Astroenzymology – the environmental limits of enzyme activity

Using organisms from extreme terrestrial environments as models for extraterrestrial life may lead us to underestimate the range of environments that life may inhabit. An alternative approach is to inspect the range of conditions over which crucial biomolecules might function. Recent investigations of enzyme activity suggest that they have the potential to function over a wider range of environmental conditions than expected. Although the upper temperature limit for enzyme stability is unclear, some enzymes are active up to 130°C. The evidence is that the instability of enzymes is a functional requirement, rather then because of any restraint on achieving higher stability. There is no evidence that enzyme activity ceases at low temperatures; it declines in a predictable manner to the lowest temperature at which it has been possible to make measurements, -100°C. It has been generally accepted that dehydration stops enzyme activity but this acceptance may have arisen partly from the technical difficulty of assessing enzyme activity without a fluid medium for diffusion. Experiments using anhydrous organic solvents or gas phase substrates suggest activity occurs in enzymes at very low hydration

An Information-Theoretic Analysis of Thompson Sampling

We provide an information-theoretic analysis of Thompson sampling that applies across a broad range of online optimization problems in which a decision-maker must learn from partial feedback. This analysis inherits the simplicity and elegance of information theory and leads to regret bounds that scale with the entropy of the optimal-action distribution. This strengthens preexisting results and yields new insight into how information improves performance

Isolation and characterisation of two chymotrypsins from Allocyttus niger (black oreo dory) viscera

Two serine proteases from the viscera of deep-sea fish, black oreo dory (Allocyttus niger),were purified by hydrophobic, affinity, and cation exchange chromatography. They were designated as chymotrypsins on the basis of substrate specificity and susceptibility to inhibitors. The pH optima of chymotrypsin I and II were 8.6 and 10, respectively. Chymotrypsin II retained a remarkable 80% activity at pH 12.5. Thermal stability of both enzymes was enhanced in the presence of calcium ions. Both chymotrypsins were inhibited by high concentrations of substrate Suc-AAPF-NA

Fractionation of nitrogen isotopes by animals: a further complication to the use of variations in the natural abundance of ¹⁵N for tracer studies

A study of the fractionation of nitrogen isotopes in the diet by cattle is described and the results discussed. Compared with the diet, urine had a lower ratio of ¹⁵N to ¹⁴N, but faeces, blood and milk all had a higher ratio. It is argued that the use of natural ¹⁵N as a tracer in grazed ecosystems is more complicated than was at first thought