Fungi hijack a ubiquitous plant apoplastic endoglucanase to release a ROS scavenging beta-glucan decasaccharide to subvert immune responses

Plant pathogenic and beneficial fungi have evolved several strategies to evade immunity and cope with host-derived hydrolytic enzymes and oxidative stress in the apoplast, the extracellular space of plant tissues. Fungal hyphae are surrounded by an inner insoluble cell wall layer and an outer soluble extracellular polysaccharide (EPS) matrix. Here, we show by proteomics and glycomics that these two layers have distinct protein and carbohydrate signatures, and hence likely have different biological functions. The barley (Hordeum vulgare) β-1,3-endoglucanase HvBGLUII, which belongs to the widely distributed apoplastic glycoside hydrolase 17 family (GH17), releases a conserved β-1,3;1,6-glucan decasaccharide (β-GD) from the EPS matrices of fungi with different lifestyles and taxonomic positions. This low molecular weight β-GD does not activate plant immunity, is resilient to further enzymatic hydrolysis by β-1,3-endoglucanases due to the presence of three β-1,6-linked glucose branches and can scavenge reactive oxygen species. Exogenous application of β-GD leads to enhanced fungal colonization in barley, confirming its role in the fungal counter-defensive strategy to subvert host immunity. Our data highlight the hitherto undescribed capacity of this often-overlooked EPS matrix from plant-associated fungi to act as an outer protective barrier important for fungal accommodation within the hostile environment at the apoplastic plant–microbe interface

Integrated Cycles for Urban Biomass as a Strategy to Promote a CO2-Neutral Society—A Feasibility Study

The integration of closed biomass cycles into residential buildings enables efficient resource utilization and avoids the transport of biowaste. In our scenario called Integrated Cycles for Urban Biomass (ICU), biowaste is degraded on-site into biogas that is converted into heat and electricity. Nitrification processes upgrade the liquid fermentation residues to refined fertilizer, which can be used subsequently in house-internal gardens to produce fresh food for residents. Our research aims to assess the ICU scenario regarding produced amounts of biogas and food, saved CO2 emissions and costs, and social–cultural aspects. Therefore, a model-based feasibility study was performed assuming a building with 100 residents. The calculations show that the ICU concept produces 21% of the annual power (electrical and heat) consumption from the accumulated biowaste and up to 7.6 t of the fresh mass of lettuce per year in a 70 m2 professional hydroponic production area. Furthermore, it saves 6468 kg CO2-equivalent (CO2-eq) per year. While the ICU concept is technically feasible, it becomes economically feasible for large-scale implementations and higher food prices. Overall, this study demonstrates that the ICU implementation can be a worthwhile contribution towards a sustainable CO2-neutral society and decrease the demand for agricultural land

Degradation and modification of cellulose acetates by biological systems

A survey is given on recent findings in the enzymology of cellulose acetate degradation. Acetyl esterases have been identified as the principal enzymes, initiating cellulose acetate degradation as a prerequisite for endoglucanase-catalyzed cellulose acetate depolymerisation. Acetyl esterases are provided by nature to deacetylate naturally occurring partly acetylated polysaccharides, i.e. xylan and chitin. Accordingly they are not designed to attack high DS cellulose acetate. Under these circumstances acetyl esterases require a pretreatment of cellulose acetate, leading to some reduction in DS, in case highly substituted material should be degraded. One of these treatments is composting under the conditions of which a partial deacetylation may occur under the action of heat and high pH, facilitating the accessibility for acetyl esterases. However from the present knowledge it cannot be excluded that certain microbial specialists exist, being capable to degrade high DS cellulose acetate

Enzyme aided analysis of the substituent distribution along the chain of cellulose acetates regioselectively modified by the action of an Aspergillus niger acetylesterase

Two cellulose acetates (CA) were regioselectively deacetylated by action of a pure Aspergillus niger acetylesterase from the carbohydrate esterase family 1. The action of acetyl esterase along the polymeric chain was monitored by a new enzyme-aided method. CA with and without esterase modification was hydrolysed with a pure endoglucanase. The fragments were deutero-acetylated and separated by preparative SEC in CHCl<sub>3</sub>. The partial degree of substitution of the individual fragments was determined by <sup>1</sup>H-NMR spectroscopy. The investigation confirmed the uniform regioselective and regular deacetylation along the polysaccharide chain. The partial substitution in C<sub>2 </sub>seemed to be of major importance for the enzyme''s mode of action