Purificação e caracterização parcial de uma B-D glicosidade de Artemia franciscana com ação sobre celobiose e lactose

-D-glucosidase (EC 3.2.1.21) is one of the most interesting glycosidases, especially for hydrolysis cellobiose releasing glucose, is last step degradation of cellulose. This function makes the -D-glucosidase is of great interest as a versatile industrial biocatalyst, being critical to various bio-treatment / biorefinery processes, such as bioethanol production. Hen in the report, a -D-glucosidase was extracts from protein extracted of the invertebrate marine Artemia franciscana was purified and characterized with a combination of precipitation with ammonium sulfate (0 - 30%, 30 to 50%, 50 to 80%), the fraction saturated in the range of 30 to 50% (called F-II) was applied in a molecular exclusion chromatography, in Sephacryl S-200, the fractions corresponding to the first peak of activity of -D-glucosidase were gathered and applied in a chromatography of ion exchange in Mono Q; the third peak this protein obtained chromatography, which coincides with the peak of activity of -D-glucosidase was held and applied in a gel filtration chromatography Superose 12 where the first peak protein, which has activity of -D-glucosidase was rechromatography on Superose 12. This enzyme is probably multimerica, consisting of three subunit molecular mass of 52.7 kDa (determined by SDS-PAGE) with native molecular mass of 157 kDa (determined by gel filtration chromatography on Superose 12 under the system FPLC). The enzyme was purified 44.09 times with a recovery of 1.01%. Using up p-nitrophenyl-β-D-glucopiranoside as substrate obtained a Km apparent of 0.229 mM and a Vmax of 1.109 mM.60min-1.mL-1mM. The optimum pH and optimum temperature of catalysis of the synthetic substrate were 5.0 and 45 °C, respectively. The activity of the -D-glucosidase was strongly, inhibited by silver nitrate and N- etylmaleimide, this inhibition indicates the involvement of radical sulfidrila the hydrolysis of synthetic substrate. The -D-glucosidase of Artemia franciscana presented degradativa action on celobiose, lactose and on the synthetic substrate -nitrophenyl-β-D-glucopiranoside indicating potential use of this enzyme in the industry mainly for the production of bioethanol (production of alcohol from the participating cellulose), and production hydrolysate milk (devoid of milk lactose)

Geração de casos de teste a partir de especificações B

With the increasing complexity of software systems, there is also an increased concern about its faults. These faults can cause financial losses and even loss of life. Therefore, we propose in this paper the minimization of faults in software by using formally specified tests. The combination of testing and formal specifications is gaining strength in searches mainly through the MBT (Model-Based Testing). The development of software from formal specifications, when the whole process of refinement is done rigorously, ensures that what is specified in the application will be implemented. Thus, the implementation generated from these specifications would accurately depict what was specified. But not always the specification is refined to the level of implementation and code generation, and in these cases the tests generated from the specification tend to find fault. Additionally, the generation of so-called "invalid tests", ie tests that exercise the application scenarios that were not addressed in the specification, complements more significantly the formal development process. Therefore, this paper proposes a method for generating tests from B formal specifications. This method was structured in pseudo-code. The method is based on the systematization of the techniques of black box testing of boundary value analysis, equivalence partitioning, as well as the technique of orthogonal pairs. The method was applied to a B specification and B test machines that generate test cases independent of implementation language were generated. Aiming to validate the method, test cases were transformed manually in JUnit test cases and the application, created from the B specification and developed in Java, was tested. Faults were found with the execution of the JUnit test cases

Gravitomagnetismo e o teste da sonda gravidade B

The so-called gravitomagnetic field arised as an old conjecture that currents of matter (no charges) would produce gravitational effects similar to those produced by electric currents in electromagnetism. Hans Thirring in 1918, using the weak field approximation to the Einsteins field equations, deduced that a slowly rotating massive shell drags the inertial frames in the direction of its rotation. In the same year, Joseph Lense applied to astronomy the calculations of Thirring. Later, that effect came to be known as the Lense- Thirring effect. Along with the de Sitter effect, those phenomena were recently tested by a gyroscope in orbit around the Earth, as proposed by George E. Pugh in 1959 and Leonard I. Schiff in 1960. In this dissertation, we study the gravitational effects associated with the rotation of massive bodies in the light of the Einsteins General Theory of Relativity. With that finality, we develop the weak field approximation to General Relativity and obtain the various associated gravitational effects: gravitomagnetic time-delay, de Sitter effect (geodesic precession) and the Lense-Thirring effect (drag of inertial frames). We discus the measures of the Lense-Thirring effect done by LAGEOS Satellite (Laser Geodynamics Satellite) and the Gravity Probe B - GPB - mission. The GPB satellite was launched into orbit around the Earth at an altitude of 642 km by NASA in 2004. Results presented in May 2011 clearly show the existence of the Lense-Thirring effect- a drag of inertial frames of 37:2 7:2 mas/year (mas = milliarcsec)- and de Sitter effect - a geodesic precession of 6; 601:8 18:3 mas/year- measured with an accuracy of 19 % and of 0.28 % respectively (1 mas = 4:84810��9 radian). These results are in a good agreement with the General Relativity predictions of 41 mas/year for the Lense-Thirring effect and 6,606.1 mas/year for the de Sitter effect.

Purificação e caracterização parcial de uma B-D glicosidase de Artemia franciscana com ação sobre celobiose e lactose

-D-glucosidase (EC 3.2.1.21) is one of the most interesting glycosidases, especially for hydrolysis cellobiose releasing glucose, is last step degradation of cellulose. This function makes the -D-glucosidase is of great interest as a versatile industrial biocatalyst, being critical to various bio-treatment / biorefinery processes, such as bioethanol production. Hen in the report, a -D-glucosidase was extracts from protein extracted of the invertebrate marine Artemia franciscana was purified and characterized with a combination of precipitation with ammonium sulfate (0 - 30%, 30 to 50%, 50 to 80%), the fraction saturated in the range of 30 to 50% (called F-II) was applied in a molecular exclusion chromatography, in Sephacryl S-200, the fractions corresponding to the first peak of activity of -D-glucosidase were gathered and applied in a chromatography of ion exchange in Mono Q; the third peak this protein obtained chromatography, which coincides with the peak of activity of -D-glucosidase was held and applied in a gel filtration chromatography Superose 12 where the first peak protein, which has activity of -D-glucosidase was rechromatography on Superose 12. This enzyme is probably multimerica, consisting of three subunit molecular mass of 52.7 kDa (determined by SDS-PAGE) with native molecular mass of 157 kDa (determined by gel filtration chromatography on Superose 12 under the system FPLC). The enzyme was purified 44.09 times with a recovery of 1.01%. Using up p-nitrophenyl-β-D-glucopiranoside as substrate obtained a Km apparent of 0.229 mM and a Vmax of 1.109 mM.60min-1.mL-1mM. The optimum pH and optimum temperature of catalysis of the synthetic substrate were 5.0 and 45 °C, respectively. The activity of the -D-glucosidase was strongly, inhibited by silver nitrate and N- etylmaleimide, this inhibition indicates the involvement of radical sulfidrila the hydrolysis of synthetic substrate. The -D-glucosidase of Artemia franciscana presented degradativa action on celobiose, lactose and on the synthetic substrate -nitrophenyl-β-D-glucopiranoside indicating potential use of this enzyme in the industry mainly for the production of bioethanol (production of alcohol from the participating cellulose), and production hydrolysate milk (devoid of milk lactose)