SBIR Phase II: Designer Cellulases for Biomass Conversion

Information

  • NSF Award
  • 0522310
Owner
  • Award Id
    0522310
  • Award Effective Date
    10/1/2005 - 19 years ago
  • Award Expiration Date
    9/30/2007 - 17 years ago
  • Award Amount
    $ 225,000.00
  • Award Instrument
    Standard Grant

SBIR Phase II: Designer Cellulases for Biomass Conversion

This Small Business Innovation Research (SBIR) Phase II project will develop new technology to improve the high-temperature performance of endoglucanase, which can be used to manufacture pulp from wood chips and other biomass. Producing pulp for papermaking via thermomechanical pulping (TMP) of biomass is a highly energy intensive process that is performed at high temperatures. Research is proposed to demonstrate the feasibility of using a directed evolution strategy and high-throughput, solid-phase enzyme library screening to engineer a new endoglucanase variant with significantly improved thermoactivity, thermostability and resistance to inhibitors. This enhanced enzyme will be sold as an additive to manufacturers who produce pulp and paper via the TMP process. Major benefits include energy savings and improvement of paper quality. <br/><br/>The commercial application of this project will be on the pulp and paper industry. New screening technology will be used to engineer an enhanced enzyme that will modify pulp fibers under high-temperature conditions. This enzyme additive will accelerate the pulp refining process and thereby lower production costs by reducing the amount of electricity needed to complete the conversion. Any significant reduction in the energy input will be very economically attractive to the pulp producers. If introducing an effective enzyme treatment could eliminate even a modest 10% of the current energy expenditure, the potential worldwide savings could total nearly US$500 million per year. The enhanced enzyme will be able to create a new market by offering these significant savings to the pulp producers. In addition, the information gained from this study could be applied to other similar enzymes to expand the market for thermostable biocatalysts and broaden the understanding of protein structure-function.

  • Program Officer
    Gregory T. Baxter
  • Min Amd Letter Date
    9/7/2005 - 19 years ago
  • Max Amd Letter Date
    1/4/2007 - 18 years ago
  • ARRA Amount

Institutions

  • Name
    KAIROS SCIENTIFIC INC.
  • City
    SAN DIEGO
  • State
    CA
  • Country
    United States
  • Address
    10225 BARNES CANYON RD., A110
  • Postal Code
    921212735
  • Phone Number
    8586268170

Investigators

  • First Name
    William
  • Last Name
    Coleman
  • Email Address
    wcoleman@kairos-scientific.com
  • Start Date
    9/7/2005 12:00:00 AM

FOA Information

  • Name
    Industrial Technology
  • Code
    308000