Barriers against wear affect the spatial distribution of tree saplings in urban woodlands

http://www.elsevier.com/locate/issn/16188667In order to maintain indigenous, self-regenerating tree populations in urban woodlands, it is essential to identify factors affecting the survival of tree seedlings and saplings. In densely populated areas, intensive recreational use may cause considerable wear of the vegetation and soil, and decrease the total number of saplings. At the same time trees, high stones and other structural elements in a woodland patch can act as natural barriers and give shelter against wear. Hence, we hypothesised that with an increasing amount of wear, a greater proportion of tree saplings survive, and is thus found, close to these natural barriers. We tested this hypothesis with observational data, and described the microhabitat associations of different sapling species in detail to define the most favourable or unfavourable microhabitats. We recorded the microhabitats of saplings and randomly chosen points in 30 medium-fertile Picea abies dominant woodlands in Helsinki and the surroundings, Finland. The description included location in relation to physical objects (stones, trees, topography, etc.), other saplings, vegetation and canopy. We then compared the sapling microhabitats to those available (the random points). Our results suggest that the microhabitat associations of saplings change with increasing wear: Sorbus aucuparia, Populus tremula, Rhamnus frangula, Picea abies and Acer platanoides saplings grew more often close to natural barriers (obstacles X30 cm high excluding other saplings), the first three showing a statistically significant response to wear in logistic regression models. The saplings were able to grow in a variety of microhabitats, but the species also differed in their microhabitat associations. In general, saplings grew in groups, and in worn sites the grouping was more pronounced. With increasing wear the saplings associated more positively with trees, canopy cover and lush vegetation

A family of thermostable fungal cellulases created by structure-guided recombination

SCHEMA structure-guided recombination of 3 fungal class II cellobiohydrolases (CBH II cellulases) has yielded a collection of highly thermostable CBH II chimeras. Twenty-three of 48 genes sampled from the 6,561 possible chimeric sequences were secreted by the Saccharomyces cerevisiae heterologous host in catalytically active form. Five of these chimeras have half-lives of thermal inactivation at 63°C that are greater than the most stable parent, CBH II enzyme from the thermophilic fungus Humicola insolens, which suggests that this chimera collection contains hundreds of highly stable cellulases. Twenty-five new sequences were designed based on mathematical modeling of the thermostabilities for the first set of chimeras. Ten of these sequences were expressed in active form; all 10 retained more activity than H. insolens CBH II after incubation at 63°C. The total of 15 validated thermostable CBH II enzymes have high sequence diversity, differing from their closest natural homologs at up to 63 amino acid positions. Selected purified thermostable chimeras hydrolyzed phosphoric acid swollen cellulose at temperatures 7 to 15°C higher than the parent enzymes. These chimeras also hydrolyzed as much or more cellulose than the parent CBH II enzymes in long-time cellulose hydrolysis assays and had pH/activity profiles as broad, or broader than, the parent enzymes. Generating this group of diverse, thermostable fungal CBH II chimeras is the first step in building an inventory of stable cellulases from which optimized enzyme mixtures for biomass conversion can be formulated

Cavitation inception of a van der Waals fluid at a sack-wall obstacle

Cavitation in a liquid moving past a constraint is numerically investigated by means of a free-energy lattice Boltzmann simulation based on the van der Waals equation of state. The fluid is streamed past an obstacle and, depending on the pressure drop between inlet and outlet, vapor formation underneath the corner of the sack-wall is observed. The circumstances of cavitation formation are investigated and it is found that the local bulk pressure and mean stress are insufficient to explain the phenomenon. Results obtained in this study strongly suggest that the viscous stress, interfacial contributions to the local pressure, and the Laplace pressure are relevant to the opening of a vapor cavity. This can be described by a generalization of Joseph's criterion that includes these contributions. A macroscopic investigation measuring mass flow rate behavior and discharge coefficient was also performed. As theoretically predicted, mass flow rate increases linearly with the square root of the pressure drop. However, when cavitation occurs, the mass flow growth rate is reduced and eventually it collapses into a choked flow state. In the cavitating regime, as theoretically predicted and experimentally verified, the discharge coefficient grows with the Nurick cavitation number

