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1.
An Acad Bras Cienc ; 86(3): 1063-76, 2014 Sep.
Artigo em Inglês | MEDLINE | ID: mdl-25211098

RESUMO

Ecological modeling has been used as a tool to estimate potential impacts caused by aquaculture to the surrounding environment. In this work, a mathematical model was applied to estimate the maximum amount of pink shrimp (Farfantepenaeus paulensis) culture units (3,100m2 pen enclosures) that could be installed at two shallow estuarine bays of Patos Lagoon (known as Coreia and Porto do Rei) with no significant effects on either water quality or viability of the culture system. To calibrate the model, information about the culture of Litopenaeus vannamei and F. paulensis as well as field data (influence of netting material, water current speed and nitrogen concentrations) were used. Under a bad scenario (water current velocity of 0.01m s-1 and a mesh clogging effect of 40%), it would be possible to install up to 29 pens at the Coreia bay, and 39 pens at the Porto do Rei bay. Results indicate that the model was useful in determining the maximum number of culture units that could be installed at these bays, and thus have the potential to become an important tool in the definition of environmental management strategies in relation to aquaculture development.


Assuntos
Aquicultura/métodos , Modelos Biológicos , Penaeidae , Animais , Aquicultura/estatística & dados numéricos , Brasil , Conservação dos Recursos Naturais , Estuários
2.
Food Chem ; 129(3): 777-82, 2011 Dec 01.
Artigo em Inglês | MEDLINE | ID: mdl-25212298

RESUMO

An alkaline peptidase was purified from the viscera of the silver mojarra (Diapterus rhombeus) in a three-step process: heat treatment, ammonium sulphate fractionation and molecular exclusion chromatography (Sephadex® G-75), with final specific activity 86-fold higher than the enzyme extract and yield of 22.1%. The purified enzyme had an estimated molecular mass of 26.5kDa and NH2-terminal amino acid sequence IVGGYECTMHSEAHE. Higher enzyme activity was observed at pH 8.5 and between 50 and 55°C. The enzyme was completely inactivated after 30min at 55°C and it was significantly more stable at alkaline pH. Km, Kcat and Kcat·Km(-1) values, using BApNA as substrate, were 0.266mM, 0.93s(-1) and 3.48mM(-1)s(-1), respectively. Enzyme activity increased in the presence of the ions (1mM) K(+), Li(+) and Ca(2+), but was inhibited by Fe(2+), Cd(2+), Cu(2+), Al(3+), Hg(2+), Zn(2+) and Pb(2+) as well as by the trypsin inhibitors TLCK and benzamidine.

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