Algoritmo SOM com estrutura hierárquica e dinâmica aplicado a compressão de imagens

ln this work the implementation of the SOM (Self Organizing Maps) algorithm or Kohonen neural network is presented in the form of hierarchical structures, applied to the compression of images. The main objective of this approach is to develop an Hierarchical SOM algorithm with static structure and another one with dynamic structure to generate codebooks (books of codes) in the process of the image Vector Quantization (VQ), reducing the time of processing and obtaining a good rate of compression of images with a minimum degradation of the quality in relation to the original image. Both self-organizing neural networks developed here, were denominated HSOM, for static case, and DHSOM, for the dynamic case. ln the first form, the hierarchical structure is previously defined and in the later this structure grows in an automatic way in agreement with heuristic rules that explore the data of the training group without use of external parameters. For the network, the heuristic mIes determine the dynamics of growth, the pruning of ramifications criteria, the flexibility and the size of children maps. The LBO (Linde-Buzo-Oray) algorithm or K-means, one ofthe more used algorithms to develop codebook for Vector Quantization, was used together with the algorithm of Kohonen in its basic form, that is, not hierarchical, as a reference to compare the performance of the algorithms here proposed. A performance analysis between the two hierarchical structures is also accomplished in this work. The efficiency of the proposed processing is verified by the reduction in the complexity computational compared to the traditional algorithms, as well as, through the quantitative analysis of the images reconstructed in function of the parameters: (PSNR) peak signal-to-noise ratio and (MSE) medium squared error

Isolamento de uma quitinase extraída do cefalotórax do camarão marinho Litopenaeus schmitti (BURKENROAD, 1936) : avaliação de suas atividades antimicrobiana e larvicida

Chitinases are enzymes involved in degradation of chitin and are present in a range of organisms, including those that do not contain chitin, such as bacteria, viruses, plants and animals, and play important physiological and ecological roles. Chitin is hydrolyzed by a chitinolytic system classified as: endo-chitinases, exo-chitinases and N-acetyl-b-D-glucosaminidases. In this study a Litochitinase1 extracted from the cephalotorax of the shrimp Litopenaeus Schmitt was purified 987.32 times using ionexchange chromatography DEAE-Biogel and molecular exclusion Sephacryl S-200. These enzyme presented a molecular mass of about 28.5 kDa. The results, after kinetic assay with the Litochitinase1 using as substrate p-nitrophenyl-N-acetyl-b-Dglucosaminideo, showed apparent Km of 0.51 mM, optimal activity at pH ranging from 5.0 to 6.0, optimum temperature at 55°C and stability when pre-incubated at temperatures of 25, 37, 45, 50 and 55°C. The enzyme showed a range of stability at pH 4.0 to 5.5. HgCl2 inhibited Litochitinase1 while MgCl2 enhances its activity. Antimicrobial tests showed that Litochitinase1 present activity against gram-negative bacterium Escherichia coli in the 800 μg/mL concentration. The larvicidal activity against Aedes aegypti was investigated using crude extracts, F-III (50-80%) and Litochitinase1 at 24 and 48 hours. The results showed larvicidal activity in all these samples with EC50 values of 6.59 mg/mL for crude extract, 5.36 mg/mL for F-III and 0.71 mg/mL for Litochitinase1 at 24 hours and 3.22 and 0.49 mg/mL for the F-III and Litochitinase1 at 48 hours, respectively. Other experiments confirmed the presence of chitin in the midgut of Aedes aegypti larvae, which may be suffering the action of Litochitinase1 killing the larvae, but also the absence of contaminating proteins as serine proteinase inhibitors and lectins in the crude extract, F-III and Litochitinase1, indicating that the death of the larvae is by action of the Litochitinase1. We also observed that the enzymes extracted from intestinal homogenate of the larvae no have activity on Litochitinase1. These results indicate that the enzyme can be used as an alternative to control of infections caused by Escherichia coli and reducing the infestation of the mosquito vector of dengue.

Purificação e caracterização de uma ß-N-acetillhexosaminadase extraída do mamífero marinho Sotalia fluviatilis

This report shows 2232 times purification of a βNAcetylhexosaminidase from hepatic extracts from the sea mammal Sotalia fluviatilis homogenate with final recovery of 8,4%. Sequenced steps were utilized for enzyme purification: ammonium sulfate fractionation, Biogel A 1.5 m, chitin, DEAESepharose and hydroxyapatite chromatographies. The protein molecular mass was estimated in 10 kDa using SDSPAGE and confirmed by MALDITOF. It was found to have an optimal pH of 5.0 and a temperature of 60°C. Using pnitrophenylNAcetylβDglycosaminide apparent Km and Vmax values were of 2.72 mM and 0.572 nmol/mg/min, respectively. The enzyme was inhibited by mercury chloride (HgCl2) and sodium dodecil sulfate (SDS)

Caracterização da frequência de atividades aéreas do golfinho-rotador, Stenella longirostris (Gray, 1828), na Baía dos Golfinhos do Parque Nacional Marinho de Fernando de Noronha

