3 - Marine biocatalysts and their stability: molecular approach

Abstract

Enzymes catalyse various biochemical reactions of an organism that render them compatible with life, and are an essential target for the adaptation of that particular system to any environment. Psychrozymes of marine psychrophiles have received increased attention in the last few years due to their central role in the cold adaptation. Cold adapted enzymes are of major interest of study in today’s microbial research to investigate the thermodynamic stability of the cold active proteins along with their flexibility or plasticity and their catalytic efficiency at the fundamental level. Analysis of structural features such as intramolecular hydrogen bonds and ion–pairs, amino acid content, surface hydrophobicity, helix stability and core packing reveal the basic intricacies involved in different small selections of structural adjustments for gaining high catalytic efficiency accompanied by reduced thermal stability and increased molecular flexibility for working at low temperatures. Psychrozymes are highly important in extremophile metabolism as well as serving as valuable models for fundamental research in protein folding, catalysis and biotechnological applications. In this chapter, an overview on the molecular aspects of marine biocatalysts, low temperature adaptation and their industrial applications are discussed.