Crystallization and preliminary X-ray diffraction analysis of a novel trypsin inhibitor from seeds of Copaifera langsdorffii

A novel trypsin inhibitor isolated from seeds of Copaifera langsdorffii was purified to homogeneity and crystallized. Crystals suitable for X-ray analysis were grown using the hanging-drop vapour-diffusion method at 291 K in sodium acetate buffer at pH values near 4.3 using PEG 4000 as precipitant. The crystals presented symmetry compatible with the space group P4(1)2(1)2 or P4(3)2(1)2, with unit-cell parameters a = b = 58.71, c = 93.75 Angstrom, and diffracted to 1.83 Angstrom resolution at the synchrotron source.5791316131

Talisia esculenta lectin and larval development of Callosobruchus maculatus and Zabrotes subfasciatus (Coleoptera : Bruchidae)

Bruchid larvae cause major losses in grain legume crops throughout the world. Some bruchid species, such as the cowpea weevil and the Mexican bean weevil, are pests that damage stored seeds. Plant lectins have been implicated as antibiosis factors against insects, particularly the cowpea weevil, Callosobruchus maculatus. Talisia esculenta lectin (TEL) was tested for anti-insect activity against C. maculatus and Zabrotes subfasciatus larvae. TEL produced ca. 90% mortality to these bruchids when incorporated in an artificial diet at a level of 2% (w/w), The LD50 and FD50 for TEL was ca. 1% (w/w) for both insects. TEL was not digested by midgut preparations of C maculatus and Z, subfasciatus. The transformation of the genes coding for this lectin could be useful in the development of insect resistance in important agricultural crops. (C) 2002 Elsevier Science B.V. All tights reserved.15712838

Trypsin inhibitor from Dimorphandra mollis seeds: purification and properties

A trypsin inhibitor from Dimorphandra mollis seeds was isolated to apparent homogeneity by a combination of ammonium sulfate precipitation, gel filtration, ion-exchange and affinity chromatographic techniques. SDS-PAGE analysis gave an apparent molecular weight of 20 kDa, and isoelectric focusing analysis demonstrated the presence of three isoforms. The partial N-terminal amino acid sequence of the purified protein showed a high degree of homology with various members of the Kunitz family of inhibitors. This inhibitor, which inhibited trypsin activity with a K-i of 5.3 x 10(-10) M, is formed by a single polypeptide chain with an arginine residue in the reactive site. (C) 2000 Elsevier Science Ltd. All rights reserved.54655355

Short and long-term antinutritional effect of the trypsin inhibitor ApTI for biological control of sugarcane borer

Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)Plant-derived trypsin inhibitors have been shown to have potent anti-insect effects and are a promising alternative for the biological control of pests. In this work, we tested the anti-insect activity of Adenanthera pavonina trypsin inhibitor (ApTI) against Diatraea saccharalis larvae, a major insect pest in sugarcane. The addition of 0.1% ApTI in short-term assays resulted in 87% and 63% decreased trypsin and chymotrypsin activities respectively. ApTI was not digested after 60 h incubation with D. saccharalis midgut proteases. The chronic effects of ApTI on F0 and F1 generations of D. saccharalis were also analyzed. The larvae from the F0 generation showed 55% and 21% decreased larval and pupal viability, respectively. ApTI-fed larvae from the F1 generation showed a decrease of 33% in survival rate and 23% in the average larval weight. Moreover, ApTI treatment reduced trypsin and chymotrypsin activities in F1 larvae. Thus, the anti-insect effects of ApTI on consecutive generations (F0 and F1) of D. saccharalis larvae demonstrate its potential for long-term control of this pest. (C) 2013 Elsevier Ltd. All rights reserved.6117Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)FUNDECT (Fundacao de Apoio ao Desenvolvimento do Ensino, Ciencia e Tecnologia do Estado do Mato Grosso do Sul)FINEP (Financiamento de Estudos e Projetos/Ministerio da Ciencia e Tecnologia)Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq

Influência do método de filetagem e categorias de peso sobre rendimento de carcaça, filé e pele da tilápia do Nilo (Oreochromis niloticus)

The objective of this study was to evaluate the processing methods (F-1 = to remove skin with pliers and then to cut in fillets; F-2 = cut in fillet and then to remove skin with knife and pliers help) and weight categories (W-1=250-300 g; W-2=301-350 g; W-3 = 351-400 g and W-4 = 401-450 g), on the carcass (CY), fillet (FY) and skin yield of Nile tilapia. Forty-eight fishes were used in a completely randomized design. There was effect for the processing method, being the F-1 mean (56.43 and 36.67 %) higher to the F-2 (53.46 and 32.89%) for CY and FY respectively. For the weight categories, W-1 (56.49 and 37.34%) and W-2 (56.34 and 36.40%) were superior as compared to W-3 (53.27 and 31.98%) and W-4 (53.71 and 33.42%), respectively for CY and FY. Crude skin percentage, clean and of fleshed were higher for F-2, but there was no effect for weight categories. The F-1 processing method promoted the best yield and skin results, and for the weight categories W-1 and W-2 higher yields

Purification and characterization of an N-acetylglucosamine-binding lectin from Koelreuteria paniculata seeds and its effect on the larval development of Callosobruchus maculatus (Coleoptera : Bruchidae) and Anagasta kuehniella (Lepidoptera : Pyralidae)

This study describes the purification of an N-acetylglucosamine-binding lectin from Koelreuteria paniculata seeds and its effects on the larval development of Callobruchus maculatus and Anagasta kuehniella. The lectin (KpLec) was characterized and isolated by gel filtration, affinity column, and reverse phase chromatography. SDS-PAGE indicated that this lectin is a dimer composed of subunits of 22 and 44 kDa. The N terminus exhibited 40% similarity with Urtiga dioica agglutinin. KpLec was tested for anti-insect activity against C. maculatus and A. kuehniella. With regard to C. maculatus, an artificial diet containing 0.7 and 1% KpLec produced LD50 and ED50 value, respectively. However, for A. kuenhiella, an artificial diet containing 0.65% KpLec produced an LD50, whereas 0.2% KpLec produced an ED50. The transformation of genes coding for this lectin could be useful in the development of insect resistance in important agricultural crops.51102980298