AN ELECTROPHORETIC STUDY ON SERUM PROTEINS IN ARABIAN RACE HORSES NATURALLY INFECTED WITH Babesia equi

Electrophoretic patterns of serum protein in 12 Arabian race horses acutely infected with Babesia equi revealed a significant decrease in albumin (P<0.01) and beta globulins (P<0.05) where, alpha globulins fractions significantly (P<0.01) increased. No significant (P>0.05) changes were recorded in gamma globulins fractions and total serum protein.

El Gueddid, a traditional Algerian dried salted meat: Physicochemical, microbiological characteristics and proteolysis intensity during its manufacturing process and ripening

El Gueddid is a traditional salted and dried meat with high popularity in Algeria. It is used as an ingredient in various dishes. In this study, different samples of El Gueddid were analyzed at different processing times to follow up their microbiological and physicochemical properties. Changes in the protein profile were also demonstrated by electrophoretic study of myofibrillar proteins. Microbiological determinations included the total viable count, coliforms, Staphylococci, lactic acid bacteria, yeasts, and molds, whereas physicochemical properties were characterized by pH, moisture, salt content and water activity. The results showed that microbial profiles were elevated for all the studied micro-organisms. Staphylococci and lactic acid bacteria were the most abundant micro-organisms in the product. Total coliforms were found in low numbers in fresh meat, being eliminated at the post salting stage of process. The physicochemical characteristics showed that the moisture content decreased in the product during the drying period. The pH also decreased during the drying period, then remained almost unchanged during the rest of the ripening period. Moreover, El Gueddid showed low water activity and high salt content. One of the most important changes in the profile of myofibrillar proteins was a reduction in the myosin heavy chain content.

Characteristics, Functional Properties, and Antioxidant Activities of Water-Soluble Proteins Extracted from Grasshoppers, Patanga succincta and Chondracris roseapbrunner

Water-soluble proteins extracted from two species of grasshoppers, Patanga succincta (WSPP) and Chondracris roseapbrunner (WSPC), were characterized as well as their functional properties and antioxidant activities were investigated. The extraction yield, on a wet weight basis, was 7.35% and 7.46% for WSPP and WSPC, respectively. The most abundant amino acid in both proteins was glutamic acid, followed by aspartic, alanine, and leucine, in that order. The electrophoretic study revealed that proteins with MW of 29, 42, 50, 69, and 146 kDa were the major protein components in WSPP and WSPC. FTIR analysis showed that those proteins remained their structural integrity. The surface hydrophobicity at pH 7 of WSPC was higher than WSPP, but the sulfhydryl group content did not show significant difference between the proteins from two species. Both grasshopper proteins were mostly soluble in strong acidic and alkaline aqueous solutions with a minimum value at pH 4. Those proteins exhibited poor emulsifying properties and foaming capacity, but they had greater foaming stability compared with bovine serum albumin (BSA) (p<0.05). WSPC showed greater DPPH• and ABTS•+ scavenging activities and ferric-reducing antioxidant power (FRAP) than did WSPP (p<0.05). Therefore, based on characteristics and functional properties, water-soluble proteins from both edible grasshoppers can be used as an ingredient in food applications.

SDS-PAGE Characterisation of Crude Seed and Leaf Proteins in Corchorus Species

Crude protein separation was carried out for Corchorus incisifolious, Corchorus aestuans, Corchorus tridens and Corchorus olitorious using Sodium Dodecyl Sulphate-Polyacrylamide Gel Electrophoresis (SDS-PAGE). Plants were collected both from wild and cultivated sites and samples included leaves and seeds for the electrophoretic study. Distinct polymorphism in electrophoretic banding patterns of seed and leaf proteins following SDS- PAGE was observed in the four Corchorus species studied. Forty- two polypeptide bands were observed in the seed and a total of eleven polypeptide bands were observed in the leaves of the Corchorus species studied. The electrophoretic study revealed protein bands with various intensities ranging from high, to low and faint. The results showed that there was variation in both the seed and leaf proteins of the Corchorus species studied. A dendrogram constructed based on the Single Linkage Cluster Analysis (SLCA) clustering method revealed three major clusters for seeds. Cluster I consisted of C. incisifolious and C. aestuans, cluster II consisted of C. tridens, while cluster III consisted of C. olitorious. The leaf protein extracts were grouped into two clusters, cluster one containing C. incisifolious and C. aestuans, while the other contained C. tridens and C. olitorious.