Navegando por Palavras-chave "sugarcane"
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- ItemSomente MetadadadosAntiproliferative and antioxidant activities of a tricin acylated glycoside from sugarcane (Saccharum officinarum) juice(Elsevier B.V., 2007-04-01) Duarte-Almeida, Joaquim Mauricio; Negri, Giuseppina; Salatino, Antonio; Carvalho, Joao Ernesto de; Lajolo, Franco Maria; Universidade de São Paulo (USP); Universidade Federal de São Paulo (UNIFESP); Universidade Estadual de Campinas (UNICAMP)From sugarcane juice, a flavone, identified by spectroscopic methods as tricin-7-O-beta-(6-methoxycinnamic)-glucoside, was isolated, in addition to orientin. the tricin derivative was shown to have antioxidant activity higher than Trolox (R) by means of the DPPH assay and lower by the beta-carotene/linoleic acid system. It showed in vitro antiproliferative activity against several human cancer cell lines, with higher selectivity toward cells of the breast resistant NIC/ADR line. (c) 2007 Elsevier B.V. All rights reserved.
- ItemSomente MetadadadosEffects of soybean proteinase inhibitors on development of the soil mite Scheloribates praeincisus (Acari : Oribatida)(Springer, 2008-03-01) Simoes, R. A.; Silva-Filho, M. C.; Moura, D. S. [UNIFESP]; Delalibera, I.; Universidade de São Paulo (USP); Universidade Federal de São Paulo (UNIFESP)Proteinase inhibitors (PI) are present in plant tissues, especially in seeds, and act as a defense mechanism against herbivores and pathogens. Serine PI from soybean such as Bowman-Birk (BBPI) and Kunitz have been used to enhance resistance of sugarcane varieties to the sugarcane borer Diatraea saccharalis (Fabricius) (Lepidoptera: Crambidae), the major pest of this crop. the use of these genetically-modified plants (GM) expressing PI requires knowledge of its sustainability and environmental safety, determining the stability of the introduced characteristic and its effects on non-target organisms. the objective of this study was to evaluate direct effects of ingestion of semi-purified and purified soybean PI and GM sugarcane plants on the soil-dwelling mite Scheloribates praeincisus (Berlese) (Acari: Oribatida). This mite is abundant in agricultural soils and participates in the process of organic matter decomposition; for this reason it will be exposed to PI by feeding on GM plant debris. Eggs of S. praeincisus were isolated and after larvae emerged, immatures were fed milled sugarcane leaves added to semi-purified or purified PI (Kunitz and BBPI) or immatures were fed GM sugarcane varieties expressing Kunitz and BBPI type PI or the untransformed near isogenic parental line variety as a control. Developmental time (larva-adult) and survival of S. praeincisus was evaluated. Neither Kunitz nor BBPI affected S. praeincisus survival. On the other hand, ingestion of semi-purified and purified Kunitz inhibitor diminished duration of S. praeincisus immature stages. Ingestion of GM senescent leaves did not have an effect on S. praeincisus immature developmental time and survival, compared to ingestion of leaves from the isogenic parental plants. These results indicate that cultivation of these transgenic sugarcane plants is safe for the non-target species S. praeincisus.
- ItemSomente MetadadadosInhibitory selectivity of canecystatin: a recombinant cysteine peptidase inhibitor from sugarcane(Elsevier B.V., 2004-08-06) Oliva, MLV; Carmona, A. K.; Andrade, S. S.; Cotrin, S. S.; Soares-Costa, A.; Henrique-Silva, F.; Universidade Federal de São Paulo (UNIFESP); Universidade Federal de São Carlos (UFSCar)The cDNA of a cystein peptidase inhibitor was isolated from sugarcane and expressed in Escherichia coli. the protein, named canecystatin, has previously been shown to exert antifungal activity on the filamentous fungus Trichoderma reesei. Herein, the inhibitory specificity of canecystatin was further characterized. It inhibits the cysteine peptidases from plant source papain (K-i = 3.3 nM) and baupain (K-i = 2.1 x 10(-8) M), but no inhibitory effect was observed on ficin or bromelain. Canecystatin also inhibits lysosomal cysteine peptidases such as human cathepsin B (K-i = 125 nM), cathepsin K (K-i = 0.76 nM), cathepsin L (K-i = 0.6 nM), and cathepsin V (K-i = 1.0 nM), but not the aspartyl peptidase cathepsin D. the activity of serine peptidases such as trypsin, chymotrypsin, pancreatic, and neutrophil elastases, and human plasma kallikrein is not affected by the inhibitor, nor is the activity of the metallopeptidases angiotensin converting enzyme and neutral endopeptidase. This is the first report of inhibitory activity of a sugarcane cystatin on cysteine peptidases. (C) 2004 Elsevier Inc. All rights reserved.
- ItemSomente MetadadadosRecombinant expression, purification, and functional analysis of two novel cystatins from sugarcane (Saccharum officinarum)(Elsevier B.V., 2006-06-01) Gianotti, A.; Rios, W. M.; Soares-Costa, A.; Nogaroto, V; Carmona, A. K.; Oliva, MLV; Andrade, S. S.; Henrique-Silva, F.; Universidade Federal de São Carlos (UFSCar); Universidade Federal de São Paulo (UNIFESP)Phytocystatins are cysteine proteinase inhibitors from plants implicated in the endogenous regulation of protein turnover, programmed cell death, and in defense mechanisms against pathogens. To date, only few cystatin genes have been characterized in most plant species. We have previously characterized the protein Canecystatin, the first cystatin described in sugarcane. in an attempt to study novel Canecystatins, we identified two ORFs encoding cystatins (referred as CaneCPI-2 and CaneCPI-3) using the data from the Sugarcane EST genome project. These ORFs were then subcloned and expressed in Escherichia coli using pET28 expression vector. High amounts (similar to 20 mg/L) of pure recombinant proteins were obtained by affinity chromatography in a single step of purification. Polyclonal antibodies against the recombinant Canecystatins were raised, allowing the immunodetection of the endogenous proteins in the plant tissues. Moreover, the proteins were able to inhibit papain in a fluorometric assay with K-i values of 0.2 and 0.25 mu M for CaneCPI-2 and CaneCPI-3, respectively. These findings contribute to a better understanding of the activity of sugarcane cystatins and encourage future activity and structural studies of these proteins. (c) 2005 Elsevier Inc. All rights reserved.