Abstract
Cold adapted microbes inhabiting at near-zero temperatures produce psychrophilic enzymes to withstand such harsh environments and sustain their life cycles. They are the requisites for the adaption of psychrophilic organisms in the cold. A remarkable characteristic demonstrated by cold active enzymes is their high catalytic activity (kcat) at low temperatures which is obtained at the expense of substrate affinity (Km) and by minimizing their reaction dependence on the temperature. This is achieved by increasing their molecular flexibility and destabilizing the active site by decreasing the strength of weak interactions along with removal of factors responsible for stabilization, subsequently refining the active site dynamics. These activity-stability-flexibility relationships are understood with the help of folding funnel model. In addition, to overcome the free energy (ΔG) barrier of the active site, they exhibit distinct partition of energy into its enthalpic and entropic constituents in contrast to their mesophilic orthologues. These characteristics of cold active enzymes make them commercially useful for several biotechnological applications such as wastewater treatment, molecular biology, food industry, etc.
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Rishi, N., Yadav, R., Krishnani, S., Singh, R. (2022). Enzymatic Behaviour of Cold Adapted Microbes. In: Goel, R., Soni, R., Suyal, D.C., Khan, M. (eds) Survival Strategies in Cold-adapted Microorganisms. Springer, Singapore. https://doi.org/10.1007/978-981-16-2625-8_5
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