+91 8617752708

Annual Research & Review in Biology, ISSN: 2347-565X,Vol.: 24, Issue.: 1

Original-research-article

Activators and Inhibitors of α-glucosidase from Penicillium chrysogenum

 

Hamed M. El-Shora1*, Mohsen E. Ibrahim2 and Mohammad W. Alfakharany2

1Department of Botany, Faculty of Science, Mansoura University, Dakahlia, Egypt.

2Department of Botany, Faculty of Science, Port Said University, Port Said, Egypt.

Article Information

Editor(s):

(1) George Perry, Dean and Professor of Biology, University of Texas at San Antonio, USA.

Reviewers:

(1) Fellah Mamoun, Abbes Laghrour University, Annaba University, Algeria.

(2) Mina Ilyas, University of Lahore, Pakistan.

Complete Peer review History: http://www.sciencedomain.org/review-history/23132

Abstracts

α-glucosidase (EC: 3.2.1.20) from Penicillium chrysogenum Thom ATCC 10106 was induced by GSH at the lower concentrations. H2O2 was inhibitor at all tested concentrations and the IC50 was 92.2%v/v. AMP, ADP and ATP enhanced the activity revealing that α-glucosidase is endothermic enzyme. The chelating agents are ethylenediaminetetraacetate (EDTA), α-α-dipyridyl and o-phenanthroline inhibited the enzyme. IC50 for these three compounds were 7.1, 10.2 and 10.9 mM, respectively. The highest activity of α-glucosidase was recorded at 150 mM phosphate buffer. Mannitol as polyol protected the enzyme against heat inactivation. The five sugars trehalose, lactose, raffinose, glucose and sucrose protected α-glucosidase against thermo-inactivation at 60ºC. Also, sarcosine as a product of glycine provided α-glucosidase with appreciable thermostability at 60ºC.

Keywords :

P. chrysogenum; glutathione; adenosine compounds; chelating agents; trehalose; mannitol. 

Full Article - PDF    Page 1-9

DOI : 10.9734/ARRB/2018/38408

Review History    Comments

Our Contacts

Guest House Road, Street no - 1/6,
Hooghly, West Bengal,
India

+91 8617752708

 

Third Floor, 207 Regent Street
London, W1B 3HH,
UK

+44 20-3031-1429