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Comparative studies on the thermal properties of a trypsin-like protease intwo hermit crabs
Helgoländer Meeresuntersuchungen volume 46, pages 45–52 (1992)
Abstract
The thermal characteristics of a trypsin-like protease were surveyed comparatively in two hermit crabs,Pagurus bernhardus (Linné) 1758 from the German Bight, andClibanarius striolatus Dana 1852 from the Western Indo-Pacific. In both enzymes, activity is maximal at a temperature around 50°C. Compared withPagurus, the protease inClibanarius is characterized by a considerably higher stability at elevated temperatures. Furthermore, the latter is less inhibited by two specific trypsin inhibitors. On an energetical level, distinct differences between the species are displayed. In both species, Km is strongly affected by temperature; lowest Km values do not coincide with the mean environmental temperature. The affinity ofPagurus protease for substrate at 40°C is about 17 times that at 0°C; inClibanarius this factor amounts only to 4.4. At temperatures >10°C, activation energy in the tropical speciesClibanarius is distinctly higher (28.3 kJ·mol−1) than in the boreal speciesPagurus (20.0 kJ·mol−1).
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This is publication no. 452 of the Alfred Wegener Institute for Polar and Marine Research at Bremerhaven.
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Dittrich, B. Comparative studies on the thermal properties of a trypsin-like protease intwo hermit crabs. Helgolander Meeresunters 46, 45–52 (1992). https://doi.org/10.1007/BF02366211
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DOI: https://doi.org/10.1007/BF02366211