Evaluation of a Lecithin Supplementation on Growth Performance, Meat Quality, Lipid Metabolism, and Cecum Microbiota of Broilers

The present study was conducted to evaluate the effects of lecithin on the performance, meat quality, lipid metabolism, and cecum microbiota of broilers. One hundred and ninety-two one-day-old AA broilers with similar body weights (38 ± 1.0 g) were randomly assigned to two groups with six replicates of sixteen birds each and were supplemented with 0 and 1 g/kg of lecithin for forty-two days. Performance and clinical observations were measured and recorded throughout the study. Relative organ weight, meat quality, lipid-related biochemical parameters and enzyme activities were also measured. Compared with broilers in the control group, broilers in the lecithin treatment group showed a significant increase in L* value and tenderness (p < 0.05). Meanwhile, the abdominal adipose index of broilers was markedly decreased in lecithin treatment after 42 days (p < 0.05). In the lipid metabolism, broilers in the lecithin treatment group showed a significant increase in hepatic lipase and general esterase values at 21 days compared with the control group (p < 0.05). Lower Firmicutes and higher Bacteroidetes levels in phylum levels were observed in the lecithin treatment group after 21 and 42 days. The distribution of lactobacillus, clostridia, and rikenella in genus levels were higher in the lecithin treatment group after 21 and 42 days. No statistically significant changes were observed in performance, relative organ weight, or other serum parameters (p > 0.05). These results indicate that supplementation with lecithin significantly influence the lipid metabolism in broilers at 21 and 42 days, which resulted in the positive effect on the meat color, tenderness, and abdominal adipose in broilers.

Purification of a chymotrypsin-like enzyme present on adult Schistosoma mansoni worms from infected mice and its characterization as a host carboxylesterase

SUMMARYA serine protease-like enzyme found in detergent extracts of Schistosoma mansoni adult worms perfused from infected mice has been purified from mouse blood and further characterized. The enzyme is approximately 85 kDa and hydrolyses N-acetyl-DL-phenylalanine β-naphthyl–ester, a chromogenic substrate for chymotrypsin-like enzymes. The enzyme from S. mansoni worms appears to be antigenically and enzymatically similar to a molecule that is present in normal mouse blood and so is seemingly host-derived. The enzyme was partially purified by depleting normal mouse serum of albumin using sodium chloride and cold ethanol, followed by repeated rounds of purification by one-dimensional sodium dodecyl sulphate polyacrylamide gel electrophoresis. The purified material was subjected to tandem mass spectrometry and its derived peptides found to belong to mouse carboxylesterase 1C. Its ability to hydrolyse α- or β-naphthyl acetates, which are general esterase substrates, has been confirmed. A similar carboxylesterase was purified and characterized from rat blood. Additional evidence to support identification of the enzyme as a carboxylesterase has been provided. Possible roles of the enzyme in the mouse host–parasite relationship could be to ease the passage of worms through the host's blood vessels and/or in immune evasion.

A Study on the Toxicity of a Medicinal Plant, Artemisia Annua L. (Asteracea) Extracts to the Sunn Pest, Eurygaster Integriceps Puton (Hemiptera: Scutelleridae)

A Study on the Toxicity of a Medicinal Plant,Artemisia AnnuaL. (Asteracea) Extracts to the Sunn Pest,Eurygaster IntegricepsPuton (Hemiptera: Scutelleridae)A methanolic extract ofArtemisia annuawas obtained to evaluate its insecticidal activities against the sunn pest (Eurygaster intefriceps). Also, the responses of general esterase (EST), glutathione S-transferase (GST), alkaline phosphatase (ALP), acid phosphatase (ACP), acethylcholinesterase (AChE) to the plant extract were investigated. Topical application of plant extract on adults showed that the mortality was dose-dependent i.e. with increasing of plant extract concentrations more mortality achieved. Esterase and GST activities were increased in the first 24 h post-treatment. However, the enzymes activities were decreased after 24 h until 72 h. The activities of ALP, ACP and AChE in insect body decreased significantly and inhibition was higher along with increasing concentrations of plant extract. Isozyme electrophoresis profiles indicated that responses of isozymes (EST and GST) to plant extract were decreased after 48 h exposure to extract so that some enzymes bands disappeared. The results indicated that the highest concentration ofA. annuaextract was the most toxic among the four extracts. The decline of the detoxification ability in insects' tissues might be the main reason for the insecticidal activities.

Purification and properties of lysophospholipase isoenzymes from pig gastric mucosa

Two lysophospholipases, named gastric lysophospholipases I and II (enzymes I and II), were purified 3730- and 2680-fold from pig gastric mucosa. The preparations showed 22 and 23 kDa single protein bands on SDS/PAGE respectively. Both enzymes lacked transacylase activity and appeared to exist as monomers. Their activities were not affected by Ca2+, Mg2+ or EDTA. Enzyme I was most active at pH 8.5 and hydrolysed a variety of lysophospholipids including acidic lysophospholipids and the acyl analogue of platelet-activating factor, whereas enzyme II was most active at pH 8 and its activity was confined to lysophosphatidylcholine and lysophosphatidylethanolamine. When 1-palmitoylglycerophosphocholine was used as substrate, enzymes I and II showed half-maximal activities at 11 and 12 microM respectively. The enzymes exhibited no phospholipase B, lipase or general esterase activity. Enzyme II was significantly inhibited by lysophosphatidic acid whereas enzyme I was only moderately inhibited. Peptide mapping with V8 protease and papain revealed structural dissimilarity between the two enzymes. Antiserum raised against enzyme I did not recognize enzyme II, but did recognize the small-sized lysophospholipase purified from rat liver. Anti-(enzyme II) consistently did not cross-react with enzyme I or the liver enzyme. These antisera specifically recognized neither the 60 kDa lysophospholipase transacylase purified from liver nor any peritoneal macrophage protein. Thus gastric mucosa contains two different small-sized lysophospholipases: one is closely related to the small-sized lysophospholipase of liver, but the other appears to be a novel isoform.

Pyrethroid and organophosphate resistance in the tobacco whitefly Bemisia tabaci (Homoptera: Aleyrodidae)

Eleven strains of Bemisia tabaci (Gennadius), including a laboratory susceptible strain, were bioassayed as adults with three organophosphorus (OP) insecticides, three pyrethroids and one OP/pyrethroid combination. The contemporary strains were from diverse geographical areas and hosts and included examples of the A-, B-, and non-B-biotypes. All recent collections were multi-resistant to these insecticides which have been used extensively for their control. The patterns of cross-resistance for the OPs were clear but less so for the pyrethroids. All populations that resisted profenofos and cypermethrin also resisted the combination of profenofos and cypermethrin. Although the importance of selection pressure on levels of resistance was not easily quantifiable the highly selected populations exhibited the highest levels of resistance. The significant within, as well as between, biotype variation in resistance factors clearly indicated that insecticide resistance and biotype were not directly related. The roles of acetylcholinesterase sensitivity and general esterase activity in resistance to OPs and pyrethroids are discussed.