Hot Spring Research Paper

A hot spring is a spring that is produced by emergence of geothermally heated ground water from the earth’s crust. There are geothermal hot springs in many locations all over the crust of the earth. Microbes can be found in hostile environments like the Hot springs, Arctic, deserts, and in rocks as much as 7 kilometers below the Earth’s surface. They typically live in complex communities with different kinds of symbiotic associations which include relationships with larger organisms like animals or plants. Microbiological exploration of hot spring is remaining a difficult task for microbiologist due to two major problems. First cultivation and isolation of microorganism at extreme temperature and second inability trap major uncultivable microbial

Sohna Hot-Spring, One of the oldest hot springs in India located in Sohna, it is 56 km from Delhi. People believe that many human diseases are cured by using spring water. In Gujarat, Tulshi Shyam and Unai hot springs and Tuva timba hot springs are widely explored for their microbial diversity. Among various hot spring in Gujarat mainly Tulshi Shyam hot spring is explore for their microbial diversity and biotechnology study. Singh et al., (2010) reported optimization, purification and characterization of extracellular thermostable enzymes; mainly amylases, proteases, cellulases and lipases which would have huge industrial applications, viz., starch processing, Food and Pharmaceuticals, detergent, and other related Biotechnological industries from Tulshi Shyam hot spring. The community analysis of Tulshi Shyam hot spring metagenome analysis was carried out using MGRAST server. The comparative community analysis was performing against the Yellow stone hot spring metagenome by Parmar and Patel, (2011). Sharma et al., (2011) reported characterization of a thermostable lipase showing loss of secondary structure at ambient temperature. A gene encoding extracellular lipase was cloned and characterized from metagenomic DNA extracted from hot spring soil was performed. The recombinant gene was expressed in E. coli and expressed protein was purified to homogeneity using hydrophobic interactions chromatography. Kinetic behavior of purified protein was also attempted. Furthermore CD spectroscopic study carried out in the temperature range of 25-95 °C revealed distortion in solution structure above 35