Alkaline proteinase from intestine of Nile tilapia (Oreochromis niloticus)

Bezerra, Ranilson S.; Lins, Eduardo J.F.; Alencar, Rodrigo B.; Paiva, Patrícia Maria Guedes; Chaves, M. E. C.; Carvalho, Luiz Bezerra de

doi:10.1016/j.procbio.2004.06.066

Cited by 124 publications

(167 citation statements)

References 24 publications

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“…It is known that Hg 2+ is among ions that act on sulfhydryl residues in proteins (Male et al 1995). The inhibition caused by this ion suggests the relevance of sulfhydryl residues for the catalytic action of most proteases (Bezerra et al 2005). The effects of Cu 2+ and Mn 2+ (respectively, 4 % and 37.5 %) proved to be stronger than those recorded for L. mormyrus enzyme (respectively, 82 % and 69 %) (El-Hadj Ali et al 2011 …”

Section: Effect Of Temperature On Protease Activity and Stabilitymentioning

confidence: 94%

Zebra blenny (Salaria basilisca) viscera as a source of solvent-stable proteases: characteristics, potential application in the deproteinization of shrimp wastes and evaluation in liquid laundry commercial detergents

et al. 2012

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The present study describes the characterization of crude protease extract from zebra blenny (Salaria basilisca) and its evaluation in liquid detergent and shrimp waste deproteinization. At least five caseinolytic proteases clear bands were observed in zymogram. The crude alkaline protease showed optimum activity at pH 8.0 and 60°C, and it was highly stable over a wide range of pH from 6.0 to 11.0. Proteolytic enzymes showed extreme stability towards non-ionic surfactants (5 % Tween 80 and 5 % Triton X-100) and oxidizing agents (1 % sodium perborate), and relative stability towards anionic surfactant (1 % Sodium dodecyl sulfate (SDS)). They also showed high stability and compatibility with various laundry liquid detergents from Tunisian market. Furthermore, the crude enzyme was stable towards several organic solvents and retained more than 50 % of its original activity after 30 days of incubation at 30°C in the presence of 50 % (v/v) dimethylsulfoxide (DMSO). Further, proteases from zebra blenny viscera were found to be effective in the deproteinization of shrimp wastes. The protein removal after 3 h at 40°C with an enzyme/substrate ratio (E/S) of 5 U/mg protein was about 77 %.

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Section: Effect Of Temperature On Protease Activity and Stabilitymentioning

confidence: 94%

Zebra blenny (Salaria basilisca) viscera as a source of solvent-stable proteases: characteristics, potential application in the deproteinization of shrimp wastes and evaluation in liquid laundry commercial detergents

et al. 2012

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“…Triplicate samples (30 µL) of crude intestine extract were incubated with substrate solution (50 µL) for 60 min at 25 °C in a microtube (Bezerra et al, 2005). The reaction was stopped with the addition of 10% trichloroacetic acid (240 µL) and the mixture was centrifuged at 8,000 × g for 5 min.…”

Section: Non-specific Enzyme Assaysmentioning

confidence: 99%

“…Thermal stability was evaluated by analyses of enzymatic activity at 25 °C after pre-incubation for 30 minutes at temperatures ranging from 25-70 °C (Bezerra et al, 2005). All values were presented as means ± standard deviations.…”

Section: Effects Of Ph and Temperature On Enzyme Activitymentioning

confidence: 99%

“…The Brazilian flounder, Paralichthys orbignyanus (Valenciennes, 1842) is a native species that inhabits coastal and estuarine areas from Rio de Janeiro -Brazil, to Mar del Plata -Argentina; however, is found in greater abundance in southern Brazil (Bianchini et al, 2010). The flounder fishery industry in the southern region of Brazil has been considered an important resource, however in the last few years has stagnated in capture rates (Brasil, 2010).…”

