Cocoyam (Colocasia esculenta) modulates some parameters of testosterone propionate-induced rat model of benign prostatic hyperplasia.

The increased global prevalence of benign prostatic hyperplasia (BPH) and the promising potentials of functional foods in ameliorating it led to this study which reported the effect of aqueous ethanol extract of cocoyam (Colocasia esculenta) tuber on some biochemical indices in testosterone propionate (TP) induced benign prostatic hyperplasia (BPH) rats. Thirty male albino rats were randomly assigned into 6 groups of 5 rats each. Group 1 (negative control) received 3 mg/kg of TP and normal saline, group 2 (positive control) received 3 mg/kg of TP and 5 mg/kg of finasteride; groups 3, 4, and 6 rats received 3 mg/kg of TP and 100, 200 and 400 mg/kg of ethanol extracts of cocoyam respectively while group 5 (normal control) received olive oil + normal saline. The study lasted for 28 days. The negative control had increased prostate weight (p < 0.05), decreased body weight gain, prostatic superoxide dismutase, catalase and glutathione concentrations; no differences (p > 0.05) in the serum total cholesterol, triacylglycerol, Very Low Density Lipoprotein, High Density Lipoprotein, Low Density Lipoprotein concentration but increased (p < 0.05) prostate levels of interleukin 10, prostate specific antigen, testosterone, total proteins and malondialdehyde relative to the normal control. Finasteride or the C. esculenta tuber extract modulated most of these parameters as corroborated by histology of the prostate. The percentage yield of the C. esculenta tuber extract was 1.56% and 23 phenolic compounds were characterized in the tuber. The study showed the potentials of C. esculenta tuber in the management of BPH.

Thermal and chemical denaturation of Colocasia esculenta tuber agglutinin from α2ß2 to unfolded state.

The major tuber storage protein of Colocasia esculenta, is a monocot mannose-binding, widely used dietary lectin, containing two polypeptides of 12.0 and 12.4 kDa. By both gel filtration and dynamic light scattering at pH 7.2, the lectin has a α2ß2 form of apparent molecular mass of 48.2 kDa and a hydrodynamic radius of 6.1 ± .2 nm; however, at pH 3, it migrates as αß and has a reduced hydrodynamic radius of 4.6 ± .3 nm. Our circular dichroism spectroscopy studies show that the lectin retains approximately 100% of its secondary structure between pH 2-8, going down to ~90% for extreme acidic/alkaline conditions. The fluorescence emission maxima of 346 to 350 nm for pH 4 to 10 show that the tryptophan residues are relatively exposed. The unfolding is a simple two-state process, N4 ↔ 4U, as seen in our denaturation scan profiles. These denaturation profiles, monitored separately by fluorescence, far-UV CD, and near-UV CD, are completely super imposable. Analyses of these profiles provide an estimate of several thermodynamic parameters at each guanidinium chloride concentration, including the melting temperature Tg, which is 346.9 K in 0 M, but lowers to 321.8 K in 3.6 M. Dimeric and tetrameric interfaces observed in the crystal structure for the same protein are used to rationalize solution data in some detail.

Optimization of Lactobacillus acidophilus cultivation using taro waste and evaluation of its biological activity.

In this study, taro waste (TW) was utilized for Lactobacillus acidophilus BCRC 14079 cultivation and the anti-tumor and immune-modulatory properties of heat-killed cells (HKCs), cytoplasmic fraction (CF), and exopolysaccharide (EPS) were evaluated. The optimum liquefaction enzyme dosage, temperature, and time determined by Box-Behnken design response surface methodology (BBD-RSM) were 9 mL/L of α-amylase, 79.2 °C, and 5 h of reaction, respectively. The optimum temperature and reaction time for saccharification were determined as 60 °C and 3 h. The optimum medium, CGMY1 medium, constitutes of TW hydrolysate containing 37 g/L of glucose, 25 g/L of corn gluten meal (CGM), and 1 g/L of yeast extract (YE). Results of MTT assay showed that HKCs and EPS from CGM medium exhibited the highest anti-proliferative in HT-29 (IC50 of HKCs, 467.25 µg/mL; EPS, 716.10 µg/mL) and in Caco-2 cells (IC50 of EPS, 741.60 µg/mL). Luciferase-based NF-ΚB and COX-2 systems indicated HKCs from CGM medium stimulated the highest expression of luciferin in both systems. The luciferase activities by using 100 and 500 µg/mL of HKCs from CGM were 24.30- and 45.83-fold in NF-ΚB system and 11.54- and 4.93-fold in COX-2 system higher than the control. In conclusion, this study demonstrated the potential of TW medium for L. acidophilus cultivation and the production of non-viable probiotics with enhanced biological activities.

