Advanced Regional Biomass Processing Depots: a key to the logistical challenges of the cellulosic biofuel industry

2011 ◽  
Vol 5 (6) ◽  
pp. 621-630 ◽  
Author(s):  
Pragnya L. Eranki ◽  
Bryan D. Bals ◽  
Bruce E. Dale
Keyword(s):  
Cellulosic Biofuel ◽  
Biofuel Industry ◽  
Biomass Processing

scholarly journals Microalgae based biorefinery: Issues to consider

2011 ◽  
Vol 4 (4) ◽  
pp. 05-21 ◽  
Author(s):  
Ángel Darío González Delgado ◽  
Viatcheslav Kafarov
Keyword(s):  
State Of The Art ◽  
Review Article ◽  
The State ◽  
Raw Material ◽  
Biodiesel Production ◽  
Multiple Products ◽  
Biofuel Industry ◽  
Biomass Processing ◽  
Biomass Transformation ◽  
Transformation Processes

Biorefining is sustainable biomass processing to obtain energy, biofuels and high value products through processes and equipment for biomass transformation. The biorefinery concept has been identified as the most promising way to create a biomass-based industry. Microalgae are classified as promising candidates in biorefinery processes because they are particularly important for obtaining multiple products.  This review article describes the biorefinery concept taking into account its different interpretations and comparing it with the traditional biomass transformation processes.  It describes the general characteristics of microalgae, and their potential to be used as a raw material in the biorefinery process.  The review focuses on the state of the art of products obtained from microalgae for the biofuel industry, mainly for biodiesel production, and the different methods to extract oil for biodiesel production as well as other products.  Based on this information, several aspects are suggested to be taken into account for the development of a topology for a microalgae-based biorefinery.

Microwave-Assisted Decarbonylation of Biomass-Derived Aldehydes Using Pd-Doped Hydrotalcites

2019 ◽  
Author(s):  
Nan An ◽  
Diana Ainembabazi ◽  
Kavya Samudrala ◽  
Christopher Reid ◽  
Kare Wilson ◽  
...  
Keyword(s):  
Heterogeneous Catalysts ◽  
Reaction Times ◽  
Inverse Correlation ◽  
Mulliken Charge ◽  
Metal Leaching ◽  
Carbonyl Carbon ◽  
Mild Conditions ◽  
Microwave Assisted ◽  
Biomass Processing ◽  
Alcohol Dehydrogenation

<p>Here we report the synthesis, characterization and activity of tunable Pd-doped hydrotalcites (Pd-HTs) for the decarbonylation of furfural, hydroxymethylfurfural (HMF), aromatic and aliphatic aldehydes under microwave conditions. The decarbonylation activity reported is a notable improvement over prior heterogeneous catalysts for this process. Furfural decarbonylation is optimized in a benign solvent compatible with biomass processing - ethanol, under relatively mild conditions and short reaction times. HMF selectively affords excellent yields of furfuryl alcohol with no humin formation, but longer reaction can also afford furan via tandem alcohol dehydrogenation and decarbonylation. Yields of substituted benzaldehydes are related to calculated Mulliken charge of the carbonyl carbon. The activity and selectivity differences can be traced to loading-dependent differences in Pd speciation on the catalysts. Poisoning studies show inverse correlation between Pd loading and metal leaching: Pd-HTs with lowest Pd loading, which consist of highly dispersed and oxidized Pd species, operate heterogeneously with negligible metal leaching. Recycling experiments are consistent with this trend, offering potential for further optimization to improve robustness.</p>

scholarly journals Two-step functional screen on multiple proteinaceous substrates reveals temperature-robust proteases with a broad-substrate range

2021 ◽  
Author(s):  
Antonio García-Moyano ◽  
Yuleima Diaz ◽  
José Navarro ◽  
David Almendral ◽  
Pål Puntervoll ◽  
...  
Keyword(s):  
Recombinant Expression ◽  
Skim Milk ◽  
In Silico Analysis ◽  
Prolonged Incubation ◽  
Genomic Libraries ◽  
Functional Screen ◽  
Biomass Processing ◽  
Screening Parameter ◽  
Marine Metagenome ◽  
Functional Screens

Abstract To support the bio-based industry in development of environment-friendly processes and products, an optimal toolbox of biocatalysts is key. Although functional screen of (meta)genomic libraries may potentially contribute to identifying new enzymes, the discovery of new enzymes meeting industry compliance demands is still challenging. This is particularly noticeable in the case of proteases, for which the reports of metagenome-derived proteases with industrial applicability are surprisingly limited. Indeed, proteolytic clones have been typically assessed by its sole activity on casein or skim milk and limited to mild screening conditions. Here, we demonstrate the use of six industry-relevant animal and plant by-products, namely bone, feather, blood meals, gelatin, gluten, and zein, as complementary substrates in functional screens and show the utility of temperature as a screening parameter to potentially discover new broad-substrate range and robust proteases for the biorefinery industry. By targeting 340,000 clones from two libraries of pooled isolates of mesophilic and thermophilic marine bacteria and two libraries of microbial communities inhabiting marine environments, we identified proteases in four of eleven selected clones that showed activity against all substrates herein tested after prolonged incubation at 55 °C. Following sequencing, in silico analysis and recombinant expression in Escherichia coli, one functional protease, 58% identical at sequence level to previously reported homologs, was found to readily hydrolyze highly insoluble zein at temperatures up to 50 °C and pH 9–11. It is derived from a bacterial group whose ability to degrade zein was unknown. This study reports a two-step screen resulting in identification of a new marine metagenome-derived protease with zein-hydrolytic properties at common biomass processing temperatures that could be useful for the modern biorefinery industry. Key points • A two-step multi-substrate strategy for discovery of robust proteases. • Feasible approach for shortening enzyme optimization to industrial demands. • A new temperature-tolerant protease efficiently hydrolyzes insoluble zein.

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