Inhibitory effect of lignin on the hydrolysis of xylan by thermophilic and thermolabile GH11 xylanases

BACKGROUND: Enzymatic hydrolysis of lignocellulosic biomass into platform sugars can be enhanced by the addition of accessory enzymes, such as xylanases. Lignin from steam pretreated biomasses is known to inhibit enzymes by non-productively binding enzymes and limiting access to cellulose. The effect of enzymatically isolated lignin on the hydrolysis of xylan by four glycoside hydrolase (GH) family 11 xylanases was studied. Two xylanases from the mesophilic Trichoderma reesei, TrXyn1, TrXyn2, and two forms of a thermostable metagenomic xylanase Xyl40 were compared. RESULTS: Lignin isolated from steam pretreated spruce decreased the hydrolysis yields of xylan for all the xylanases at 40 and 50 °C. At elevated hydrolysis temperature of 50 °C, the least thermostable xylanase TrXyn1 was most inhibited by lignin and the most thermostable xylanase, the catalytic domain (CD) of Xyl40, was least inhibited by lignin. Enzyme activity and binding to lignin were studied after incubation of the xylanases with lignin for up to 24 h at 40 °C. All the studied xylanases bound to lignin, but the thermostable xylanases retained 22–39% of activity on the lignin surface for 24 h, whereas the mesophilic T. reesei xylanases become inactive. Removing of N-glycans from the catalytic domain of Xyl40 increased lignin inhibition in hydrolysis of xylan when compared to the glycosylated form. By comparing the 3D structures of these xylanases, features contributing to the increased thermal stability of Xyl40 were identified. CONCLUSIONS: High thermal stability of xylanases Xyl40 and Xyl40-CD enabled the enzymes to remain partially active on the lignin surface. N-glycosylation of the catalytic domain of Xyl40 increased the lignin tolerance of the enzyme. Thermostability of Xyl40 was most likely contributed by a disulphide bond and salt bridge in the N-terminal and α-helix regions. GRAPHICAL ABSTRACT: [Image: see text] SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1186/s13068-022-02148-4

Emulsifier composition of solid lipid nanoparticles (SLN) affects mechanical and barrier properties of SLN-protein composite films

Protein films can be applied to improve food quality and to reduce packaging waste. To overcome their poor water barrier properties, lipids are often incorporated. The function of incorporated lipid depends on the interface between filler and matrix. This study aimed to tailor the properties of a protein–lipid film by designing the oil/water interface to see if the concept of inactive/active filler is valid. Therefore, we varied the emulsifier stabilizing solid lipid nanoparticles (SLN) to promote (viaβ-lactoglobulin) or to minimize (via Tween 20) interactions between particle surface and protein. SLN were incorporated into protein films and film properties were determined. Addition of SLN led to significantly decreased water vapor permeability (WVP) of protein films. However, WVP was mainly affected by the emulsifiers and not by the lipid. Protein-stabilized SLN (BS) replaced a lacking protein in the protein network and therefore did not influence the mechanical properties of the films at ambient temperature. BS-composite films were temperature sensitive, as lipid and sucrose palmitate melted at temperatures above 40°C. Tween 20-stabilized SLN(TS) led to reduced tensile strengths, probably due to perturbative effects of TS and plasticizing effects of Tween 20. Dynamic mechanical analysis showed that TS and Tween 20 increased film mobility. Melting of lipid and emulsifiers, and temperature-dependent behavior of Tween 20 led to a strong temperature dependence of the film stiffness. By designing the interface, particles can be used to tailor mechanical properties of protein films. Tuned edible films could be used to control mass transfers between foods.Peer reviewe

