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Title: Enhanced processive cellulases

Abstract

Nucleic acid sequences encoding chimeric polypeptides that exhibit enhanced cellulase activities are disclosed herein. These nucleic acids may be expressed in hosts such as fungi, which in turn may be cultured to produce chimeric polypeptides. Also disclosed are chimeric polypeptides and their use in the degradation of cellulosic materials.

Inventors:
; ; ; ; ; ; ; ; ; ;
Publication Date:
Research Org.:
National Renewable Energy Lab. (NREL), Golden, CO (United States)
Sponsoring Org.:
USDOE
OSTI Identifier:
1364629
Patent Number(s):
9,683,248
Application Number:
14/365,200
Assignee:
Alliance for Sustainable Energy, LLC NREL
DOE Contract Number:
AC36-08G028308
Resource Type:
Patent
Resource Relation:
Patent File Date: 2012 Dec 17
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES

Citation Formats

Adney, William S., Beckham, Gregg T., Jarvis, Eric, Himmel, Michael E., Decker, Stephen R., Linger, Jeffrey G., Podkaminer, Kara, Baker, John O., Taylor, II, Larry, Xu, Qi, and Singh, Arjun. Enhanced processive cellulases. United States: N. p., 2017. Web.
Adney, William S., Beckham, Gregg T., Jarvis, Eric, Himmel, Michael E., Decker, Stephen R., Linger, Jeffrey G., Podkaminer, Kara, Baker, John O., Taylor, II, Larry, Xu, Qi, & Singh, Arjun. Enhanced processive cellulases. United States.
Adney, William S., Beckham, Gregg T., Jarvis, Eric, Himmel, Michael E., Decker, Stephen R., Linger, Jeffrey G., Podkaminer, Kara, Baker, John O., Taylor, II, Larry, Xu, Qi, and Singh, Arjun. Tue . "Enhanced processive cellulases". United States. doi:. https://www.osti.gov/servlets/purl/1364629.
@article{osti_1364629,
title = {Enhanced processive cellulases},
author = {Adney, William S. and Beckham, Gregg T. and Jarvis, Eric and Himmel, Michael E. and Decker, Stephen R. and Linger, Jeffrey G. and Podkaminer, Kara and Baker, John O. and Taylor, II, Larry and Xu, Qi and Singh, Arjun},
abstractNote = {Nucleic acid sequences encoding chimeric polypeptides that exhibit enhanced cellulase activities are disclosed herein. These nucleic acids may be expressed in hosts such as fungi, which in turn may be cultured to produce chimeric polypeptides. Also disclosed are chimeric polypeptides and their use in the degradation of cellulosic materials.},
doi = {},
journal = {},
number = ,
volume = ,
place = {United States},
year = {Tue Jun 20 00:00:00 EDT 2017},
month = {Tue Jun 20 00:00:00 EDT 2017}
}

Patent:

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  • The mechanism of action of cellulose-degrading enzymes is illuminated through a multidisciplinary collaboration that uses molecular dynamics (MD) simulations and expands the capabilities of MD codes to allow simulations of enzymes and substrates on petascale computational facilities. There is a class of glycoside hydrolase enzymes called cellulases that are thought to decrystallize and processively depolymerize cellulose using biochemical processes that are largely not understood. Understanding the mechanisms involved and improving the efficiency of this hydrolysis process through computational models and protein engineering presents a compelling grand challenge. A detailed understanding of cellulose structure, dynamics and enzyme function at the molecularmore » level is required to direct protein engineers to the right modifications or to understand if natural thermodynamic or kinetic limits are in play. Much can be learned about processivity by conducting carefully designed molecular dynamics (MD) simulations of the binding and catalytic domains of cellulases with various substrate configurations, solvation models and thermodynamic protocols. Most of these numerical experiments, however, will require significant modification of existing code and algorithms in order to efficiently use current (terascale) and future (petascale) hardware to the degree of parallelism necessary to simulate a system of the size proposed here. This work will develop MD codes that can efficiently use terascale and petascale systems, not just for simple classical MD simulations, but also for more advanced methods, including umbrella sampling with complex restraints and reaction coordinates, transition path sampling, steered molecular dynamics, and quantum mechanical/molecular mechanical simulations of systems the size of cellulose degrading enzymes acting on cellulose.« less
  • No abstract prepared.
  • Producing fuels, chemicals, and materials from renewable resources to meet societal demands remains an important step in the transition to a sustainable, clean energy economy. The use of cellulolytic enzymes for the production of nanocellulose enables the coproduction of sugars for biofuels production in a format that is largely compatible with the process design employed by modern lignocellulosic (second generation) biorefineries. However, yields of enzymatically produced nanocellulose are typically much lower than those achieved by mineral acid production methods. In this study, we compare the capacity for coproduction of nanocellulose and fermentable sugars using two vastly different cellulase systems: themore » classical 'free enzyme' system of the saprophytic fungus, Trichoderma reesei (T. reesei) and the complexed, multifunctional enzymes produced by the hot springs resident, Caldicellulosiruptor bescii (C. bescii). Here, we demonstrate by comparative digestions that the C. bescii system outperforms the fungal enzyme system in terms of total cellulose conversion, sugar production, and nanocellulose production. In addition, we show by multimodal imaging and dynamic light scattering that the nanocellulose produced by the C. bescii cellulase system is substantially more uniform than that produced by the T. reesei system. These disparities in the yields and characteristics of the nanocellulose produced by these disparate systems can be attributed to the dramatic differences in the mechanisms of action of the dominant enzymes in each system.« less
  • The present invention provides three fungal cellulases, their coding sequences, recombinant DNA molecules comprising the cellulase coding sequences, recombinant host cells and methods for producing same. The present cellulases are from Orpinomyces PC-2.
  • The present invention provides three fungal cellulases, their coding sequences, recombinant DNA molecules comprising the cellulase coding sequences, recombinant host cells and methods for producing same. The present cellulases are from Orpinomyces PC-2.