<?xml version="1.0" encoding="utf-8"?>
<Journal>
<Journal-Info>
<name>International Journal of Pharma and Bio Sciences</name>
<website>ijpbs.net</website>
<email>editorijpbs@rediffmail.com (or) editorofijpbs@yahoo.com (or) prasmol@rediffmail.com</email>
</Journal-Info>
<article>
<article-id pub-id-type='other'>10.22376/ijpbs.2019.10.1.p1-12</article-id>
<issue_number>Volume 6 Issue 4</issue_number>
<issue_period>2015 (October - December)</issue_period>
<title>MICROBIAL α-AMYLASES: STRUCTURE, FUNCTION AND APPLICATION – A REVIEW </title>
<abstract>α-amylases are most important industrial enzyme and hold a major market share of enzyme sales. They hydrolyze starch molecules to small diverse products as dextrin and progressively smaller molecules of glucose units. α-amylases belong to the family 13(GH-13) of the glycoside hydrolase group of enzymes. Microbial α-amylases have a wide range of applications ranging from starch conversion to pharmaceutical applications. This article highlights on the characteristic features of α-amylase structure, function, family, primary microbial sources and uses of α-amylases in industrial purposes.</abstract>
<authors>B.N. SWARGIARI</authors>
<keywords>Î±-amylase, glycoside hydrolases, GH-13, metalloenzymes, TIM barrel, catalytic domain.</keywords>
<pages>1133-1140</pages>
</article>
</Journal>
