University System of Maryland

University of California

Frank Thomson Robb

Pongpan Laksanalamai

Douglas S Clark

Harvey W Blanch

Melinda E Clark

Timothy Whitehead

Joel Edward Graham

Anchalee Jiemjit

The present invention relates to maintaining the activity and stability of enzymes and biologically active proteins at increased temperatures by contacting same with a combination of isolated passive and active chaperones from a hyperthermopilic Archaeon, wherein the chaperones may include heat shock proteins, prefoldin and/or chaperonin proteins.

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Hydrolysis and degradation of cellulose-containing biomass by use of a polypeptide having cellulase activity is provided. Also provided are polypeptides having cellulase activity, such as archaeal cellulases, polynucleotides encoding the polypeptides, and compositions containing the polypeptides, and methods of use thereof.

Polypeptides for use in the deconstruction of cellulose

The invention provides methods and compositions for increasing tolerance of microorganisms to toxic agents, such as solvents; and for increasing production of solvents from solvent-generating microorganisms. The methods comprise engineering a microorganism of interest to express a heterologous heat-shock protein/chaperone, e.g., Group II chaperonin or a prefoldin such as &#x3b3;-prefoldin, where the heterologous protein is from an extremophile, such as an archaean.

Heterologous expression of extremophile heat shock proteins and chaperones in microorganisms to increase tolerance to toxic compounds

Small heat shock proteins, e.g.,(Pfu-sHSP and/or Pfu-tsHSP), confer thermotolerance on cellular cultures and on proteins in cellular extracts during prolonged incubation at elevated temperature, demonstrating the ability to protect cellular proteins and maintain cellular viability under heat stress conditions. Such heat shock proteins are effective to combat enzymatic aggregation and intracellular precipitation during heat stress, and thereby enable enhancement of the utility and stability of enzymes in various applications, e.g., Taq polymerase in PCR applications, digestive enzymes in microbial degradative applications, etc.

Enhanced protein thermostability and temperature resistance

Small heat shock proteins, e.g., (Pfu-sHSP), confer thermotolerance on cellular cultures and on proteins in cellular extracts during prolonged incubation at elevated temperature, demonstrating the ability to protect cellular proteins and maintain cellular viability under heat stress conditions. Such heat shock proteins are effective to combat enzymatic aggregation and intracellular precipitation during heat stress, and thereby enable enhancement of the utility and stability of enzymes in various applications, e.g., Taq polymerase in PCR applications, digestive enzymes in microbial degradative applications, etc.

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Gaithersburg, MD, United States of America

Frank Thomson Robb