Extratos aquosos de inhame (Dioscorea rotundata Poirr. ) e de mastruz (Chenopodium ambrosioides L. ) no desenvolvimento da lagarta-do-cartucho-do-milho Spodoptera frugiperda (J. E. Smith, 1797) / Aqueous extracts of yam (Dioscorea rotundata Poirr. ) and chenopodium (Chenopodium ambrosioides L. ) in the development of fall armyworm Spodoptera frugiperda (J. E. Smith, 1797)

RESUMO: Estudou-se o efeito de extratos aquosos de inhame (0; 5; 10; e 20% p/p) e de mastruz (0; 2; 4; 6; 8 e 10% p/p) na biologia da lagarta-do-cartucho. Secções de folhas de milho foram mergulhadas por 30 segundos em soluções de cada concentração; após a secagem, colocou-se em cada secção uma lagarta recém-eclodida. Foram avaliadas a viabilidade e a duração das fases larval e pupal, peso e comprimento das lagartas e pupas. Em relação ao extrato de inhame, a concentração de 20% causou maior influência na fase larval, sendo a viabilidade reduzida para 12%, com duração de 7 dias, diferindo da testemunha com 17 dias. O extrato da mesma planta a 10% causou 48% de mortalidade. Em todas as concentrações esse extrato também afetou a fase de pupa; na testemunha, 85% das pupas foram viáveis, enquanto nos demais tratamentos a viabilidade não excedeu a 25%. Para o peso e comprimento das lagartas, os resultados não foram significativos. Para o mastruz, o extrato a 20% causou influência na fase larval com baixa viabilidade e mortalidade logo nos primeiros seis dias de avaliação. Outras concentrações de mastruz não deferiram entre si nas fases larval e pupal. Verificou-se que a alimentação das lagartas com folhas tratadas com mastruz diminuiu o peso das pupas.

ABSTRACT: The effect of aqueous extracts of yam (0, 5, 10, and 20% h/h) and chenopodium (0, 2, 4, 6, 8 and 10% h/h) on the biology of fall armyworm was studied. Sections of maize leaves were dipped for 30 seconds in solutions of each concentration; after the section dried, a recently hatched caterpillar was placed onto each treated section. The viability and duration of the larval and pupal stages and the weight and length of the caterpillars and pupae were evaluated. For yam, the extract at 20% concentration caused the greatest influence on the larval stage of the insect, significantly reducing larval viability to 12%, with 7 day larval stage duration, differing from the control at 17 days. The extract of the same plant at 10% caused 48% larval mortality. At all concentrations, that extract also affected the pupal stage; in the control, pupal viability was 85%, whereas for the other concentrations the viability did not exceed 25%. No significant differences were observed for the weight and length of caterpillars. For chenopodium, the extract at 20% concentration caused influence on the larval stage, as it showed the lowest viability, causing mortality in six days. Other chenopodium concentrations did not show differences for the larval and pupal stages. Feeding caterpillars with leaves treated with the extract of chenopodium decreased pupal weight.

Structural analysis and binding properties of isoforms of tarin, the GNA-related lectin from Colocasia esculenta.

The lectins, a class of proteins that occur widely in animals, plants, fungi, lichens and microorganisms, are known for their ability to specifically bind to carbohydrates. Plant lectins can be classified into 12 families including the Galanthus nivalis agglutinin (GNA)-related lectin superfamily, which is widespread among monocotyledonous plants and binds specifically to mannose, a behavior that confers remarkable anti-tumor, anti-viral and insecticidal properties on these proteins. The present study characterized a mitogenic lectin from this family, called tarin, which was purified from the crude extract from taro (Colocasia esculenta). The results showed that tarin is a glycoprotein with 2-3% carbohydrate content, composed of least 10 isoforms with pIs ranging from 5.5 to 9.5. The intact protein is a heterotetramer of 47kDa composed of two non-identical and non-covalently associated polypeptides, with small subunits of 11.9kDa and large subunits of 12.6kDa. The tarin structure is stable and recovers or maintains its functional structure following treatments at different temperatures and pH. Tarin showed a complex carbohydrate specificity, binding with high affinity to high-mannose and complex N-glycans. Many of these ligands can be found in viruses, tumor cells and insects, as well as in hematopoietic progenitor cells. Chemical modifications confirmed that both conserved and non-conserved amino acids participate in this interaction. This study determined the structural and ligand binding characteristics of a GNA-related lectin that can be exploited for several different purposes, particularly as a proliferative therapeutic molecule that is able to enhance the immunological response.

