• Animal Bioscience
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• v.37 no.8
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• pp.1408-1417
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• 2024

Objective: This study investigated the effects of dietary supplementation with lysolecithins (LPC) on growth performance, nutrient digestibility, blood profiles, immunity, and liver health in broiler chickens. Methods: A cohort of 240 one-day-old male Arbor Acres broilers of comparable weight was divided into four treatment groups, each comprising six replicates of 10 birds. The groups were defined as follows: positive control with recommended metabolizable energy (PC+ME), negative control with 90 kcal/kg reduced ME (NC+ME), PC supplemented with 300 mg/kg LPC (PC+LPC), and NC supplemented with 300 mg/kg LPC (NC+LPC). Results: LPC supplementation led to a statistically significant reduction in the feed conversion ratio (p = 0.05) and a decrease in the proportion of abdominal fat and the liver (p<0.05). Digestibility of dry matter was also enhanced (p<0.05). Malondialdehyde concentrations in the liver were significantly reduced by LPC (p<0.01), with a noteworthy interaction between energy levels and LPC affecting this reduction (p<0.05). Serum levels of interleukin-6 were reduced on day 21, and both endotoxin and interleukin-6 levels were lower on day 42. Notably, a significant interaction was observed between the energy levels and LPC on relative liver weight and endotoxin concentrations in the serum (p<0.05). Conclusion: The study concluded that LPC positively affects growth performance, nutrient digestibility, immune response, and antioxidative capacity in broiler chickens, affirming its value as a beneficial feed additive in poultry nutrition.

• Journal of Microbiology and Biotechnology
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• v.30 no.8
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• pp.1244-1251
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• 2020

Phospholipase A₂ (PLA₂) from Streptomyces violaceoruber is a lipolytic enzyme used in a wide range of industrial applications including production of lysolecithins and enzymatic degumming of edible oils. We have therefore investigated expression and secretion of PLA₂ in two workhorse microbes, Pichia pastoris and Escherichia coli. The PLA₂ was produced to an activity of 0.517 ± 0.012 U/ml in the culture broth of the recombinant P. pastoris. On the other hand, recombinant E. coli BL21 star (DE3), overexpressing the authentic PLA₂ (P-PLA₂), showed activity of 17.0 ± 1.3 U/ml in the intracellular fraction and 21.7 ± 0.7 U/ml in the culture broth. The extracellular PLA2 activity obtained with the recombinant E. coli system was 3.2-fold higher than the corresponding value reached in a previous study, which employed recombinant E. coli BL21 (DE3) overexpressing codon-optimized PLA₂. Finally, we observed that the extracellular PLA₂ from the recombinant E. coli P-PLA₂ culture was able to hydrolyze 31.1 g/l of crude soybean lecithin, an industrial substrate, to a conversion yield of approximately 95%. The newly developed E. coli-based PLA₂ expression system led to extracellular production of PLA₂ to a productivity of 678 U/l·h, corresponding to 157-fold higher than that obtained with the P. pastoris-based system. This study will contribute to the extracellular production of a catalytically active PLA₂.