As concerns about global warming and the pollution of many natural resources increase, the identification of novel plant-based nutrient sources and natural bioremediation methods are of increasing significance. Many protein sources have been studied for these purposes, and mushrooms are emerging as a new source of plant-based protein and for various biotechnological applications. The stability of proteins from mushrooms is of particular interest for both applications, as excessive stability could lead to food intolerance, but is necessary for practical applications, such as bioremediation of pharmaceutical, industrial dye, and heavy metal pollutants. Kinetically stable proteins (KSPs) are proteins that have a high-energy unfolding barrier and thus unfold at a much slower rate than most proteins, and resistance to denaturation by sodium dodecyl sulfate (SDS) is used as a proxy for determining if a protein possesses this stability. Here we apply diagonal two-dimensional (D2D) SDS- polyacrylamide gel electrophoresis (PAGE), to isolate and allow the proteomics-level identification of KSPs by matrix-assisted laser desorption/ ionization (MALDI). The identification of these proteins in various edible species of mushrooms will provide the initial steps to determining if the isolated KSPs have applications in allergenicity studies and bioremediation. It has also been noted that many of these proteins are post-translational glycosylated. Thus, this study will also provide the basis for structural studies to understand the effects that post-translational modifications have on SDS resistance and protein stability.

Identification and analysis of kinetically stable proteins (KSPs) in various mushroom species for applications in mycoremediation and allergenicity studies

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