Purification and properties of alpha amylase produced from bacillus subtilis isolated from the soil

Thesis Overview

<p> </p><p><strong>1.0 &nbsp; &nbsp; &nbsp; &nbsp; &nbsp; </strong><strong>Introduction</strong></p><p>The potential of using microorganisms as biotechnological sources of industrially relevant enzymes has stimulated interest in the exploration of extracellular enzymatic activity in several microorganisms (Abu <em>et al</em>., 2005). Microbial species exist in many environments like extremes of temperature, pH, chemical content and pressure. This existence of microbes is due to certain genetic and or physiological adaptations (Aguilar,1996). Thermophiles are the organisms which are adapted to grow optimally at high temperatures. The enzymes from thermophiles are known as thermophilic enzymes and these enzymes find a number of commercial applications because of their thermostability and thermoactivity. One of the most attractive attributes of thermophiles is that they produce enzymes capable of catalysing biochemical reactions at temperature higher than those of mesophilic organisms (Aguilar,1996).</p><p>Alteration in the amino acid composition of proteins bring about additional electrostatic interactions, formation of hydrogen and disulfide bonds, enhancement of hydrophobic interactions or compaction of the structure and there are only a few cysteine residues in thermophilic enzymes. Amylases are enzymes which utilize and hydrolyse starch and glycogen as substrate. On the basis of how amylase breakdown starch molecules and produce glucose, these are classified as α-Amylase (which breaks down the bonds at random manner), β-amylase (which acts on the glucose-glucose bonds and remove two glucose unit at a time and produce maltose and amyloglucosidase (AMG), β-Amylase breaks the non reducing end of the straight chain and produce glucose. Amylase producing industries need a temperature tolerating amylase-producing bacterial strains which are able to produce thermostable amylase enzyme, because temperature and pH controls are critical during some stages of production.</p><p>α-Amylase (endo 1,4-α D glucan glucohydrolase) is an extracellular enzyme which acts on substrate starch and degrades it into disaccharide and trisaccharide (Crabb and Mitchinson,1997). Amylase can be derived from various sources such as microorganisms (bacteria and fungi), plants and animals. Microbial production of amylase is more fruitful than that of other sources like plants or animals because microbial amylase is fast, cost efficient, easy and moderate for obtaining enzymes of desired characteristics (Leveque <em>et al</em>., 2000). In general, the enzymes get denatured and lose their activities at temperatures over 50-600C.</p> <br><p></p>