Martin Marietta Energy Systems, Inc.

The United States of America As Represented by the United States

Lockheed Martin Energy Research Corporation

Lockheed Martin Energy Systems, Inc.

Lockheed Martin Energy Research Systems, Inc.

Jonathan Woodward

Charles D Scott

Brian H Davison

Brendlyn D Faison

Timothy C Scott

Susan M Mattingly

The present invention is an enzymatic method for producing hydrogen comprising the steps of: a) forming a reaction mixture within a reaction vessel comprising a substrate capable of undergoing oxidation within a catabolic reaction, such as glucose, galactose, xylose, mannose, sucrose, lactose, cellulose, xylan and starch. The reaction mixture further comprises an amount of glucose dehydrogenase in an amount sufficient to catalyze the oxidation of the substrate, an amount of hydrogenase sufficient to catalyze an electron-requiring reaction wherein a stoichiometric yield of hydrogen is produced, an amount of pH buffer in an amount sufficient to provide an environment that allows the hydrogenase and the glucose dehydrogenase to retain sufficient activity for the production of hydrogen to occur and also comprising an amount of nicotinamide adenine dinucleotide phosphate sufficient to transfer electrons from the catabolic reaction to the electron-requiring reaction; b) heating the reaction mixture at a temperature sufficient for glucose dehydrogenase and the hydrogenase to retain sufficient activity and sufficient for the production of hydrogen to occur, and heating for a period of time that continues until the hydrogen is no longer produced by the reaction mixture, wherein the catabolic reaction and the electron-requiring reactions have rates of reaction dependent upon the temperature; and c) detecting the hydrogen produced from the reaction mixture.

Method for the enzymatic production of hydrogen

A structurally stable gel bead containing an entrapped enzyme and a method for its manufacture. The enzyme is covalently cross-linked to gelatin in the presence of glutaraldehyde prior to the formation of the gel bead, to prevent leakage of the enzyme. Propylene glycol alginate is then added to the mixture. Once the gel beads are formed, they are then soaked in glutaraldehyde, which imparts structural stability to the gel beads. This method can be used with many types of enzymes, such as proteases, carbohydrases, proteases, ligases, isomerases, oxidoreductases, and specialty enzymes. These and other enzymes can be immobilized in the gel beads and utilized in a number of enzymatic processes. Exogenously added ions are not required to maintain the structural stability of these gel beads.

Structurally stable gel bead containing entrapped enzyme and method for

A method for enzymatically separating the non-inked cellulose fibers from the inked cellulose fibers in cellulosic materials. The cellulosic material, such as newsprint, is introduced into a first chamber containing a plastic canvas basket. This first chamber is in fluid communication, via plastic tubing, with a second chamber containing cellobiase beads in a plastic canvas basket. Cellulase is then introduced into the first chamber. A programmable pump then controls the flow rate between the two chambers. The action of cellulase and stirring in the first chamber results in the production of a slurry of newsprint pulp in the first chamber. This slurry contains non-inked fibers, inked fibers, and some cellobiose. The inked fibers and cellobiose flow from the first chamber to the second chamber, whereas the non-inked fibers remain in the first chamber because they are too large to pass through the pores of the plastic canvas basket. The resulting non-inked and inked fibers are then recovered.

Method for separating the non-inked cellulose fibers from the inked

A process for converting cellulosic materials, such as waste paper, into fuels and chemicals, such as sugars and ethanol, utilizing enzymatic hydrolysis of the major carbohydrate of paper: cellulose. A waste paper slurry is contacted by cellulase in an agitated hydrolyzer. An attritor and a cellobiase reactor are coupled to the agitated hydrolyzer to improve reaction efficiency. Additionally, microfiltration, ultrafiltration and reverse osmosis steps are included to further increase reaction efficiency. The resulting sugars are converted to a dilute product in a fluidized-bed bioreactor utilizing a biocatalyst, such as microorganisms. The dilute product is then concentrated and purified.

Enhanced attrition bioreactor for enzyme hydrolysis of cellulosic

Enhanced attrition bioreactor for enzyme hydrolysis or cellulosic

A process for converting cellulosic materials, such as waste paper, into fuels and chemicals utilizing enzymatic hydrolysis of the major constituent of paper, cellulose. A waste paper slurry is contacted by cellulase in an agitated hydrolyzer. The cellulase is produced from a continuous, columnar, fluidized-bed bioreactor utilizing immobilized microorganisms. An attritor and a cellobiase reactor are coupled to the agitated hydrolyzer to improve reaction efficiency. The cellulase is recycled by an adsorption process. The resulting crude sugars are converted to dilute product in a fluidized-bed bioreactor utilizing microorganisms. The dilute product is concentrated and purified by utilizing distillation and/or a biparticle fluidized-bed bioreactor system.

Process for converting cellulosic materials into fuels and chemicals

A process for recovering cellulase from the hydrolysis of cellulose, and reusing it in subsequent hydrolyois procedures. The process utilizes a commercial adsorbent that efficiently removes cellulase from reaction products which can be easily removed by simple decantation.

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Oak Ridge, TN, United States of America

Jonathan Woodward