Global interest in sugarcane has increased significantly in recent years due to its economic impact on sustainable energy production. Sugarcane breeding and better agronomic practices have contributed to a huge increase in sugarcane yield in the last 30 years. Additional increases in sugarcane yield are expected to result from the use of biotechnology tools in the near future. Genetically modified (GM) sugarcane that incorporates genes to increase resistance to biotic and abiotic stresses could play a major role in achieving this goal. However, to bring GM sugarcane to the market, it is necessary to follow a regulatory process that will evaluate the environmental and health impacts of this crop. The regulatory review process is usually accomplished through a comparison of the biology and composition of the GM cultivar and a non-GM counterpart. This review intends to provide information on non-GM sugarcane biology, genetics, breeding, agronomic management, processing, products and byproducts, as well as the current technologies used to develop GM sugarcane, with the aim of assisting regulators in the decision-making process regarding the commercial release of GM sugarcane cultivars.
A lectin was purified from Crotalaria paulina seeds by ion-exchange and FPLC molecular exclusion chromatography. CrpL had an apparent molecular mass of 30 kDa, as determined by SDS-PAGE under non-reducing and reducing conditions. CrpL effectively agglutinated human and cow erythrocytes, and this activity was not affected by 20 mM EDTA, showing no dependence of divalent cations. Hemagglutination was inhibited by N-acetyl-D-galactosamine, D-galactose and was also inhibited by glycoproteins, fetuin and asialofetuin. The N-terminal amino acid sequence of CrpL was identical to those of other lectins from the genus Crotalaria, and amino acid composition showed high amounts of Asx and Glx, and was rich in Gly, Ala and Ser, as also reported for lectins from other Crotalaria species. CrpL inhibited the growth of Xanthomonas axonopodis pv. phaseoli and Xanthomonas axonopodis pv. passiflorae, suggesting a role of this lectin in the defense of seeds against bacterial infections.
SummaryA new trypsin inhibitor (CPTI) has been isolated from Crotalaria paulina seeds. Puri cation of the inhibitor was carried out by gel ltration, ion-exchange chromatography, and subsequent reversed-phase HPLC. The presence of a single polypeptide chain, with a molecular mass of 20 kDa and isoelectric point 4.0, was detected. The trypsin inhibitor had a K i value of 4.5 £ 10 ¡ 8 M and was capable of acting on human, bovine, and porcine trypsin and weakly on bovine chymotrypsin. Amino acid analysis showed that CPTI has a high content of aspartate, glutamate, leucine, serine, and glycine, having 177 amino acid residues in its composition. These data suggest that the protein belongs to the Kunitz-type trypsin inhibitors. IUBMB Life, 48: 519-523, 1999
A new trypsin inhibitor (CPTI) has been isolated from Crotalaria paulina seeds. Purification of the inhibitor was carried out by gel filtration, ion-exchange chromatography, and subsequent reversed-phase HPLC. The presence of a single polypeptide chain, with a molecular mass of 20 kDa and isoelectric point 4.0, was detected. The trypsin inhibitor had a Ki value of 4.5 x 10(-8) M and was capable of acting on human, bovine, and porcine trypsin and weakly on bovine chymotrypsin. Amino acid analysis showed that CPTI has a high content of aspartate, glutamate, leucine, serine, and glycine, having 177 amino acid residues in its composition. These data suggest that the protein belongs to the Kunitz-type trypsin inhibitors.
Four different detergents, ASB 14, SB 3-10, CHAPS and Triton X100, were utilized to determine the optimal detergent for the solubilization of membrane proteins from the phytopathogenic bacterium Xylella fastidiosa. These proteins were differentially solubilized in distinct buffers containing the detergent and subjected to bidimensional electrophoresis within the non-linear pH range of 3-10. The detergents ASB 14 and SB 3-10 were the most effective revealing 221 and 157 spots, respectively. CHAPS and Triton X100 were less effective and revealed only 72 and 43 spots, respectively. MALDI-TOF tryptic peptide mass fingerprinting of 18 excised proteins from the ASB 14 treatment revealed that 83% were membrane proteins and that the theoretical efficiency of solubilization for ASB 14 was estimated to be 87%. This study demonstrates the effectiveness of the detergent ASB 14 for the solubilization of membrane proteins from the bacterium X. fastidiosa.
