The promising property of enzymes from thermoacidophiles is activity at low pH and high temperature, and therefore, these enzymes can be used in starch, textile and fruit juice industries. The demand for enzymes from extremophiles may increase in the future because of their activity under harsh industrial conditions.
Thermophilic Bacillus strain with an optimum temperature of growth at 45C and capable of producing alpha-amylase was isolated from soil.
The present study was undertaken with the following objective in mind.
1. Identification of the isolate.
2. Assessment of amylase production in different media.
3. Study the effect of different factors on amylase production.
Based on their mode of action, the enzymes are divided into two categories: endoamylases (amylases, pullulanases, isoamylase) and exoamylases amylase, glucoamylase. Amylases are extracellular enzymes that catalyze the hydrolysis of 1,4-glycosidic linkages in starch liberating linear and branched oligosaccharides of varying chain lengths as well as glucose; the end products have confirmation at C1.
These are categorized based on their end product as saccharifying and liquefying amylases. Saccharifying amylases produce free sugars but reduce the viscosity of starch pastes slowly. On the contrary, liquefying amylases rapidly reduce the viscosity of starch pastes without producing free sugars as compared to saccharifying amylases.
Production of α-amylases
The production of α-amylase in submerged and solid-state fermentation has been studied extensively. The growth and enzyme production of various microorganisms are affected by a number of physical and chemical parameters, such as carbon, nitrogen and phosphate sources, metal ions, temperature, pH, agitation, aeration, inoculum age, and size. Most α-amylases are inducible enzymes.
Types of Amylase
α- Amylase
Amylase refers to a group of an enzyme whose catalytic function is to hydrolyze the starch. They digest carbohydrates (Polysaccharides) into smaller disaccharide units, eventually converting them into monosaccharides such as glucose.
α- amylase are endo-acting which hydrolysis α-(1,4) glycosidic linkages in starch and related substrates. They produce α-limiting dextrin, oligosaccharides, and glucose as end products.
β- Amylase
It is an exo-acting enzyme that hydrolyzes starch from the nonreducing end of the polysaccharide chain. This enzyme catalyzes the maltose from the non-reducing ends of starch. The enzyme has a strict specificity to produce β- anomeric maltose and has been classified as a typical inverting enzyme together with glucoamylase by Koshland.
Microorganisms Involved in Producing Amylase
Starch is one of nature’s major energy storage compounds. Such energy storage compounds are only useful when are rapidly broken down and the stored energy is released. There are two enzymes that do this task. Both are named “Amylase” and are produced by different groups of microorganisms. Bacteria and molds are high produced by different groups of microorganisms.
Amylases can be derived from several sources, such as plants, animals, bacteria, and fungi. Because of the short growth period, biochemical diversity and the ease with which enzyme concentrations might be increased by environmental and genetic manipulation, the enzymes from microbial sources generally meet industrial demands.
In this study, it was found that the Bacillus sp. MD-1 was found to be a good amylase producer. Optimum enzyme production occurred in medium IV with an initial pH of 6.0 at temperature 420C and 48 h of incubation at 120 rpm. However further are required to assess the full potentials of the isolate.
This was an overview of the project "production of amylase from thermophilic bacillus". If you need more information, just download the project from the below link. All credits go to the author and use this project only for your reference purpose.
Author:- Mamta Deorari
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