Integrated Micro-chromatography Systems, Inc.

Medical University of South Carolina

Dpx Technologies, Inc.

Lim Andrew Lee

John Tomashek

Caleb Reece Schlachter

Pongkwan Sitasuwan

Qian Wang

William Edward Brewer

Gary Horvath

Jia Yang

Margarita Marinova

Brian Todd Mullis

Robert S Earnhardt, Jr

Sunil Hwang

Chimeric and other variant β-glucuronidase enzymes with enhanced properties as compared to unmodified enzyme are provided. The enzymes of the invention advantageously exhibit enhanced enzymatic activity, enhanced substrate range, enhanced pH range, enhanced temperature range and/or enhanced enzyme stability. Methods of using the variant enzymes for hydrolysis of glucuronide substrates, including opiates and benzodiazepines, are also provided.

Chimeric and other variant β-glucuronidase enzymes with enhanced properties

Mutatedsulfatase (PaS) enzymes with enhanced enzymatic activity as compared to the parental wild type enzyme are provided. The variant sulfatases of the invention advantageously allow for accurate analysis of bodily samples for the presence of drugs. Methods of using the mutated enzymes for hydrolysis of sulfate ester linkages are also provided, including with substrates such as opioids or steroids containing a sulfate ester linkage.

Variant sulfatase enzymes with enhanced properties

Blends of enzymes of the same enzyme class (same EC number), such as beta-glucuronidase enzyme blends, are provided that exhibit synergistic levels of activity across a range of substrates as compared to the activity levels of each enzyme in the blend individually. The blends also may exhibit a greater effective substrate range, as well as greater effective pH and/or temperature ranges as compared to single enzyme preparations. Predictive methods for determining optimal enzyme blends, methods for preparing enzyme blends, enzyme blend compositions, enzyme blend formulations and methods of using such enzyme blends are provided.

Compositions of beta-glucuronidase enzyme blends with enhanced enzymatic activity and methods of preparation thereof

Chimeric and other variant &#x3b2;-glucuronidase enzymes with enhanced properties as compared to unmodified enzyme are provided. The enzymes of the invention advantageously exhibit enhanced enzymatic activity, enhanced substrate range, enhanced pH range, enhanced temperature range and/or enhanced enzyme stability. Methods of using the variant enzymes for hydrolysis of glucuronide substrates, including opiates and benzodiazepines, are also provided.

Chimeric and other variant beta-glucuronidase enzymes with enhanced properties

The present invention provides a disposable pipette tip for dispersive solid phase extraction (SPE) that allows for rapid, automatable purification of large biomolecules, such as nucleic acids, proteins and polypeptides without the need for additional tools such as centrifuges, magnetic plates or vacuum manifolds. The pipette tip is designed for optimal biomolecule isolation while maintaining sample integrity. Optimized methods of using the dispersive pipette extraction system for isolation of large biomolecules are also provided.

Dispersive pipette extraction system for purification of large biomolecules

Methods are generally disclosed for attaching a cell binding motif to a carboxy end of a coat protein of a Tobacco Mosaic Virus particle to form a modified-TMV particle; and attaching a cell to the cell binding motif of the modified-TMV particle. Methods are also disclosed for incorporated virus particles, e.g., TMV virus particles into hydrogels.

Incorporation of plant virus particles and polymers as 2D and 3D scaffolds to manipulate cellular behaviors

Mutated &#x3b2;-glucuronidase enzymes with enhanced enzymatic activity and thermostability as compared to wild type enzyme are provided. The enzymes of the invention advantageously allow for accurate analysis of bodily samples for the presence of drugs in 30 minutes or less, as compared to the several hours needed using prior enzyme preparations. Methods of using the mutated enzymes for hydrolysis of glucuronide substrates, including opiates and benzodiazepines, are also provided.

Mutant &#x3b2;-glucuronidase enzymes with enhanced enzymatic activity

Mutatedstrain 269Y &#x3b2;-glucuronidase enzymes with enhanced enzymatic activity at low pH (e.g., below pH 6.8), as well as enhanced thermostability as compared to wild type enzyme are provided. The enzymes of the invention advantageously allow for accurate analysis of bodily samples for the presence of drugs at low pH and in 30 minutes or less, as compared to the several hours needed using prior enzyme preparations. Methods of using the mutated enzymes for hydrolysis of glucuronide substrates, including opiates and benzodiazepines, are also provided.

Mutant lactobacillus beta-glucuronidase enzymes with enhanced enzymatic activity

Mutatedsp. RLH1 &#x3b2;-glucuronidase enzymes with enhanced enzymatic activity and thermostability as compared to wild type enzyme are provided. The enzymes of the invention advantageously allow for accurate analysis of bodily samples for the presence of drugs in 30 minutes or less, as compared to the several hours needed using prior enzyme preparations. Methods of using the mutated enzymes for hydrolysis of glucuronide substrates, including opiates and benzodiazepines, are also provided.

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Columbia, SC, United States of America

Lim Andrew Lee