The aerial activities, leaps and slaps with parts of the body in the surface of water, are part of the behavioral repertoire of several species of cetaceans. Among them, the spinner dolphin, Stenella longirostris, shows greater diversity in such behavior. For the spinner dolphins of Fernando de Noronha, the aerial activities are classified as vertical and horizontal, with eight patterns to be noted (tail slap, head slap, motor boating, partial leap, leap, spin, tail over head and tail over head with spin) discriminated between these categories. Such behaviors can be used as a parameter to identify behavioral changes, as well as patterns of daily and seasonal activity. In this manner, this study aimed to characterize the frequency in performance of such activity while the dolphins were within the Dolphin Bay of Fernando de Noronha, and verify possible daily and seasonal hourly fluctuations on such behaviors. The data analyzed in this study was acquired during the period of January 2006 through December 2010, totaling 1431 days of observation from land set point, with 113027 aerial activities registered, daily average of 72,27 (SD=96,10). During 5478h and 54 min of observation the horizontal aerial activity was the most observed and rotation was the most executed pattern. Greater frequency of execution of aerial activity was observed in adults, but for both adults and calves, was observed a predominance of horizontal activities, with spin being the pattern most executed. Positive correlation was observed between the amount of aerial activity performed and the number of animals inside the Bay. Hourly daily fluctuation was observed in the expression of aerial activities by spinner dolphins, and was observed a peak of activity between 8h and 8h59min for the overall frequency relative of aerial activities, as well as for the categories and patterns. Seasonal differences were observed between the rainy and dry season with the greater amount of activity being observed during the rainy season. Nevertheless, the same profile of frequency relative of aerial activity was observed in both seasons with the peak amount being during the same period. When discriminated the aerial activities in categories and patterns, for both seasons, there was a similar pattern of hourly fluctuation; for most of parameters, higher frequency relative of execution of aerial activity remain between 8h and 8h59min

Isolamento de uma quitinase extraída do cefalotórax do camarão marinho Litopenaeus schmitti (BURKENROAD, 1936) : avaliação de suas atividades antimicrobiana e larvicida

Chitinases are enzymes involved in degradation of chitin and are present in a range of organisms, including those that do not contain chitin, such as bacteria, viruses, plants and animals, and play important physiological and ecological roles. Chitin is hydrolyzed by a chitinolytic system classified as: endo-chitinases, exo-chitinases and N-acetyl-b-D-glucosaminidases. In this study a Litochitinase1 extracted from the cephalotorax of the shrimp Litopenaeus Schmitt was purified 987.32 times using ionexchange chromatography DEAE-Biogel and molecular exclusion Sephacryl S-200. These enzyme presented a molecular mass of about 28.5 kDa. The results, after kinetic assay with the Litochitinase1 using as substrate p-nitrophenyl-N-acetyl-b-Dglucosaminideo, showed apparent Km of 0.51 mM, optimal activity at pH ranging from 5.0 to 6.0, optimum temperature at 55°C and stability when pre-incubated at temperatures of 25, 37, 45, 50 and 55°C. The enzyme showed a range of stability at pH 4.0 to 5.5. HgCl2 inhibited Litochitinase1 while MgCl2 enhances its activity. Antimicrobial tests showed that Litochitinase1 present activity against gram-negative bacterium Escherichia coli in the 800 μg/mL concentration. The larvicidal activity against Aedes aegypti was investigated using crude extracts, F-III (50-80%) and Litochitinase1 at 24 and 48 hours. The results showed larvicidal activity in all these samples with EC50 values of 6.59 mg/mL for crude extract, 5.36 mg/mL for F-III and 0.71 mg/mL for Litochitinase1 at 24 hours and 3.22 and 0.49 mg/mL for the F-III and Litochitinase1 at 48 hours, respectively. Other experiments confirmed the presence of chitin in the midgut of Aedes aegypti larvae, which may be suffering the action of Litochitinase1 killing the larvae, but also the absence of contaminating proteins as serine proteinase inhibitors and lectins in the crude extract, F-III and Litochitinase1, indicating that the death of the larvae is by action of the Litochitinase1. We also observed that the enzymes extracted from intestinal homogenate of the larvae no have activity on Litochitinase1. These results indicate that the enzyme can be used as an alternative to control of infections caused by Escherichia coli and reducing the infestation of the mosquito vector of dengue.

Purificação e caracterização de uma ß-N-acetillhexosaminadase extraída do mamífero marinho Sotalia fluviatilis

This report shows 2232 times purification of a βNAcetylhexosaminidase from hepatic extracts from the sea mammal Sotalia fluviatilis homogenate with final recovery of 8,4%. Sequenced steps were utilized for enzyme purification: ammonium sulfate fractionation, Biogel A 1.5 m, chitin, DEAESepharose and hydroxyapatite chromatographies. The protein molecular mass was estimated in 10 kDa using SDSPAGE and confirmed by MALDITOF. It was found to have an optimal pH of 5.0 and a temperature of 60°C. Using pnitrophenylNAcetylβDglycosaminide apparent Km and Vmax values were of 2.72 mM and 0.572 nmol/mg/min, respectively. The enzyme was inhibited by mercury chloride (HgCl2) and sodium dodecil sulfate (SDS)