A European Union-funded international project led by the University of Aberdeen, Scotland will study microscopic algae that live in oceans and seas as potential biofuel sources within the next four years.

Dubbed as the AccliPhot Project with participation of 12 partners across Europe, this multidisciplinary endeavor will look into the mechanisms by which marine microalgae respond to changes in light and other conditions, and use that information to make new products, especifically biofuels. Turning to marine microalgae as biofuel source will not harm the water and land resources for agricultural use since the vast ocean around us can be readily used to grow them. Microalgae can be grown for large scale production in huge water tanks called photo-bioreactors supplied with carbon dioxide, light and some minerals. Cultivating them in a manner that does not compete for valuable agricultural resources could contribute significantly to sustainable way of meeting the future energy demand.

In the United Arab Emirates, researchers at the Masdar Institute of Science and Technology are screening mangrove root sediments for novel enzymes that can break down cellulosic waste.

UAE's mangrove trees are believed to be hosting microbes that produce cellulosic enzymes. These microbes survive by extracting the energy from plant waste that falls into the water. And because the mangrove environment in UAE is characteristically hot, saline, and intense, the resilient microbes that live there may be producing enzymes that can withstand the extreme conditions that are normally required for biorefining process in biofuels and biochemicals production.

Discovery of novel cellulosic enzymes from mangrove root sediments will be aided by genomics and bioinformatics tools. The research team is also searching the UAE's deserts, coasts, marshes and salt flats for potential biofuel plants that thrive in extreme environments.

Scientists working at the US Department of Energy's Brookhaven National Laboratory have constructed a fusion protein that increases the production of alkanes – long carbon-chain molecules similar to gasoline hydrocarbons that can be biologically synthesized and extracted as a renewable alternative to petrochemicals.

In an earlier experiment, the research team discovered that the alkane-producing enzyme known as aldehyde-deformylating oxygenase or ADO, which naturally makes alkanes in certain bacteria, could not prolong its activity during the process due to buildup of hydrogen peroxide, a toxic by-product that completely inhibits the enzyme. To mitigate this inhibition problem, the scientists molecularly fused the ADO enzyme with another enzyme, catalase, which degrades hydrogen peroxide to oxygen and water. Laboratory assays showed that the engineered bi-functional enzyme was able to run the reaction for over 225 cycles versus three cycles for the native ADO. Expression of the fusion protein in bacteria resulted in at least five-fold increase in alkane production compared with the use of ADO enzyme alone.

The results of this study are described in the Proceedings of National Academy of Sciences. Now the BNL scientists are preparing to take on another challenge - making the combo enzyme work with algae and green plants.

A new cost-efficient chemical process for fuel conversion from biomass to liquid hydrocarbons has been designed by a team of researchers led by the Los Alamos National Laboratory in New Mexico, USA as reported in the journal Catalysis Science & Technology.

The researchers employed a method that exposed the chemical ring of furans, molecules that are generated from the breakdown of cellulose in biomass, so that they could be easily altered chemically. Opening these rings into linear chains is a critical step in fuel conversion because these linear molecules subsequently can be converted into alkanes, the hydrocarbons used in gasoline and diesel fuels. The said method was performed under relatively mild temperature of 80 degrees Celsius using hydrochloric acid as a catalyst. Current conversion technologies are prohibitively expensive because these require extreme conditions of high temperature and high pressure.

The researchers tested the process on several biomass-derived molecules and analyzed the selectivity and mechanism of reaction. This information is believed to be a key to designing better catalysts and processes for biomass conversion.

The February 7 issue of the journal Biotechnology for Biofuels reports the study conducted by researchers from the US Department of Agriculture that seeks to address the low ethanol yield from fermentation systems contaminated by lactic acid bacteria or LAB.

The study embarks on the exploitation of antimicrobial proteins called lysins produced by bacteriophages or viruses that typically infect bacteria. Lysins exert their lethal effects on target bacteria by degrading the bacterial cell wall component called peptidoglycan. Initially the researchers isolated and screened a number of lysins for their ability to kill Lactobacillus strains from fuel ethanol fermentation. Using knowledge from bacteriophage genome databases, four lysin molecules identified from the preliminary screening were produced in vitro, purified and rigorously assayed against a variety of LAB including the notorious L. fermentum under laboratory conditions that simulated industrial fermentation environments.

Overall, results suggest that potent bacteriophage lysins can be used to control unwanted lactobacilli contamination in ethanol fermentation systems without the pitfall of bacterial resistance associated with conventional antibiotics.