cryoenzymes
Cryoenzymes, commonly referred to as psychrophilic enzymes, are enzymes that catalyze chemical reactions efficiently at low temperatures, typically near or below 15°C, and originate from organisms adapted to cold environments such as polar oceans, alpine soils, and deep-sea habitats. Their activity profile is characterized by high catalytic efficiency at low temperatures, a broad catalytic temperature range, and relatively low thermal stability compared to mesophilic counterparts. These enzymes often exhibit increased structural flexibility, particularly around the active site, and reduced stabilizing interactions such as ion pairs and disulfide bonds, enabling substrates to access the active site more readily in cold conditions. Such adaptations come at the cost of stability at higher temperatures, limiting industrial use without stabilization strategies.
Biological role: In cold environments, cryoenzymes enable metabolic processes at temperatures where other enzymes would be
Applications: In biocatalysis and bioprocessing, cryoenzymes are attractive for reactions requiring low-temperature operation to preserve thermolabile
Discovery and study: Cryoenzymes are identified via cultivation of psychrophilic microbes, metagenomic sequencing, and enzyme assays
Limitations: Limitations include limited stability, production challenges, and the need for cold-chain storage. Ongoing research seeks