Role of pCeMT, a putative metallothionein from Colocasia esculenta, in response to metal stress.

Metallothioneins (MTs) play a major role in metal homeostasis and/or detoxification in plants. In this study, a novel gene, pCeMT, was isolated from Colocasia esculenta and characterized. Our results indicate that Escherichia coli cells expressing pCeMT exhibited enhanced Cd, Cu, and Zn tolerance and accumulation compared with control cells. Furthermore, pCeMT-overexpressing tobacco seedlings displayed better growth under Cd, Cu, and Zn stresses and accumulated more Cd and Zn compared with the wild type. Interestingly, transgenic tobacco displayed markedly decreased hydrogen peroxide (H(2)O(2)) and lipid peroxidation levels under Cd, Cu, and Zn treatments. These results suggest that pCeMT could play an important role in the protection of plant cells from oxidative stress by reactive oxygen species (ROS) scavenging and in the detoxification of free metals by metal binding, leading to improved plant metal tolerance.

Crystal structure of tarocystatin-papain complex: implications for the inhibition property of group-2 phytocystatins.

Tarocystatin (CeCPI) from taro (Colocasia esculenta cv. Kaohsiung no. 1), a group-2 phytocystatin, shares a conserved N-terminal cystatin domain (NtD) with other phytocystatins but contains a C-terminal cystatin-like extension (CtE). The structure of the tarocystatin-papain complex and the domain interaction between NtD and CtE in tarocystatin have not been determined. We resolved the crystal structure of the phytocystatin-papain complex at resolution 2.03 Å. Surprisingly, the structure of the NtD-papain complex in a stoichiometry of 1:1 could be built, with no CtE observed. Only two remnant residues of CtE could be built in the structure of the CtE-papain complex. Therefore, CtE is easily digested by papain. To further characterize the interaction between NtD and CtE, three segments of tarocystatin, including the full-length (FL), NtD and CtE, were used to analyze the domain-domain interaction and the inhibition ability. The results from glutaraldehyde cross-linking and yeast two-hybrid assay indicated the existence of an intrinsic flexibility in the region linking NtD and CtE for most tarocystatin molecules. In the inhibition activity assay, the glutathione-S-transferase (GST)-fused FL showed the highest inhibition ability without residual peptidase activity, and GST-NtD and FL showed almost the same inhibition ability, which was higher than with NtD alone. On the basis of the structures, the linker flexibility and inhibition activity of tarocystatins, we propose that the overhangs from the cystatin domain may enhance the inhibition ability of the cystatin domain against papain.

Molecular cloning, recombinant gene expression, and antifungal activity of cystatin from taro (Colocasia esculenta cv. Kaosiung no. 1).

A cDNA clone, designated CeCPI, encoding a novel phytocystatin was isolated from taro corms (Colocasia esculenta) using both degenerated primers/RT-PCR amplification and 5'-/3'-RACE extension. The full-length cDNA gene is 1,008 bp in size, encodes 206 amino acid residues, with a deduced molecular weight of 29 kDa. It contains a conserved reactive site motif Gln-Val-Val-Ser-Gly of cysteine protease inhibitors, and another consensus ARFAV sequence for phytocystatin. Sequence analysis revealed that CeCPI is phylogenetically closely related to Eudicots rather than to Monocots, despite taro belonging to Monocot. Recombinant GST-CeCPI fusion protein was overexpressed in Escherichia coli and its inhibitory activity against papain was identified on gelatin/SDS-PAGE. These results confirmed that recombinant CeCPI protein exhibited strong cysteine protease inhibitory activity. Investigation of its antifungal activity clearly revealed a toxic effect on the mycelium growth of phytopathogenic fungi, such as Sclerotium rolfsii Sacc. etc., at a concentration of 80 microg recombinant CeCPI/ ml. Moreover, mycelium growth was completely inhibited and the sclerotia lysed at a concentration of 150-200 microg/ml. Further studies have demonstrated that recombinant CeCPI is capable of acting against the endogenous cysteine proteinase in the fungal mycelium.