Section: Introductionmentioning

confidence: 99%

“…Thus, aquaculture for this species may be considered as an alternative resource to increase market supply (Sampaio et al, 2008). Reproduction and larviculture of Brazilian flounder is well established (Bianchini et al, 2010), and the effects of salinity on growth are also known (Sampaio et al, 2007); these represent important features to be considered in a new species for coastal and estuarine aquaculture. However, there is a lack of current literature related to the digestive physiology and nutritional requirements of this species.…”

Section: Introductionmentioning

confidence: 99%

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Characterization of digestive enzymes from captive Brazilian flounder Paralichthys orbignyanus

et al. 2017

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Knowledge of specific enzyme activity, along with animal habits and digestive capacity is essential in formulating an appropriate diet for any species. In this study, we evaluated and characterized the activity of digestive enzymes present in the liver, intestine, and stomach of Paralichthys orbignyanus. The effects of pH and temperature on enzyme activity were also evaluated via the use of specific substrates. The use of specific substrates and inhibitors showed strong evidence of the presence of trypsin (BApNA= 0.51 ± 0.2 mU mg -1 ), chimotrypsin (SApNA= 2.62 ± 1.8 mU mg -1 ), and aminopeptidases (Leu-p-Nan =0.9709 ± 0.83 mU mg -1 ) in the intestine. Optimum pH for the activity of trypsin, chemotrypsin, leucino aminopeptidase, amilase, and pepsin were 9.5, 9.0, 8.0, 7.5, and 3.5, respectively, while optimum temperatures were 50, 50, 50, 40, and 45 °C, respectively. These results provide additional information regarding the biology of Brazilian flounder and can be used as a basis for further studies regarding fish feeding physiology.Keywords: trypsin, protease, digestive tract. Caracterização de enzimas digestivas do linguado brasileiro de cativeiro Paralichthys orbignyanusResumo O conhecimento da atividade enzimática é essencial para formular uma correta dieta específica para espécie, além de estarem correlacionadas com o hábito da alimentação e capacidade digestive. Neste estudo determinamos e caracterizamos a atividade enzimática presente no intestino, estômago e fígado do linguado Paralichthys orbignyanus. Os efeitos da temperatura e pH sobre a atividade enzimática também foram avaliados utilizando substratos específicos. O uso de substratos e inibidores específicos mostrou uma forte evidência da presença da tripsina (BApNA = 0,51 ± 0,2 mU mg-1), quimotripsina (SAPNA = 2,62 ± 1,8 mU mg-1), e as aminopeptidases (Leu-p-Nan = 0,97 ± 0,83 mU mg-1) no intestino. O pH ótimo observado para a atividade de tripsina, quimotripsina, leucino aminopeptidase, amilase e pepsina foi 9,5, 9,0, 8,0, 7,5 e 3,5, respectivamente. A temperatura ótima observada foi 50, 50, 50, 40 e 45 °C, respectivamente. Estes resultados fornecem informações adicionais sobre a biologia do linguado brasileiro e pode ser usado como base para novos estudos sobre fisiologia alimentar.Palavras-chave: tripsina, proteases, trato digestório.Candiotto, F.B. et al.

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Characterization of protease and effects of temperature and salinity on the biochemical changes during fermentation of Antarctic krill

et al. 2017

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Alkaline proteinase from intestine of Nile tilapia (Oreochromis niloticus)

Cited by 124 publications

References 24 publications

Zebra blenny (Salaria basilisca) viscera as a source of solvent-stable proteases: characteristics, potential application in the deproteinization of shrimp wastes and evaluation in liquid laundry commercial detergents

Zebra blenny (Salaria basilisca) viscera as a source of solvent-stable proteases: characteristics, potential application in the deproteinization of shrimp wastes and evaluation in liquid laundry commercial detergents

Characterization of digestive enzymes from captive Brazilian flounder Paralichthys orbignyanus

Characterization of protease and effects of temperature and salinity on the biochemical changes during fermentation of Antarctic krill

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