Abstract: A method is disclosed for analyzing a biological sample by antibody profiling for identifying forensic samples or for detecting the presence of an analyte. In an embodiment of the invention, the analyte is a drug, such as marijuana, cocaine, methamphetamine, methyltestosterone, or mesterolone. The method comprises attaching antigens to the surface of a solid support in a preselected pattern to form an array wherein the locations of the antigens are known; contacting the array with the biological sample such that a portion of antibodies in the sample reacts with and binds to antigens in the array to form immune complexes; washing away antibodies that do form immune complexes; and detecting the immune complexes, to form an antibody profile. Forensic samples are identified by comparing a sample from an unknown source with a sample from a known source.

Abstract: An enzyme isolated from an extremophilic microbe, and a method for utilizing same is described, and wherein the enzyme displays optimum enzymatic activity at a temperature of greater than about 80 degrees C., and a pH of less than about 2, and further may be useful in methodology including the pretreatment of a biomass so as to facilitate the production of an end product.

Abstract: A method of detecting a metal in a sample comprising a plurality of metal is disclosed. The method comprises providing the sample comprising a metal to be detected. The sample is added to a reagent solution comprising an enzyme and a substrate, where the enzyme is inhibited by the metal to be detected. An array of chelating agents is used to eliminate the inhibitory effects of additional metals in the sample. An enzymatic activity in the sample is determined and compared to an enzymatic activity in a control solution to detect the metal to be detected. A method of determining a concentration of the metal in the sample is also disclosed. A method of detecting a valence state of a metal is also disclosed.

Abstract: The invention relates to thermal and pH stable catalases. One catalase of the invention was purified and characterized from Thermus brockianus. As a part of the characterization, the enzyme was compared to typical catalases from commercial sources and found to be significantly more thermal/alkaline stable than these other enzymes. The catalase purified from T. brockianus consists of four identical subunits having a molecular mass of approximately 42.5 kDa, for a total molecular mass of approximately 178 kDa.