Production of β-cyclodextrin from pH and thermo stable cyclodextrin glycosyl transferase, obtained from arthrobacter mysorens and its evaluation as a drug carrier for Irbesartan

Rajesh, Y and Narayanan, K and Reddy, Sreenivasa M and Bhaskar, Vijaya K and Shenoy, Gautham G and Subrahmanyam, VM and Rao, Venkata J (2015) Production of β-cyclodextrin from pH and thermo stable cyclodextrin glycosyl transferase, obtained from arthrobacter mysorens and its evaluation as a drug carrier for Irbesartan. Current Drug Delivery, 12. pp. 1-10. ISSN 1875-5704

[img] PDF
V.M. Subrahmanyam-CDD-MS[1].pdf - Published Version
Restricted to Registered users only

Download (2MB) | Request a copy

Abstract

Cyclodextrins (CDs) are carrier molecules produced by cyclization of α-1,4-glucans by Cyclodextrin Glycosyl Transferase (CGTase). These torus shaped molecules have hydrophobic cavity and hydrophilic shell making them useful in pharmaceutical, food, textile, pesticide and cosmetic industries. In this study, culture conditions for the production of CGTase by organism belonging to Arthrobacter genus obtained from a paddy field soil were optimized by single parameter mode. Soluble starch, yeast extract and magnesium sulphate played an important role in CGTase production. Percentage increase in CGTase yield under optimized conditions was 396.77%. The enzyme precipitated by 60% ammonium sulphate was purified using DEAE-sepharose. The molecular weight of the purified protein as determined by SDS-PAGE was 75 kDa. Purified CGTase was thermostable and stable over a wide pH range. Dissolution studies on β-cyclodextrin-Irbesartan complex revealed that β-CDs formed were useful in preparing immediate release oral dosage forms.

Item Type: Article
Uncontrolled Keywords: Thermostable CGTase; cyclodextrin; β- cyclodextrin and Irbesartan inclusion complex.
Subjects: Pharmacy > MCOPS Manipal > Pharmaceutical Biotechnology
Depositing User: KMC Library
Date Deposited: 24 Sep 2015 14:32
Last Modified: 24 Sep 2015 14:32
URI: http://eprints.manipal.edu/id/eprint/144104

Actions (login required)

View Item View Item