Thermophiles are a group of microbes adapted to thrive in ecological niches such as deep-sea hydrothermal vents, hot springs, and solfataric fields. Thermophilic microorganisms are found to be potential and good alternative source of thermostable enzymes [1
]. The investigation and application of thermostable enzymes from thermophilic microorganisms have received a lot of attention in industries ranging from food industry to waste management industries.
Thermophiles are of interest to enhance the thermostability of industrial enzymes. The modern concept of the nature of the thermostability of the enzymes from the thermophilic microorganisms can be reduced to two basic ideas. Firstly, the enhanced thermal stability of enzymes in thermophilic cells could be due to their molecular structure being different from that of their counter part mesophilic proteins. Secondly, the increased stability of the enzymes could be due to their supramolecular association with other components of the cell (lipids, polysaccharides, or proteins). In order to survive at high temperatures, thermophilic prokaryotes (Archaea and Eubacteria) adopt different strategies like GC-rich codons, the ratio of charged amino acids compared to uncharged amino acids, ionic interactions, amino acid preferences and their distribution, posttranslational modifications, and solute accumulation [3
]. Most of the industrial microbial lipases derived from fungi and mesophilic bacteria [4
]. Bacteria produce different classes of lipolytic enzyme, including carboxylesterases (EC 18.104.22.168), which hydrolyse small ester containing molecules at least partly soluble in water, true lipases (EC 22.214.171.124), which display maximal activity towards water insoluble long-chain triglycerides, and various types of phospholipase [5
More than 50 lipases have been identified, purified, and characterized to date which originate from natural sources such as animals, plants, and microorganisms (native or genetically engineered). A large number of beneficial thermophiles which produced lipases with good thermal stabilities have been found in diverse habitats [6
]. Their thermal stabilities particularly in the absence of sufficient amounts of water increase their popularity [8
The enormous potential of microbial lipases arises from the facts that they are (1) quite stable and active in organic solvents, (2) do not require cofactors, (3) exhibit a high degree of enhantio- and regioselectivity, and (4) possess a wide range of substrate specificity for the conversion of various unnatural substrates [9
]. Therefore screening and identification of thermostable lipolytic bacteria will act as a meaningful addition to the database on bacterial lipase research.