In order to evaluate the feasibility of dried seaweed Gracilaria lemaneiformis (Bory) as a dietary ingredient for the rabbitfish Siganus canaliculatus (Park), juvenile fish (average weight 15.64 ± 0.15 g) were fed with two isonitrogenous (32% crude protein) and isolipid (8% lipid) diets for 8 weeks, with one diet incorporating 33% of dried G. lemaneiformis (DGL), which accounted for 6% protein and 17% carbohydrate (DGL-diet), and the other containing no DGL (control diet). After 8 weeks, the growth performance and feed utilization efficiency of fish fed with the DGL-diet were inferior to fish fed with the control diet, although some non-specific immunity parameters were better in fish fed with the DGL-diet compared with those of fish fed control diet. Nutritional composition (whole body composition, amino acid, and fatty acid composition in dorsal muscle) except methionine and tyrosine in muscle showed no differences between the two groups. Furthermore, the survival rate of fish and apparent digestibility coefficient of diets were the same between the two groups. These results indicated that incorporation of DGL in diet of S. canaliculatus is feasible, and further studies are recommended to optimize the level of DGL in diet of S. canaliculatus to improve growth performance.
α-Amylase as an important industrial enzyme has been widely used in starch processing, detergent, and paper industries. To improve expression efficiency of recombinant α-amylase from Bacillus licheniformis (B. licheniformis), the α-amylase gene from B. licheniformis was optimized according to the codon usage of Pichia pastoris (P. pastoris) and expressed in P. pastoris. Totally, the codons encoding 305 amino acids were optimized in which a total of 328 nucleotides were changed and the G+C content was increased from 47.6 to 49.2%. The recombinants were cultured in 96-deep-well microplates and screened by a new plate assay method. Compared with the wild-type gene, the optimized gene is expressed at a significantly higher level in P. pastoris after methanol induction for 168 h in 5- and 50-L bioreactor with the maximum activity of 8100 and 11000 U/mL, which was 2.31- and 2.62-fold higher than that by wild-type gene. The improved expression level makes the enzyme a good candidate for α-amylase production in industrial use.
Fish oil (FO) substitution has been studied in many marine carnivorous fish, but seldom in marine herbivorous or omnivorous species. To evaluate the feasibility of using soybean oil (SO) as a dietary lipid and confirm its capability of converting C 18 polyunsaturated fatty acid (PUFA) into long chain polyunsaturated fatty acid (LC-PUFA) in the marine herbivorous teleost Siganus canaliculatus, juvenile fish were fed with four formulated diets differing in lipid composition, with SO accounting for 0.76% (SO0), 23% (SO23), 45% (SO45) and 67% (SO67) of total dietary lipid respectively. After feeding for 8 weeks, growth performance including weight gain, specific growth rate, feed conversion ratio and protein efficiency rate were better in the SO23 and, especially, SO45 groups than in the SO0 and SO67 groups (P < 0.05). Tissue fatty acid compositions were affected by diet, with the liver contents of eicosapentaenoic (EPA), docosapentaenoic (DPA), docosahexaenoic (DHA) acids and total n-3 PUFA displaying parallel changes with the corresponding dietary fatty acids. While the muscle contents of EPA, DPA and total n-3 PUFA between SO0 and SO23 groups, and the liver contents of arachidonic acid (ARA) and 20:4n-3, as well as the muscle content of 20:3n-6 between SO0 and SO45 groups showed no difference, confirming the biosynthesis of LC-PUFA from C 18 precursors in vivo as the contents of corresponding fatty acids in diets SO23/SO45 were much lower than those in diet SO0 (P < 0.05). The results indicate that SO may be a suitable dietary lipid source for S. canaliculatus, and can replace up to 67% or 45% of total dietary FO without negatively compromising growth performance or nutritional quality of fish respectively. Moreover, the study increases our knowledge of FO substitution in marine herbivorous fish.
A gene encoding Rhizopus oryzae lipase containing prosequence (ProROL) was cloned into the pPICZαA and electrotransformed into the Pichia pastoris X-33 strain. The lipase was functionally expressed and secreted in Pichia pastoris with a molecular weight of 35 kDa. The maximum lipase activity of recombinant lipase (rProROL) was 21,000 U/mL, which was obtained in a fed-batch cultivation after 168 h induction with methanol in a 50-L bioreactor. After fermentation, the supernatant was concentrated by ultrafiltration with a 10 kDa cut off membrane and purified with ion exchange chromatography using SP Sepharose Fast Flow chromatography. The optimum pH and temperature of the rProROL were pH 9.0 and 40 °C, respectively. The lipase was stable from pH 4.0 to 9.0 and from 25 to 55 °C. The enzyme activity was enhanced by Ca2+ and inhibited by Hg2+ and Ag+. The lipase showed high activity toward triglyceride-Tripalmitin (C16:0) and triglyceride-Trilaurin (C12:0).
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