Evaluation and single-laboratory verification of a proposed modification to the U.S. Food and Drug Administration method for detection and identification of Campylobacter jejuni or Campylobacter coli from raw silo milk.

The current U.S. Food and Drug Administration (FDA) methodology for detection of Campylobacter, a leading source for foodborne illness, is outdated.

Review of current methodologies to isolate and identify Campylobacter spp. from foods.

This article summarizes the most effective protocols to isolate Campylobacter spp. (mainly Campylobacter jejuni and Campylobacter coli) from food, primarily poultry products, and includes a summary of the current methods recommended by the Food and Drug Administration and the U.S.

Effects of transglutaminase catalysis on the functional and immunoglobulin binding properties of peanut flour dispersions containing casein.

The functionality of light roasted peanut flour (PF) dispersions containing supplemental casein (CN) was altered after polymerization with microbial transglutaminase (TGase). The formation of high molecular weight covalent cross-links was observed with likely development of PF-PF, PF-CN, and CN-CN polymers based on Western blotting patterns visualized using antiserum directed against Ara h 1, Ara h 2, Ara h 3, or casein. The gelling temperature of TGase-treated PF dispersions containing 2.

The effect of transglutaminase crosslinking on the rheological characteristics of heated peanut flour dispersions.

Peanut flour (PF) is a high-protein ingredient prepared after the partial extraction of oil from roasted peanut seed. Microbial transglutaminase (TGase) catalyzes protein crosslinking via acyl-transfer reactions, resulting in the modification of functional properties such as viscosity, gelation, solubility, and water holding capacity. This work was conducted to observe changes in rheological properties of PF dispersions in the presence and the absence of TGase and amidated pectin (AP).

Transglutaminase polymerization of peanut proteins.

Transglutaminase promotes protein cross-linking reactions through an acyl transferase mechanism involving protein-bound glutaminyl residues and primary amines including the epsilon-amino group of lysine residues in soy, myosin, gluten, oat globulin, casein, and whey. Herein, we present a first report of exogenous transglutaminase catalysis of several peanut protein fractions, including purified Ara h 1. In most cases, SDS-PAGE banding patterns revealed the formation of high molecular weight polymers while catalysis of Ara h 1 resulted in distinct dimer formation.