll 1,4 and Cramoll 3 seed lectins present themselves as candidates for histochemical probes for prostate pathologies when compared to commercial lectins such as Con-A and PNA

Moringa oleifera: Resource management and multiuse life tree

Moringa oleifera Lamarck (Moringaceae family) is a plant native from the Western and sub-Himalayan parts of Northwest India, Pakistan and Afghanistan. This species is widely cultivated across Africa, South-East Asia, Arabia, South America and Caribbean Islands. M. oleifera culture is also being distributed in the Semi-Arid Northeast of Brazil. It is a multiuse life tree with great environmental economic importance in industrial and medical areas. This review reports different purposes of M. oleifera including sustaining environmental resources, soil protection and shelter for animals. This plant requires not much care and distinct parts have bioactive compounds. Moringa tissues used in human and animal diets, also withdraw pollutants from water. The seeds with coagulant properties used in water treatment for human consumption, remove waste products like surfactants, heavy metals and pesticides. The oil extracted from seeds is used in cosmetic production and as biodiesel. M. oleifera tissues also contain proteins with different biological activities, including lectins, chitin-binding proteins, trypsin inhibitors, and proteases. The lectins are reported to act as insecticidal agents against Aedes aegypti (vector of dengue, chikungunya and yellow fevers) and Anagasta kuehniella (pest of stored products) and also showed water coagulant, antibacterial and blood anticoagulant activities. The presence of trypsin inhibitors has been reported in M. oleifera leaves and flowers. The inhibitor from flowers is toxic to larvae of A. aegypti. The flowers also contain caseinolytic proteases that are able to promote clotting of milk. In this sense, M. oleifera is a promising tree from a biotechnological point of view, since it has shown a great variety of uses and it is a source of several compounds with a broad range of biological activities.Conselho Nacional de Desenvolvimento Científico e Tecnológico for fellowship (LCBBC) and to the Foundation for Science and Technology, POPH/FSE (AFSS

Lyophilization of ImunoparvumR° as an alternative to reduce its side-effects

In Brazil, Imunoparvum R° is used as an immunomodulator. It is commercialized in 2 ml ampoules containing 2 mg of Propionebacterium acnes (formerly known as Corynebacterium parvum)/ml, in a 0.5 % phenol and 0.85% sodium chloride solution. High therapeutic power associated to minimum side effects is a great challenge to the pharmaceuticalindustry. Research results have shown that Imunoparvum R° induces side effects in humans and animals, probably because of its phenol content (SOUSA, 1993; RODRIGUES, 2001). The objective of this study was to determine the phenol content of lyophilized and non-lyophilized Imunoparvum R° and to compare their side effects in mice. It was demonstrated that the lyophilization process reduces the phenol content and the side effects of Imunoparvum R°, when compared to the commercialized Propionebacterium acnes suspension

Removal of tetracycline from contaminated water by Moringa oleifera seed preparations

The aim of this study was to evaluate tetracycline antibiotic (TA) removal from contaminated water by Moringa oleifera seed preparations. The composition of synthetic water approximate river natural contaminated water and TA simulated its presence as an emerging pollutant. Interactions between TA and protein preparations (extract; fraction and lectin) were also evaluated. TA was determined by solid phase extraction followed by high performance liquid chromatography - mass spectrometry. Moringa extract and flour removed TA from water. Extract removed TA in all concentrations and better removal (40%) was obtained with 40 mg L1; seed flour (particles 5 mm (0.50 g L1) removed 55% of antibiotic. Interactions between TA and seed preparations were assayed by haemagglutinating activity (HA). Specific HA (SHA) of extract (pH 7) was abolished with tetracycline (5 mg L1); fraction (75%) and lectin HA (97%) were inhibited with TA. Extract SHA decreased by 75% at pH 8. Zeta potential (ZP) of extract 700 mg L1 and tetracycline 50 mg L1 , pH range 5 to 8, showed different results. Extract ZP was more negative (10.73 mV to 16.00 mV) than tetracycline ZP (0.27 mV to 20.15 mV); ZP difference was greater in pH 8. The focus of this study was achieved since moringa preparations removed TA from water and compounds interacting with tetracycline involved at least lectin binding sites. This is a natural process, which do not promote environmental damage.This work was supported by the Fundacao para a Ciencia e a Tecnologia and POPH/FSE under Grant SFRH/BPD/37349/2007; the Conselho Nacional de Desenvolvimento Cientifico e Tecnologico (CNPq) for fellowships (PMGP and LCBBC); the authors thank the FCT Strategic Project of UID/BIO/04469/2013 unit, the project RECI/BBB-EBI/0179/2012 [FCOMP-01-0124-FEDER-027462] and the project 'BioInd - Biotechnology and Bioengineering for improved Industrial and Agro-Food processes,' REF. NORTE-07-0124-FEDER-000028 Co-funded by the Programa Operacional Regional do Norte (ON.2 - O Novo Norte), QREN, FEDER

Ferromagnetic Levan Composite: An Affinity Matrix to Purify Lectin

A simple and inexpensive procedure used magnetite and levan to synthesize a composite recovered by a magnetic field. Lectins from Canavalia ensiformis (Con A) and Cratylia mollis (Cramoll 1 and Cramoll 1, 4) did bind specifically to composite. The magnetic property of derivative favored washing out contaminating proteins and recovery of pure lectins with glucose elution. Cramoll 1 was purified by this affinity binding procedure in two steps instead of a previous three-step protocol with ammonium sulfate fractionation, affinity chromatography on Sephadex G-75, and ion exchange chromatography through a CM-cellulose column

Preparação de lectinas de Moringa oleifera com atividade coagulante

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Purification of a lectin from Cratylia mollis crude extract seed by a single step PEG/phosphate aqueous two-phase system

The partitioning and purification of lectins from the crude extract of Cratylia mollis seeds (Cramoll 1,4) was investigated in aqueous two-phase systems (ATPS). A factorial design model (24) was used to evaluate the influence of polyethylene glycol (PEG) molar mass (15008000g/mol), PEG concentration (12.517.5% w/w), phosphate (1015% w/w) concentration, and pH (68) on the differential partitioning, purification factor, and yield of the lectin. Polymer and salt concentration were the most important variables affecting partition of lectin and used to find optimum purification factor by experimental BoxBehnken design together with the response surface methodology (RSM). ATPS showed best conditions composed by 13.9% PEG1500, 15.3% phosphate buffer at pH 6, which ensured purification factor of 4.70. Sodium dodecyl sulfatepolyacrylamide gel electrophoresis showed a single band of protein with 26.1kDa. Furthermore, results demonstrated a thermostable lectin presenting activity until 60°C and lost hemagglutinating activity at 80°C. According to the obtained data it can be inferred that the ATPS optimization using RSM approach can be applied for recovery and purification of lectins.We are grateful to the following bodies for the grants awarded: CAPES (Coordination for the Improvement of Level Personnel Superior); FACEPE (Pernambuco Science and Technology Foundation): Researcher's scholarship grant: BFP-0017-5.05/18 CNPq (National Council for Scientific Development and Technological) process: 427153/2016-6 and we also thank the reviewers for their valuable comments and suggestions as these helped us to improve the manuscript.info:eu-repo/semantics/publishedVersio