Preliminary evaluation of purified lignin and hemicellulose as prebiotics candidates for Atlantic Salmon,Salmo salar L.

A study was conducted to investigate the potential of purified lignin and hemicellulose as prebiotics in diets for Atlantic salmon, Salmo salar L., postsmolt in seawater (30 ppt) at 14.9 ± 1.2°C. Triplicate groups of fish (initial individual body mass of 101.6 ± 1.2 g) were fed either the fishmeal-dense (32% of fishmeal) control diet (A) or one of the nine diets (15% fishmeal) supplemented with lignin:hemicellulose ratios (% diet:% diet) of 0.05:0 (B), 0.25:0 (C), 0.50:0 (D), 1.00:0 (E), 0:0.05 (F), 0:0.25 (G), 0:0.50 (H), 0.05:0.25 (I), and 0.25:0.50 (J) for 12 weeks in a complete randomized experimental design. At the end of the experiment, the thermal-unit growth coefficient (TGC) was significantly lower in salmon fed diets with 0.50% and 1.00% purified lignin than those fed the control diet, while there was no significant difference between the other treatments and the control diet (P < 0.05). The feed efficiency (FE) was significantly lower in salmon fed diets with 0.50% and 1.00% purified lignin and 0.05% hemicellulose than those fed the control diet, while there was no significant difference between the other treatments and the control diet (P < 0.05). The hepatosomatic index (HSI), intestinal villus length, and apparent digestibility coefficient (ADC) of nutrients in diets were similar (P > 0.05) among all the diets. This study demonstrated that inclusions of up to 0.25% of dietary purified lignin alone, and 0.25%–0.50% of dietary hemicellulose alone or in combination with dietary lignin can be considered as candidate prebiotics in Atlantic salmon nutrition.     

PrPSc spreading patterns in the brain of sheep linked to different prion types

ABSTRACT: Scrapie in sheep and goats has been known for more than 250 years and belongs nowadays to the so-called prion diseases that also include e.g. bovine spongiform encephalopathy in cattle (BSE) and Creutzfeldt-Jakob disease in humans. According to the prion hypothesis, the pathological isoform (PrPSc) of the cellular prion protein (PrPc) comprises the essential, if not exclusive, component of the transmissible agent. Currently, two types of scrapie disease are known - classical and atypical/Nor98 scrapie. In the present study we examine 24 cases of classical and 25 cases of atypical/Nor98 scrapie with the sensitive PET blot method and validate the results with conventional immunohistochemistry. The sequential detection of PrPSc aggregates in the CNS of classical scrapie sheep implies that after neuroinvasion a spread from spinal cord and obex to the cerebellum, diencephalon and frontal cortex via the rostral brainstem takes place. We categorize the spread of PrPSc into four stages: the CNS entry stage, the brainstem stage, the cruciate sulcus stage and finally the basal ganglia stage. Such a sequential development of PrPSc was not detectable upon analysis of the present atypical/Nor98 scrapie cases. PrPSc distribution in one case of atypical/Nor98 scrapie in a presumably early disease phase suggests that the spread of PrPSc aggregates starts in the di- or telencephalon. In addition to the spontaneous generation of PrPSc, an uptake of the infectious agent into the brain, that bypasses the brainstem and starts its accumulation in the thalamus, needs to be taken into consideration for atypical/Nor98 scrapie.