Coccidioidomycosis is most often diagnosed serologically and the quantitative complement-fixing antibody test (CF) is considered prognostically useful. Because CF is complex, labor-intensive, and poorly standardized, an enzyme-linked immunoassay (ELISA) alternative would be attractive. The present invention features an antibody-binding domain that is restricted to a 200 amino acid recombinant peptide of the known antigen responsible for CF activity. Overlapping truncations of this peptide do not bind CF antibodies, suggesting that the responsible epitope(s) are conformational. Further, anchoring the antigenic peptide to the ELISA plate by means of a C-terminal tag instead of allowing the peptide to randomly adhere to the plastic plate improves sensitivity of antibody detection by one to two logs in different sera. The newly developed ELISA shows a significant quantitative correlation with CF. This ELISA shows potential as the basis for a new quantitative assay for coccidioidal antibodies.

Methods are disclosed for detecting and measuring polysaccharide-hydrolyzing enzyme activity or concentration by partial hydrolysis using a pre-determined, yet short, incubation time and a pre-determined temperature. The resulting reaction mixture has unique chemical (i.e., reaction products) and physical (i.e., viscosity) properties that can be used to detect or measure the polysaccharide-hydrolyzing enzyme activity or concentration.

Detecting xanthan gum in a sampling location includes delivering a tagged polypeptide to the sampling location. The tagged polypeptide includes a polypeptide and a fluorescent probe bound to the polypeptide, such that the fluorescent probe is released from the polypeptide to yield an unbound fluorescent probe when the polypeptide interacts with xanthan gum. Light that excites the unbound fluorescent probe is directed toward the sampling location, and an intensity of fluorescence emitted from the unbound fluorescent probe is assessed, wherein a non-zero intensity is indicative of the presence of xanthan gum in the sampling location. A device for the detection of xanthan gum has a sensing region including the tagged polypeptide, a light source adapted to direct light to the sensing region, the light source adapted to provide one or more wavelengths of light to excite the fluorescent probe, and a detector for detecting fluorescence emitted from the fluorescent probe.

The present invention relates to determination of the microorganism content in material comprising cellulose within the pulp and paper industry. The material comprising cellulose is enzymatically pretreated and microorganisms are determined using PCR based technology.

A method is provided for determining, the presence and concentration of an analyte by contacting the sample with a solution comprising: magnetic beads, a capture probe capable of binding the analyte, a reporter probe and cellulose, whereby, if the analyte is present, an MB-analyte-reporter-cellulase sandwich is formed; and then contacting the solution comprising the sandwich with an electrode covered with an electrically insulating layer comprising or consisting of cellulose and/or a cellulose derivative, wherein the MB-analyte-reporter-cellulase sandwich leads to degradation of the insulating layer thereby causing a measurable change in electrical properties at the electrode surface, wherein the change in electrical properties is a function of the amount of analyte in the sample. Devices and biosensor applying the method are also provided.

Disclosed herein are methods for quantifying total endotoxin load in a biofilm sample. Also provided are methods for identifying a gram-negative biofilm derived bacterial infection. The disclosed methods more accurately define actual total endotoxin levels and can detect the presence of endotoxin in a given biofilm volume at a higher resolution than current extraction techniques.

There is disclosed a peptide with mucolytic activity, The peptide comprising an amino acid sequence having at least 60% sequence identity to the amino add sequence defined in SEQ ID NO: 1, but does not consist of the amino sequence defined in SEQ ID NO: 2.

Disclosed herein include methods of detecting and measuring enzymatic activity in coating compositions comprising one or more enzymes contained therein, for example following film formation of the coating compositions. Media-based assays and spectrophotometric-based biochemical assays for analysis of in-film enzymatic activity are provided. Methods of configuring coating compositions to enable spectrophotometric-based analysis are also provided.

Described herein are methods for the alteration and/or transfer of fungal functional traits, e.g., phenotypic activity, via the controlled transfer of endohyphal symbionts, e.g., bacteria, among fungal species. Also described are methods for the identification of endohyphal bacterial symbionts as determinants of cellulase and ligninase activity in fungi, and the use of endohyphal bacterial symbionts to alter the activity, including cellulase and ligninase activities, of the fungi. In particular, the fungi described herein are endophytic fungi, that is, fungi which colonize living, and subsequently senescent, plant tissue.

Coccidioidomycosis is most often diagnosed serologically and the quantitative complement-fixing antibody test (CF) is considered prognostically useful. Because CF is complex, labor-intensive, and poorly standardized, an enzyme-linked immunoassay (ELISA) alternative would be attractive. The present invention features an antibody-binding domain that is restricted to a 200 amino acid recombinant peptide of the known antigen responsible for CF activity. Overlapping truncations of this peptide do not bind CF antibodies, suggesting that the responsible epitope(s) are conformational. Further, anchoring the antigenic peptide to the ELISA plate by means of a C-terminal tag instead of allowing the peptide to randomly adhere to the plastic plate improves sensitivity of antibody detection by one to two logs in different sera. The newly developed ELISA shows a significant quantitative correlation with CF. This ELISA shows potential as the basis for a new quantitative assay for coccidioidal antibodies.