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| Lazzari,R.; Uczay,J.; Henriques,J.K.S.; Durigon,E.G.; Kunz,D.F.; Peixoto,N.C.; Fronza,D.. |
| ABSTRACT In fish farming, the use of alternative ingredients has been studied, so that alternative sources can be used to minimize feed costs. This study evaluated the incorporation of grape, orange, guava, and fig residues in diets for silver catfish and its effects on growth, digestive enzymes and body composition. A total of 180 fish (initial mean weight = 22.93±0.75 g) were reared in a recirculation aquaculture system. There was no difference (P>0.05) in the parameters of growth, dry matter, mineral matter, plasma protein, cholesterol, triglycerides, lipase, and trypsin of fish. Glucose levels were higher in fish fed diets containing fig, orange, and grape residue (P<0.05). Lipase activity was higher in fish fed orange residue, compared to guava... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: By-products; Nutrition; Rhamdia quelen. |
| Ano: 2019 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0102-09352019000100323 |
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| Pereira,M.E.; Dörr,F.A.; Peixoto,N.C.; Lima-Garcia,J.F.; Dörr,F.; Brito,G.G.. |
| The present study describes the main characteristics of the proteolytic activities of the velvetbean caterpillar, Anticarsia gemmatalis Hübner, and their sensitivity to proteinase inhibitors and activators. Midguts of last instar larvae reared on an artificial diet were homogenized in 0.15 M NaCl and centrifuged at 14,000 g for 10 min at 4ºC and the supernatants were used in enzymatic assays at 30ºC, pH 10.0. Basal total proteolytic activity (azocasein hydrolysis) was 1.14 ± 0.15 absorbance variation min-1 mg protein-1, at 420 nm; basal trypsin-like activity (N-benzoyl-L-arginine-p-nitroanilide, BApNA, hydrolysis) was 0.217 ± 0.02 mmol p-nitroaniline min-1 mg protein-1. The maximum proteolytic activities were observed at pH 10.5 using azocasein and at pH... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Anticarsia gemmatalis (Lepidoptera: Noctuidae); Azocasein hydrolysis; BApNA hydrolysis; Proteinase inhibitors; Protein digestion; Serine-proteinases. |
| Ano: 2005 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2005001100010 |
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