RESUMO -Desde os primórdios o homem buscou selecionar as plantas alimentícias para maior produtividade. O conhecimento da estrutura do DNA permitiu que a engenharia genética se desenvolvesse consideravelmente fornecendo ferramentas para a realização de alterações específicas no genoma. Os produtos destas alterações são denominados transgênicos ou organismos geneticamente modificados (OGM) e apresentam alto potencial de aplicação em diversas áreas da atividade humana como: agricultura, medicina, saúde, produção e processamento de alimentos, produção bioquímica, controle de doenças e biorremediação. Atualmente, as plantas transgênicas, oriundas da tecnologia do DNA recombinante, trouxeram novas variedades já cultivadas em mais de 100 milhões de hectares em 23 países, incluindo o Brasil, onde 8 variedades já foram aprovadas pela Comissão Técnica Nacional de Biossegurança (CTNBio). Esse método de melhoramento genético facilitou a introdução de características desejáveis em plantas, como resistência a estresses bióticos e abióticos e otimização da composição de alguns nutrientes essenciais à saúde animal e humana. Enquanto estes avanços da biotecnologia abrem novas perspectivas para a solução de problemas em áreas como a agricultura, a liberação de transgênicos para uso na natureza traz preocupações quanto a possíveis problemas de natureza ecológica e para a saúde humana e animal. Estas preocupações deram origem à criação de agências governamentais para controlar o uso desta tecnologia e regulamentar a segurança dos alimentos transgênicos e seus derivados. Até o momento, os estudos científicos mostram que os transgênicos liberados comercialmente são tão seguros ou mais ao meio ambiente e a saúde animal e humana que os convencionais.Palavras-chave: organismos geneticamente modificados, saúde humana e animal, segurança alimentar, transgênicos em rações Use of ingredients from OGM in feed and its impact on the production of food of animal origin for humanABSTRACT -From the origins the man has looked and selected vegetables with nutritive value for larger productivity. The knowledge of DNA structure allowed genetic engineering to develop and supplying tools for the accomplishment of specific alterations in the genome considerably. The products of these alterations are denominated transgenic or organisms genetically modified (OGM) and they present high application potential in several areas of the human activity as: agriculture, medicine, health, production and processing of foods, biochemical production and control of diseases. Nowadays, transgenic plants, originating from technology of the DNA recombinant, brought new varieties cultivated already in more than 100 million hectares in 23 countries, including Brazil, where 8 varieties were already approved for the National Technical Commission of Biosafety (CTNBio). That method of genetic improvement facilitated the introduction of desirable characteristics in plants, such as, resistance to biotic and non-biotic stress and optimization of the composition of some essential ...
Trypsin inhibitors of two varieties of Bauhinia variegata seeds have been isolated and characterized. Bauhinia variegata candida trypsin inhibitor (BvcTI) and B. variegata lilac trypsin inhibitor (BvlTI) are proteins with Mr of about 20,000 without free sulfhydryl groups. Amino acid analysis shows a high content of aspartic acid, glutamic acid, serine, and glycine, and a low content of histidine, tyrosine, methionine, and lysine in both inhibitors. Isoelectric focusing for both varieties detected three isoforms (pI 4.85, 5.00, and 5.15), which were resolved by HPLC procedure. The trypsin inhibitors show Ki values of 6.9 and 1.2 nM for BvcTI and BvlTI, respectively. The N-terminal sequences of the three trypsin inhibitor isoforms from both varieties of Bauhinia variegata and the complete amino acid sequence of B. variegata var. candida L. trypsin inhibitor isoform 3 (BvcTI-3) are presented. The sequences have been determined by automated Edman degradation of the reduced and carboxymethylated proteins of the peptides resulting from Staphylococcus aureus protease and trypsin digestion. BvcTI-3 is composed of 167 residues and has a calculated molecular mass of 18,529. Homology studies with other trypsin inhibitors show that BvcTI-3 belongs to the Kunitz family. The putative active site encompasses Arg (63)-Ile (64).
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