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Multi-lab Separations Consortium Aims to Decarbonize Biofuels

May 19, 2023

The Bioprocessing Separations Consortium, originally established in 2016 by the U.S. Department of Energy’s (DOE) Bioenergy Technologies Office (BETO) and led by Argonne National Laboratory, recently received a three year funding renewal to continue advancing separations technologies critical to converting biomass to low-carbon biofuel. The Biosciences Area’s Advanced Biofuels and Bioproducts Process Development Unit (ABPDU) represents Berkeley Lab as a partner in the consortium.

Transforming Waste into Bio-based Chemicals

September 30, 2020

Researchers at Berkeley Lab have transformed lignin, a waste product of the paper industry, into a precursor for a useful chemical with a wide range of potential applications. The work was a collaboration between the Advanced Biofuels and Bioproducts Process Development Unit, the Joint BioEnergy Institute, and the Queens University of Charlotte. In a recent study, they demonstrated their ability to convert lignin into a chemical compound that is a building block of bio-based ionic liquids.

AIChE Honors Biological Systems and Engineering Researchers

August 8, 2017

The American Institute of Chemical Engineers (AIChE) has recognized two Biological Systems and Engineering (BSE) early-career researchers–Akash Narani and Ning Sun–with honors to be bestowed at the 2017 AIChE Annual Meeting in Minneapolis, Minn., this fall.

JBEI/BSE Paper Among PLOS ONE Top 10% Most Cited Articles

July 21, 2017

A paper by Joint BioEnergy Institute (JBEI) and Biological Systems and Engineering (BSE) researchers has been ranked among the top 10% most cited PLOS ONE articles. “A Thermophilic Ionic liquid-tolerant Cellulase Cocktail for the Production of Cellulosic Biofuels” published in 2012 has already been viewed 8,871 times and cited 50 times as of today. The paper reports the development of an Ionic Liquid-tolerant cellulase cocktail by combining thermophilic bacterial glycoside hydrolases produced by a mixed consortia with recombinant glycoside hydrolases.

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