Cloning and expression of α-Amylase gene from Bacillus subtilis in Pichia pastoris and Escherichia coli.
Introduction
Enzyme is a type of catalyst that present in living organisms used for many biotechnological functions in various industrial processing. It has a special characteristic that allows the chemical reaction to speed up without being altered, thus significantly improve the industrial productivity (Roy et al. 2012). Among various enzymes available in market, α-amylase has received a special attention in commercial production due to its widely used applications. α-Amylase contributed to 50% of the world enzyme production and has a great importance in many industries such as in food processing, laundry and also in pharmaceutical (Asgher et al. 2007). α-Amylase enzyme acts on α-1,4 glycosidic bonds in starch substrate backbone leading to the formation of soluble maltodextrins, glucose and maltose (Vidyalakshmi et al. 2009). This characteristic is extremely useful especially in industries that require the hydroxylation of starch such as the production of sugar syrups. The α-amylase enzyme can be obtained from various sources such as plants animals and microbes (Ahmed et al. 2011). However, the naturally occurring enzyme is still insufficient to support all the industrial production and therefore, it is crucial to find a new alternative sources, which is cost-efficient and high yield capacity to meet the supply demand (Yin et al. 2003).
In industries, the microbial α-amylase enzyme such as from Bacillus subtilis is more preferable compared to other sources due to its thermo stability (Asgher et al. 2007). This unique feature is favorable in many commercial processing that requires high temperature such as the liquefaction of starch. The aim of this literature review is to determine the cloning and expression of α-amylase gene from Bacillus subtilis in E.