alexa β-Galactosidase of Penicillium chrysogenum: Production, Purification, and Characterization of the Enzyme


Journal of Food & Industrial Microbiology

Author(s): Zoltn Nagy, Tnde Kiss, Attila Szentirmai, Sndor Bir

Abstract Share this page

Intracellular β-galactosidase from Penicillium chrysogenum NCAIM 00237 was purified by procedures including precipitation with ammonium sulfate, ion-exchange chromatography on DEAE–Sephadex, affinity chromatography, and chromatofocusing. These steps resulted a purification of 66-fold, a yield of about 8%, and a specific activity of 5.84 U mg−1 protein. Some enzyme characteristics were determined using o-nitrophenyl-β-d-galactopyranoside as substrate. The pH and temperature optimum of the activity were about 4.0 and 30°C respectively. The Km and pI values were 1.81 mM and 4.6. β-Galactosidase of P. chrysogenum is a multimeric enzyme of about 270 kDa composed of monomers with a molecular mass of 66 kDa.

This article was published in Protein Expression and Purification and referenced in Journal of Food & Industrial Microbiology

Relevant Expert PPTs

Relevant Speaker PPTs

Recommended Conferences

Peer Reviewed Journals
Make the best use of Scientific Research and information from our 700 + peer reviewed, Open Access Journals
International Conferences 2017-18
Meet Inspiring Speakers and Experts at our 3000+ Global Annual Meetings

Contact Us

© 2008-2017 OMICS International - Open Access Publisher. Best viewed in Mozilla Firefox | Google Chrome | Above IE 7.0 version