The performance of Nile tilapia (Oreochromis niloticus) raised in cages furnished with an automatic dispenser, supplied at different frequencies (once per hour and once every two hours) and periods (daytime, nighttime and both) was evaluated. Eighteen 1.0m³ cages were placed into a 2000m² pond, two meters deep with a 5% water exchange. One hundred and seventy tilapias, with initial weight of 16.0±4.9g, were dispersed into each 1m³ cage and the feed ration was adjusted every 21 days with biometry. Data was collected from March to July (autumn and winter). Significant difference to final weight (P<0.05) among treatments was observed. The increase in feeding frequency improves the productive performance of Nile tilapias in cages and permitted better management of the food. The better feed conversion rate for high feeding frequency (24 times day-1) can result in saving up to 360kg of food for each ton of fish produced, increasing the economic sustenance for tilapia culture and suggesting less environmental pollution.

Lipase from Aspergillus sp. obtained by solid-state fermentation (SSF) on wheat bran (LWB), soybean bran (LSB) and soybean bran combined with sugarcane bagasse (LSBBC) were 67.5, 58 and 57.3 U of crude lipase per gram substrate, respectively. The optimum pH of activity and stability of the LWB was between 8 and 9, and the optimum temperature of activity and stability was 50 °C and up to 60 °C, respectively. The LSB and LSBBC showed two peaks of optimum pH (4 and 6) and optimal values of temperature and stability at 50 °C. The LSB was stable in the pH range of 6–7, while LSBBC in the range of pH 4–7. All the enzymes show activities on p-nitrophenyl esters (butyrate, laurate and palmitate). LWB stood out either on the hydrolysis of sunflower oil, presenting 66.1% of the activity over commercial lipase and on the esterification of oleic acid and ethanol, surpassing the activities of the commercial lipases studied. The thin layer chromatography showed that LWB and LSB have produced ethyl esters from corn oil, while LWB produced it from sunflower oil.

This study aimed to evaluate the performance of a commercial protease (Novo-Pro D (NPD)), both in soluble and immobilized forms, in the hydrolysis of proteins (using casein as model protein). Immobilization of the protease NPD on 6% agarose activated with glyoxyl groups for 24 h at 20 °C and pH 10.0 allowed preparing immobilized biocatalyst with around 90% immobilization yield, 92% recovered activity versus small substrate, and a thermal stability 5.3-fold higher than the dialyzed soluble enzyme at 50 °C and pH 8.0. Immobilization times longer than 24 h lead to a decrease in the recovered activity and did not improve the biocatalyst stability. At 50 °C and pH 6.5, the immobilized NPD was around 20-fold more stable than the dialyzed soluble protease. Versus casein, the immobilized NDP presented a 10% level of activity, but it allowed hydrolyzing casein (26 g/L) at 50 °C and pH 6.5 up to a 40% degree of hydrolysis (DH) after 2 h reaction, while under the same conditions, only a 34% DH was achieved with soluble NPD. In addition, the immobilized NPD showed good reusability, maintaining the DH of casein for at least ten 2h-reaction batches.