RESUMO
The need to fully exploit fishing resources due to increasing production and consequent waste generation requires research to promote the sustainability of the fishing industry. Fish waste from the industry is responsible for relevant environmental contamination. However, these raw materials contain high amounts of collagen and other biomolecules, being attractive due to their industrial and biotechnological applicability. Thus, to reduce the waste from pirarucu (Arapaima gigas) processing, this study aimed to obtain collagen from pirarucu skin tissue. The extraction process used 0.05 M sodium hydroxide, 10% butyl alcohol, and 0.5 M acetic acid, with extraction temperature of 20°C. The obtained yield was 27.8%, and through sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), it was determined that the collagen obtained was type I. This study showed that collagen solubility was highest at pH 3 and the lowest solubility was at concentrations of 3% sodium chloride. The denaturation temperature of collagen was 38.1°C, and its intact molecular structure was observed using the Fourier transform infrared spectrophotometry technique with an absorption radius of 1. The results showed that it was possible to obtain collagen from pirarucu skin at 20°C, which has the typical characteristics of commercial type I collagen. In conclusion, the procedures used may be considered to be an interesting alternative for collagen extraction, a new product obtained from the processing of fish waste.
Assuntos
Colágeno , Proteínas de Peixes , Animais , Proteínas de Peixes/análise , Proteínas de Peixes/química , Colágeno Tipo I , Pele/química , Peixes , Água DoceRESUMO
The need to fully exploit fishing resources due to increasing production and consequent waste generation requires research to promote the sustainability of the fishing industry. Fish waste from the industry is responsible for relevant environmental contamination. However, these raw materials contain high amounts of collagen and other biomolecules, being attractive due to their industrial and biotechnological applicability. Thus, to reduce the waste from pirarucu (Arapaima gigas) processing, this study aimed to obtain collagen from pirarucu skin tissue. The extraction process used 0.05 M sodium hydroxide, 10% butyl alcohol, and 0.5 M acetic acid, with extraction temperature of 20°C. The obtained yield was 27.8%, and through sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), it was determined that the collagen obtained was type I. This study showed that collagen solubility was highest at pH 3 and the lowest solubility was at concentrations of 3% sodium chloride. The denaturation temperature of collagen was 38.1°C, and its intact molecular structure was observed using the Fourier transform infrared spectrophotometry technique with an absorption radius of 1. The results showed that it was possible to obtain collagen from pirarucu skin at 20°C, which has the typical characteristics of commercial type I collagen. In conclusion, the procedures used may be considered to be an interesting alternative for collagen extraction, a new product obtained from the processing of fish waste.
RESUMO
Abstract 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.
Resumo 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.
Assuntos
Animais , Linguado/fisiologia , Proteínas de Peixes/metabolismo , Proteínas de Peixes/química , Trato Gastrointestinal/enzimologia , Aminopeptidases/metabolismo , Aminopeptidases/química , Temperatura , Estabilidade Enzimática , Brasil , Serina Endopeptidases/metabolismo , Serina Endopeptidases/química , Concentração de Íons de Hidrogênio , Fígado/enzimologiaRESUMO
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.
Assuntos
Aminopeptidases , Proteínas de Peixes , Linguado/fisiologia , Trato Gastrointestinal/enzimologia , Fígado/enzimologia , Serina Endopeptidases , Aminopeptidases/química , Aminopeptidases/metabolismo , Animais , Brasil , Estabilidade Enzimática , Proteínas de Peixes/química , Proteínas de Peixes/metabolismo , Concentração de Íons de Hidrogênio , Serina Endopeptidases/química , Serina Endopeptidases/metabolismo , TemperaturaRESUMO
Cokeromyces recurvatus Poitras was isolated from an endocervical specimen obtained from a 37-year-old, insulin-dependent diabetic. The patient's diabetic condition had been well controlled for 10 years, and she had no other known medical problem. This is only the fourth time that this zygomycete has been recovered from a human source. While there was no evidence of tissue invasion in the present patient, the observation of fungus-like structures in two separate Papanicolaou-stained cervical smears prepared 1 year apart suggests that C. recurvatus may be capable of colonizing endocervical tissue.