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PARTIAL CHARACTERIZATION OF AMYLASE ENZYME FROM NEWLY
ISOLATED BACTERIAL STRAIN FROM GARDEN SOIL
ABHISHEK
1
, VISHAL
2
, MANPREET
3
, NAVNEET BATRA
4
& MEENU WALIA
5
1,2,3
Department of Biotechnology, SD College, Ambala Cantt., India
4
Department of Biotechnology, GGDSD College, Chandigarh, India
5
Assistant Professor, Department of Biotechnology, SD College, Ambala Cantt., India
ABSTRACT
Amylase producing bacterial strain MB2 was isolated from soil and it showed maximum production of enzyme in 48
hours. Crude enzyme has an optimum temperature of 40
o
C and optimum pH of 7.0. The relative enzyme activity of 97%
was observed at pH 6. After incubation for 40oC, the enzyme lost only 2.5% of activity after 48 hours of incubation.
More than 90% of activity were retained even after 48 hours at pH 7. Calcium acts as an activator for amylase.
KEYWORDS: Amylase, Stability, Starch Hydrolysis, Optimum pH & Calcium
Received: Jun 09, 2017; Accepted: Jul 04, 2017; Published: Jul 10, 2017; Paper Id.: IJBTRAUG20172
INTRODUCTION
Amylase is an industrially important enzyme, which break down starch into maltose and dextrins, which
further finally degraded into glucose units. Due to the commercial application of amylase enzyme in paper
industry, induction of sugar from production of sugar syrup, fabrics decision, liquefaction of starch, brewing
industry, pharmaceuticals is essentially important for industrial purpose (Ito et al., 1998; Ammar et al., 2002; Xie
et al., 2014). Application of α-amylase for fiber splitting in leather processing was reported by Pandi et al., (2016).
The main source of amylase enzyme are plants, animals and microorganisms. Mainly, microorganisms are used for
amylase production. Because of their stability at extreme conditions, biochemical versatility, the production rate is
higher and large scale availability of microbial strains in a short time is possible at low cost production.
Amylase is also known as glycoside hydrolases as it acts on α 1, 4 glycosidic bond. They are highly
specific for substrate. Alpha and beta are the main subtypes of amylase enzyme. Alpha amylase is faster acting
enzyme as compared to beta amylase. Endoamylase and exoamylase are two categories of enzyme. Endoamylase
enzyme led to the formation of linear and branched chain oligosaccharides by catalyzing hydrolysis in a random
manner within the starch molecule. However, exoamylases produces shorter end products by hydrolyzing from the
nonreducing end. Amylose and amylopectin are two glucose polymers which are connected by glycosidic bond
and ultimately led to the formation of the starch molecule. Amylose is a linear polymer which consists of 6000
glucose units that are joined by α-1, 4 glycosidic bond, while amylopectin consists of 10-60 glucose units which
are linked by α-1, 4 glycosidic bond by 15-45 glucose units having α-1, 6 linked side chains. To maintain their
structural conformation, stability and activity amylase enzyme require calcium ion.
Amylase enzyme isolated from bacteria, fungi and yeast have been used in scientific research and in
Original Article
International Journal of Bio-Technology
and Research (IJBTR)
ISSN (P):2249-6858; ISSN (E):2249-796X
Vol. 7, Issue 3, Jun 2017, 21-28
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