alexa
Reach Us +44-1647-403003
Chemical Modification Of Polyvinyl Alcohol Fibrous Carrier Support For Immobilization And Stabilization Of Alcohol Dehydrogenase | 67613
ISSN: 2161-0703

Journal of Medical Microbiology & Diagnosis
Open Access

Like us on:

Our Group organises 3000+ Global Conferenceseries Events every year across USA, Europe & Asia with support from 1000 more scientific Societies and Publishes 700+ Open Access Journals which contains over 50000 eminent personalities, reputed scientists as editorial board members.

Open Access Journals gaining more Readers and Citations
700 Journals and 15,000,000 Readers Each Journal is getting 25,000+ Readers

This Readership is 10 times more when compared to other Subscription Journals (Source: Google Analytics)
Recommended Conferences
Share This Page

Chemical modification of polyvinyl alcohol fibrous carrier support for immobilization and stabilization of alcohol dehydrogenase

JOINT EVENT ON 15th International PHARMACEUTICAL MICROBIOLOGY AND BIOTECHNOLOGY CONFERENCE & 10th Annual MEDICAL MICROBIOLOGY SUMMIT & EXPO

Priydarshani Shinde

Monash University, Australia

Posters & Accepted Abstracts: J Med Microb Diagn

DOI: 10.4172/2161-0703-C1-006

Abstract
Immobilization of yeast alcohol dehydrogenase (ADH) on polyvinyl alcohol fiber (PVA) carrier has been investigated with regards to increase in stability at different pHs, storage and reusability. The strategy for immobilization involved functionalization of the fibrous carrier with chloropropionyl chloride followed by amination with ethylenediamine (EDA) serving as a spacer and finally crosslinking the ADH via glutaraldehyde (GA). The immobilization of ADH on PVA fibrous carrier results in optimal reaction pH shift from 7 to 9 and improvement in thermal stability by preserving 80% activity upon heating at 60ºC for 2 h. In addition the immobilized enzyme maintained 60% of its original activity after 8 repetitive use and showed reasonable storage stability at 4ºC in phosphate buffer (PBS) for 28 days. Alcohol dehydrogenases (ADHs) are widely used enzyme from dehydrogenase group of the enzyme to perform selective oxidations and reductions ranging from kinetic resolution to asymmetric reduction and can be used to generate an asymmetric center to facilitate the synthesis of chiral drugs. Therefore there is an interest for stabilization of ADH which in turn can be used in the development of flow reactors and biosensor applications.
Biography

Priydarshani Shinde has completed his MSc in Organic Chemistry from University of Pune and pursuing Doctoral research from Monash University in collaboration with National Science Agency of Australia (CSIRO), Melbourne, Australia. She has industrial experience in the biotech industry with a strong background of Biochemistry, Organic and Analytical Chemistry. She completed her Post-graduate Diploma in Patent Law. Currently, her research area extends the enhancement of ADH enzyme activity by immobilization methods for industrial applications.

Email: [email protected]

Top