Summary1. Some large carnivore populations are increasing in Europe and North America, and minimizing interactions between people and carnivores is a major management task. Analysing the effects of human disturbance on wildlife from a predator-prey perspective is also of conservation interest, because individual behavioural responses to the perceived risk of predation may ultimately influence population distribution and demography. 2. The Scandinavian brown bear population provides a good model to study the interactions between an expanding large carnivore population, and people who use forests extensively for professional and recreational activities. We experimentally approached 52 GPS-collared brown bears (293 approaches on foot) from 2006 to 2011, to document the reaction of bears and quantify the effect of disturbance on bear movements. 3. None of the bears reacted aggressively to the observers. Although the location of the animals was known, bears were usually in quite concealed spots and were physically detected in only 16% of the approaches (seen in 42 approaches; heard in 6). However, the bears altered their daily movement patterns after the approaches. Bears increased movement at night-time and moved less at daytime, which was most visible in days 1 and 2 after the approaches, altering their foraging and resting routines. 4. Synthesis and applications. We provide experimental evidence on the effect of human disturbance on a large carnivore. The lack of aggressive reactions to approaching observers reinforces the idea that European brown bears generally avoid people, although bears can respond aggressively if they feel threatened (e.g. when wounded). However, the movement patterns of the bears changed after disturbance. Separating large carnivores and people temporally and spatially is an important goal for conservation and management. Conserving the shrub cover that provides concealment to the carnivores and keeping people away from the most densely vegetated spots in the forests is a way to avoid encounters between carnivores and people, therefore promoting human safety and carnivore conservation.
Enzymatic depolymerization of seaweed polysaccharides is gaining interest for the production of functional oligosaccharides and fermentable sugars. Herein, we describe a thermostable alginate lyase that belongs to Polysaccharide Lyase family 17 (PL17) and was derived from an Arctic Mid-Ocean Ridge (AMOR) metagenomics dataset. This enzyme, AMOR_PL17A, is a thermostable exolytic oligoalginate lyase (EC 4.2.2.26), which can degrade alginate, poly β-d-mannuronate and poly α-l-guluronate within a broad range of pH, temperature and salinity conditions. Site-directed mutagenesis showed that tyrosine Y251, previously suggested to act as catalytic acid, indeed is essential for catalysis; whereas mutation of tyrosine Y446, previously proposed to act as catalytic base, did not affect enzyme activity. The observed reaction products are protonated and deprotonated forms of the 4,5-unsaturated uronic acid monomer, Δ, two hydrates of DEH (4-deoxy-l-erythro-5-hexulosuronate), which are formed after ring opening and, finally, two epimers of a 5-membered hemiketal called 4-deoxy-d-manno-hexulofuranosidonate (DHF) formed through intramolecular cyclisation of hydrated DEH. The detection and NMR assignment of these hemiketals refine our current understanding of alginate degradation. Importance The potential markets for seaweed-derived products and seaweed processing technologies are growing, yet commercial enzyme-cocktails for complete conversion of seaweed to fermentable sugars are not available. Such an enzyme-cocktail would require the catalytic properties of a variety of different enzymes, where fucoidanases, laminarinases and cellulases together with endo- and exo-acting alginate lyases would be the key enzymes. Here we present an exo-acting alginate lyase that efficiently produces monomeric sugars from alginate. Since it is only the second characterized exo-acting alginate lyase capable of degrading alginate at industrially relevant higher temperatures of 60 °C, this enzyme may be of great biotechnological and industrial interest. In addition, in-depth NMR-based structural elucidation reveal previously undescribed rearrangement products of the unsaturated monomeric sugars generated from exo-acting lyases. The insight provided by the NMR assignment of these products facilitates future assessment of product formation by alginate lyases.
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