This document provides butyrylcholinesterases having an enhanced ability to hydrolyze acyl ghrelin as well as nucleic acids encoding such butyrylcholinesterases. This document also provides methods and materials for treating obesity and/or aggression. For example, methods for administering a nucleic acid encoding a wild-type or mutant butyrylcholinesterase having the ability to hydrolyze acyl ghrelin to a mammal under conditions wherein the level of acyl ghrelin within the mammal is reduced, under conditions wherein the rate of body weight gain of the mammal is reduced, under conditions wherein the mammal's level of aggression is reduced, and/or under conditions wherein the mammal's rate of developing stress-induced tissue damage are provided.

The presently-disclosed subject matter describes fusion proteins comprising butyrylcholinesterase (BChE) having an improved production yield and biological half-life and nucleotides encoding the same.

This document provides butyrylcholinesterases having an enhanced ability to hydrolyze acyl ghrelin as well as nucleic acids encoding such butyrylcholinesterases. This document also provides methods and materials for treating obesity and/or aggression. For example, methods for administering a nucleic acid encoding a wild-type or mutant butyrylcholinesterase having the ability to hydrolyze acyl ghrelin to a mammal under conditions wherein the level of acyl ghrelin within the mammal is reduced, under conditions wherein the rate of body weight gain of the mammal is reduced, under conditions wherein the mammal’s level of aggression is reduced, and/or under conditions wherein the mammal’s rate of developing stress-induced tissue damage are provided.

Described herein are engineered cells, enzymes, methods of use, and bee bread incorporating engineered cells and enzymes as described herein. In certain aspects, described herein are a bacterium containing therein one or more stably-expressing expression vectors for exogenous expression of one or more recombinant carboxylesterase enzymes or oxalate decarboxylase enzymes, thereby providing the engineered cell an exogenous pathway for hydrolyzing ester bonds or removing a carboxyl group. Engineered cells and recombinant enzymes as described herein can be incorporated into bee bread to be fed to a member of the Apidae family of bees or of the Apis or Bombus genus. In additional aspects, such bacteria can also be selected and amplified from the milieu of the hive microorganisms and in some cases they can be molecularly bred to enhance their metabolic capabilities without genetic engineering.

An apparatus and method for detecting an analyte of interest using paper spray mass spectrometry includes a spray material; a sample on the spray material including an enzyme of interest; a solvent to hydrate the sample, promote enzymatic activity, and extract analytes of interest from the sample; a substrate specific to the enzyme of interest, wherein any of the spray material and the solvent includes the substrate; a voltage source to apply a voltage to the spray material to create charged droplets of a mixture containing the sample; and a mass spectrometer to perform spectrometry on the droplets to perform any of: identify the analytes of interest in the sample; and measure a level of inhibition in any enzymes contained in the sample.

In general, among other things, compounds of Formula I are provided:

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or a pharmaceutically acceptable salt thereof. Other compounds are also provided. Methods of diagnosis and treatment are also provided.

Disclosed herein are proteins having at least 90% sequence identity to a wild-type human butyrylcholinesterase and compositions comprising same. The disclosed proteins may have at least one mutation at a position within the acyl binding pocket and at least one mutation adjacent to the acyl biding pocket. Further disclosed are proteins having at least 90% sequence identity to a wild-type human butyrylcholinesterase, wherein the protein may comprise a mutation at a position selected from one or more of 282, 283, and 284.

The presently-disclosed subject matter describes fusion proteins comprising butyrylcholinesterase (BChE) having an improved production yield and biological half-life and nucleotides encoding the same.

Methods of glycoprotein production employing monosaccharides capable of producing a global increase in flux through the sialic acid pathway are provided.

Disclosed herein are methods for the large-scale production of a highly thermally stable acetylcholinesterase (AChE) and butyrylcholinesterase (BChE). Additionally, the expression methods disclosed herein can produce ChE preparations consisting of extract or purified forms that can be produced in high amounts and are highly thermally stable. These ChE products can be used in vitro detection, detoxification and decontamination methods.