<?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 3 Issue 1</issue_number>
<issue_period>2012 (January - March)</issue_period>
<title>Different Aspects Of Production Of Thermolysin-Like Protease From <i>Thermoactinomyces Thalpophilus</i> </title>
<abstract> lessThan i greaterThan Thermoactinomyces thalpophilus  lessThan /i greaterThan (Gene Bank accession number EF 397000) isolated from the waters of a thermal spring situated in Western Ghats, Maharashtra, India was found to be a potent producer of thermolysin-like protease (TLP). TLP was capable of bringing about condensation/ biotransformation of two amino acids, viz. Z-L-aspartic acid and L-phenylalanine methyl ester into aspartame, which is an artificial, non-saccharide sweetener used as a sugar substitute in some foods and beverages. The maximum yield 181 U/ml/min was obtained at 55 lessThan sup greaterThan o lessThan /sup greaterThan C in glucose yeast extract medium(pH 7.2) containing CaCl lessThan sub greaterThan 2  lessThan /sub greaterThan ( 0.2 % w/v) with an inoculum size of 0.5% v/v after 18 hours incubation under shake-culture conditions (130 rpm)</abstract>
<authors>D.R Majumder And P.P Kanekar</authors>
<keywords>TLP, biotransformation, aspartame, Thermoactinomyces thalpophilus., Thermolysin</keywords>
<pages>610-627</pages>
</article>
</Journal>
