Spanish 
Chinese 
Russian 
German 
French 
Japanese 
Portuguese 
Hindi 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
Google Scholar citation report
Citations : 3330
Journal of Biotechnology & Biomaterials received 3330 citations as per Google Scholar report
Indexed In
- Index Copernicus
- Google Scholar
- Sherpa Romeo
- Open J Gate
- Genamics JournalSeek
- Academic Keys
- ResearchBible
- China National Knowledge Infrastructure (CNKI)
- Access to Global Online Research in Agriculture (AGORA)
- Electronic Journals Library
- RefSeek
- Hamdard University
- EBSCO A-Z
- OCLC- WorldCat
- SWB online catalog
- Virtual Library of Biology (vifabio)
- Publons
- Geneva Foundation for Medical Education and Research
- Euro Pub
- ICMJE
Useful Links
Recommended Journals
Related Subjects
Share This Page
In Association with
Purification, partial biochemical characterization and immobilization of Vigna mungo �±-galactosidase on magnetic chitosan nanoparticles
6th World Congress on Biotechnology
Ramadevi Mutra, Deepesh Panwar and Mukesh Kapoor
CSIR-Central Food Technological Research Institute, India
Posters-Accepted Abstracts: J Biotechnol Biomater
Abstract
�±-galactosidase (�±-D-galactoside galacto hydrolase, E.C. 3.2.1.22) catalyses the hydrolysis of �±-1, 6-linked terminal galactose residues from oligosaccharides like melibiose, raffinose and stachyose as well as galactomannans, galactolipids and galactoproteins. �±-galactosidase have plethora of applications in food & feed (improvement in nutritional value food/feed, gelling properties of gums & beet sugar crystallization), medicine (blood group transformation, treatment of Anderson-Fabryâ��s disease and xeno-rejection) and paper & pulp industry. In the present study, �±-galactosidase from locally available variety of black gram (Vigna mungo) seeds was purified to homogeneity by using a combination of citric acid precipitation, ammonium sulphate precipitation (25-60% saturation), DEAE-Cellulose, CM-Sepharose followed by ConA Sepharose 4B chromatography with 39.1% yield and 1500-fold purification. The purified enzyme migrated as a single band (Mwâ��40 kDa) on silver stained SDS-PAGE. Purified �±-galactosidase showed high activity in a narrow range of pH 4-5 with maximal activity at pH 5. The enzyme had less than 20% of its activity at acidic pH (3) or alkaline pH (8). The optimum temperature of �±-galactosidase was found to be 55o C. Most of the tested metal ions were found to reduce the activity of �±-galactosidase by up to 29% at 1 mM concentration. However, Hg++ drastically inhibited enzyme activity. The purified �±-galactosidase was immobilized on chitosan iron oxide nanoparticles (�±-GAL-MNP) using glutaraldehyde (540 mM) as a cross linker with high immobilization efficiency (â��90%). The �±-galactosidase loaded nanoparticles were further characterized by Scanning Electron Microscopy and Fourier Transform Infrared Spectroscopy. Further, cross-linked enzyme aggregates of crude �±-galactosidase were made and also immobilized on chitosan iron oxide nanoparticles (�±-GAL-CLEA-MNP). The �±-GAL-MNP and �±-GAL-CLEA-MNP showed good retention of activity after repeated usage.Biography
Email: mkapoor@cftri.res.in
