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Anaerobic digestion has been widely employed in waste treatment for its ability to capture methane gas released as a product during the digestion. Certain wastes, however, cannot be easily digested due to their low nutrient level insufficient for anaerobic digestion, thus co-digestion is a viable option. Numerous studies have shown that using co-substrates in anaerobic digestion systems improve methane yields as positive synergisms are established in the digestion medium, and the supply of missing nutrients are introduced by the co-substrates. Nevertheless, large-scale implementation of co-digestion technology is limited by inherent process limitations and operational concerns. This review summarizes the results from numerous laboratory, pilot, and full-scale anaerobic co-digestion (ACD) studies of wastewater sludge with the co-substrates of organic fraction of municipal solid waste, food waste, crude glycerol, agricultural waste, and fat, oil and grease. The critical factors that influence the ACD operation are also discussed. The ultimate aim of this review is to identify the best potential co-substrate for wastewater sludge anaerobic co-digestion and provide a recommendation for future reference. By adding co-substrates, a gain ranging from 13 to 176% in the methane yield was accomplished compared to the mono-digestions.

A novel xylanase gene, xyn10A, was cloned from Flavobacterium johsoniae, overexpressed in a flavobacterial expression system, the recombinant enzyme purified by Ni-affinity chromatography, and enzyme structure and activity analyzed. Xyn10A was found to be a modular xylanase with an Fn3 accessory domain on its N-terminal and a catalytic region on the C-terminal. The optimum pH and temperature for Xyn10A was 8.0 and 30° C, but Xyn10A retained 50% activity at 4°C, indicating that Xyn10A is a cold-active xylanase. A Fn3-deletion xylanase had relative activity ca. 3.6-fold lower than the wild-type, indicating that Fn3 promotes xylanase activity. The Fn3 region also contributed to stability of the enzyme at elevated temperatures. However, Fn3 did not bind this xylanase to insoluble substrates. The enzyme hydrolyzed xylo-oligosaccharides into xylobiose, and xylose with xylobiose as the main product, confirming that Xyn10A is a strict endo-β-1,4-xylanase. Xyn10A also hydrolyzed birchwood and beechwood xylan to yield mainly xylose, xylobiose and xylotriose.