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Some like it cold: biocatalysis at low temperatures.
Expression, purification, crystallization and preliminary X-ray crystallographic studies of a psychrophilic cellulase from Pseudoalteromonas haloplanktis.
Crystallographic studies of this cold-adapted enzyme have been initiated in order to contribute to the understanding of the molecular basis of the cold adaptation and the high catalytic efficiency of the enzyme at low and moderate temperatures.
Did psychrophilic enzymes really win the challenge?
These particular properties render cold enzymes particularly useful in investigating the possible relationships existing between stability, flexibility, and specific activity and make them potentially unrivaled for numerous biotechnological tasks.
A perspective on cold enzymes: current knowledge and frequently asked questions.
The impact of low temperatures on life, the diversity of adaptation to counteract these effects and the features proposed to account for low thermal stability and cold-activity are examined, following the chronological order of the catalytic cycle phases.
Extreme catalysts from low-temperature environments.
The linker region plays a key role in the adaptation to cold of the cellulase from an Antarctic bacterium.
The data indicate that the sequential shortening of the LR induces a regular decrease of the specific activity towards macromolecular substrates, reduces the relative flexibility and concomitantly increases the thermostability of the shortened enzymes.