Thermostability is considered to be an important parameter to measure the feasibility of
enzymes for industrial applications. Generally, higher thermostability makes an enzyme …

By far the largest proportion of the Earth's biosphere is comprised of organisms that thrive in
cold environments (psychrophiles). Their ability to proliferate in the cold is predicated on a …

Psychrophiles thriving permanently at near‐zero temperatures synthesize cold‐active
enzymes to sustain their cell cycle. Genome sequences, proteomic, and transcriptomic …

Enzymes from extremophilic microorganisms usually catalyze chemical reactions in non-
standard conditions. Such conditions promote aggregation, precipitation, and denaturation …

The molecular bases of thermal and cold stability and adaptation, which allow proteins to
remain folded and functional in the temperature ranges in which their host organisms live …

The biotechnological applications of enzymes are limited due to the activity–stability trade-
off, which implies that an increase in activity is accompanied by a concomitant decrease in …

The molecular mechanisms underlying thiol-based redox control are poorly defined.
Disulfide bonds between Cys residues are commonly thought to confer extra rigidity and …

Cold-adapted enzymes, produced in cold-adapted organisms, are a class of enzyme with
catalytic activity at low temperatures, high temperature sensitivity, and the ability to adapt to …

Many industrial processes used to produce chemicals and pharmaceuticals would benefit
from enzymes that function under extreme conditions. Enzymes from extremophilic …

Thermolysin hydrolyzates of freshly isolated, extensively stored (6 years, 6° C, dry) and
heated (60 min, 90° C, in excess water) bovine serum albumin (BSA) samples were …