Emulsifier Composition of Solid Lipid Nanoparticles (SLN) Affects Mechanical and Barrier Properties of SLN‐Protein Composite Films

Protein films can be applied to improve food quality and to reduce packaging waste. To overcome their poor water barrier properties, lipids are often incorporated. The function of incorporated lipid depends on the interface between filler and matrix. This study aimed to tailor the properties of a protein–lipid film by designing the oil/water interface to see if the concept of inactive/active filler is valid. Therefore, we varied the emulsifier stabilizing solid lipid nanoparticles (SLN) to promote (via β‐lactoglobulin) or to minimize (via Tween 20) interactions between particle surface and protein. SLN were incorporated into protein films and film properties were determined. Addition of SLN led to significantly decreased water vapor permeability (WVP) of protein films. However, WVP was mainly affected by the emulsifiers and not by the lipid. Protein‐stabilized SLN (BS) replaced a lacking protein in the protein network and therefore did not influence the mechanical properties of the films at ambient temperature. BS‐composite films were temperature sensitive, as lipid and sucrose palmitate melted at temperatures above 40 °C. Tween 20‐stabilized SLN (TS) led to reduced tensile strengths, probably due to perturbative effects of TS and plasticizing effects of Tween 20. Dynamic mechanical analysis showed that TS and Tween 20 increased film mobility. Melting of lipid and emulsifiers, and temperature‐dependent behavior of Tween 20 led to a strong temperature dependence of the film stiffness. By designing the interface, particles can be used to tailor mechanical properties of protein films. Tuned edible films could be used to control mass transfers between foods

The Hydrophobicity of Lignocellulosic Fiber Network Can Be Enhanced with Suberin Fatty Acids

Suberin fatty acids were extracted from outer bark of Silver birch (Betula pendula Roth.) using an isopropanolic sodium hydroxide solution. Laboratory sheets composed of lignocellulosic fiber networks were prepared from unbleached and unrefined softwood kraft pulp and further impregnated with suberin fatty acid monomers and cured with maleic anhydride in ethanol solution. The treatment resulted in hydrophobic surfaces, in which the contact angles remained over 120 degrees during the entire measurement. The fiber network also retained its water vapor permeability and enhanced fiber–fiber bonding resulted in improved tensile strength of the sheets. Scanning electron microscopy (SEM) images revealed that the curing agent, together with suberin fatty acids, was evenly distributed on the fiber surfaces and smoothing occurred over the wrinkled microfibrillar structure. High concentrations of the curing agent resulted in globular structures containing betulinol derivates as revealed with time-of-flight secondary ion mass spectrometry (ToF-SIMS). Also, the larger amount of suberin fatty acid monomers slightly impaired the optical properties of sheets

The Hydrophobicity of Lignocellulosic Fiber Network Can Be Enhanced with Suberin Fatty Acids

Suberin fatty acids were extracted from outer bark of Silver birch (Betula pendula Roth.) using an isopropanolic sodium hydroxide solution. Laboratory sheets composed of lignocellulosic fiber networks were prepared from unbleached and unrefined softwood kraft pulp and further impregnated with suberin fatty acid monomers and cured with maleic anhydride in ethanol solution. The treatment resulted in hydrophobic surfaces, in which the contact angles remained over 120 degrees during the entire measurement. The fiber network also retained its water vapor permeability and enhanced fiber–fiber bonding resulted in improved tensile strength of the sheets. Scanning electron microscopy (SEM) images revealed that the curing agent, together with suberin fatty acids, was evenly distributed on the fiber surfaces and smoothing occurred over the wrinkled microfibrillar structure. High concentrations of the curing agent resulted in globular structures containing betulinol derivates as revealed with time-of-flight secondary ion mass spectrometry (ToF-SIMS). Also, the larger amount of suberin fatty acid monomers slightly impaired the optical properties of sheets