<?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 5 Issue 1</issue_number>
<issue_period>2014 (January - March)</issue_period>
<title>ISOLATION, PURIFICATION AND QUANTITATIVE ANALYSIS OF CYSTEINE PROTEASE, BROMELAIN FROM ANANAS COMOSUS (PINEAPPLE) </title>
<abstract>Proteases were extracted and assayed from the fruit of  lessThan i greaterThan Ananas comosus lessThan /i greaterThan  (Pineapple). They were precipitated utilizing variable concentrations of acetone (40%,60%,80%,100%), ammonium sulphate (45%,65%) and Jello (40%,60%,80%,100%). The extracted enzymes exhibited proteolytic activity which was determined using other assay techniques. Activity determined for  lessThan i greaterThan Ananas comosus lessThan /i greaterThan  was 2U/mL. The enzymes were, in their crude state, analyzed using SDS-AGE. Bands were observed between the molecular weight range of 24-45 KDa. The enzymes were purified from the extract by anion exchange chromatography using Silica Gel Column (pH-8.0, Sodium Phosphate Buffer). The elution of  lessThan i greaterThan Ananas comosus  lessThan /i greaterThan extract resulted in two bound fractions. Since the second fraction of the  lessThan i greaterThan Ananas comosus  lessThan /i greaterThan extract exhibited no protease activity, it was ignored. The purified samples were analyzed using SDS-AGE, the purified extract of  lessThan i greaterThan Ananas comosus  lessThan /i greaterThan displays a single band (characteristic of bromelain, a monomeric molecule).</abstract>
<authors>HEMANT KR. SHARMA, RICHA SRIVASTAVA AND SHUBHANGI SHUKLA</authors>
<keywords>Protease, SDS-PAGE, Silica Gel, Ananas comosus</keywords>
<pages>429-437</pages>
</article>
</Journal>
