Purification and characterization of α-glucosidase from Penicillium chrysogenum.

Hamed M El-Shora, Saida M Messgo, Mohsen E. Ibrahim, Mohamed W alfakharany


α-glucosidase (EC: was isolated and purified from Penicillium chrysogenum Thom ATCC 10106 by ammonium sulphate precipitation (75%), DEAE-cellulose and Sephadex G-200. The specific activity was 140 units (U) mg-1 protein. The enzyme expressed a single band using SDS-PAGE and the molecular weight of the enzyme was nearly 43KDa. The optimal pH and temperature were 8 and 40ºC. The activation energy was 17.94 k J mol-1. The optimal incubation time was 40 min. Glutamine, glutamic acid, cysteine, alanine, phenylalanine, glycine, methionine, asparagine enhanced the enzyme activity and cysteine was the best enhancer. However, cystine and arginine inhibited α-glucosidase activity. The Vmax values were 48 and 38.1 U mg-1 protein with and without of cysteine, respectively. However, Km values were 0.21 and 0.25 mM in absence and presence of cysteine, respectively.


P. chrysogenum, α-glucosidase, Purification, Amino acids, Kinetics.

Full Text:



Bhat, M, Zinjarde SS, Bharagava SY, Kumar AR, Joshi BN, Antidiabetic activity of Gnidia glauca and Dioscorea bulbifera: Potent amylase and glucosidase inhibitors Evi Based Complement Alternative Medical. 2012; doi:10.1155/2012/929051. [2] Lin, A. H. M., Nichols, B. L., Quezada-Calvillo, R., Avery, S. E., Sim, L., Rose, D. R., Hamaker, B. R. Unexpected high digestion rate of cooked starch by the Ct-maltase-glucoamylase small intestine mucosal α-glucosidase subunit. PLoS One. 5 (2012) 354-373.‏ [3] El-Shora, H.M., Ibrahim, M.E., Alfakharany, M. W. Activators and Inhibitors of α-glucosidase from Penicillium chrysogenum. Annu Res and Rev in Biol, 24 (2018) 1-9. [4] West, I. C. Radicals and oxidative stress in diabetes. Diab Med. 3 (2000) 171-180.‏ [5] Hiroyuki, F., Tomohide, Y., and Kazunori, O. Efficacy and safety of Touchi extract, an α-glucosidase inhibitor derived from fermented soybeans, in non-insulin-dependent diabetic mellitus. The J. of Nutritional Biochem. 6 (2001) 351-356. [6] Kim, W. J., Lee, S. W., Park, S. W., Kim, Y. H., Yun, S. C., Lee, J. Y., Choi, S. W. Randomized comparison of everolimus-eluting stent versus sirolimus-eluting stent implantation for de novo coronary artery disease in patients with diabetes mellitus (Essence-Diabetes). Circulation. 8 (2011) 886-892.‏‏ [7] De Souza P. M., de Sales P. M., Simeoni, L. A., Silva, E. C., Silveira D. , Magalhaes P., Inhibitory activity of α-glucosidase by plant extracts from the Birazilian cerrado, Planta Medica. 78 (2012) 393-399. [8] Hirsh AJ, Yao SY, Young JD, Cheeseman CI. Inhibition of glucose absorption in the rat jejunum: a novel action of alpha-D-glucosidase inhibitors Gastroenterol, 113 (1997) 205-511. [9] Bakkalbaşi E, Menteş O, Artik N. Food ellagitannins-occurrence, effects of processing and storage. Critical Rev in Food Sci and Nutri. 3 (2009) 283-298. [10] Ye, R., Jung, D. Y., Jun, J. Y., Li, J., Luo, S., Ko, H. J., Lee, A. S. Grp78 heterozygosity promotes adaptive unfolded protein response and attenuates diet-induced obesity and insulin resistance. Diabetes. 1 (2010) 6-16. [11] Shobana, S., Sreerama, Y. N., Malleshi, N. G. Composition and enzyme inhibitory properties of finger millet (Eleusine coracana L.) seed coat phenolic: Mode of inhibition of α-glucosidase and pancreatic amylase. Food Chem. 4 (2009) 1268-1273. [12] El-Shora, H.M., Youssef, M., Salwa, A.K. Inducers and inhibitors of laccase from Penicillium. Biotechnol. 7 (2008) 35-42. [13] El-Shora, H.M., Khalaf, S.A. Characterization of glutamine synthetase from Penicillium cyclopium. Ann of Microbiol. 55 (2002) 263-294. [14] Eaton, A. D., Clesceri,L. S., Greenberg, A. E., Standard Methods for the Examination of Water and Waste water, 20th Ed., American Public Health Association. Washington, USA. 1998. [15] Vanderzant, C., Splittstoesser D. F. Compendium of methods for the microbiological examination of food, 3rd ed. American Public Health Association, Washington, D.C.; 1992. [16] Bradford, M. M, A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochem. 72 (1976) 248-254. [17] Laemmli, U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227 (1970) 680-685. [18] El-Shora, H.M., Metwally, A.M., Salwa, A.K. Essential groups and stability of α-glucosidase of Penicillium notatum. Ann. of Microbiol.59 (2009) 285-291. [19] Marín, D., Linde, D., Lobato, M. F. Purification and biochemical characterization of an α-glucosidase from Xanthophyllomyces dendrorhous. Yeast 2 (2006) 117-125.‏ [20] Tanaka Y1, Aki T, Hidaka Y, Furuya Y, Kawamoto S, Shigeta S, Ono K, Suzuki O. Purification and characterization of a novel fungal alpha-glucosidase from Mortierella alliacea with high starch-hydrolytic activity. Biosci, Biotechnol and Biochem. 66 (2002) 2415-2423. [21] Berthelot, K1 and Delmotte FM, Purification and characterization of an alpha-glucosidase from Rhizobium sp. (Robinia pseudoacacia L.) strain USDA 4280. App Environmen Microbiol. 7 (1999) 2907-2911. [22] Carvalho AF, Boscolo M, da Silva R, Ferreira H, Gomes E, Purification and characterization of the alpha-glucosidase produced by thermophilic fungus Thermoascus aurantiacus CBMAI 756. J. of Microbiol. 4 (2010) 452-459. [23] Palmer, T. Understanding Enzymes 2nd Ed., Ellis Horwood Publisher. 1985. [24] Palmer, J. Attention in visual search: Distinguishing four causes of set- size effects. Curr Direction in Psychological Sci. 4 (1995) 118-123. [25] Lizotte, P. A., Henson, C. A. and Duke, S. H. Purification and characterization of pea epicotyl β-amylase. Plant Physiol. 92 (1990) 615-621. [26] Warangkar, S.C., Khobragade, C.N. Purification, characterization and effect of thiol compounds on activity of the Erwinia carotovora asparaginase. Enzyme Research, dio-org| 10.4061| 2010| 165878. [27] El-Shora, H. M., Abou-El-Wafa, G. S., Kadhim, A. I. Purification and biochemical characteristic of protease from the red seaweed Pterocladia capillacea. Intern. J. of Curr Microbiol of App Sci. 5 (2016) 297-308. [28] El-Shora, H. M., Rania Hegazy M. Effect of amino acids and aldehydes on tyrosinase activity from Marrow. J. of Plant Production, Man. Uni. 5 (2014) 295 – 303.


  • There are currently no refbacks.

Copyright (c) 2018 Mohamed W alfakharany

Creative Commons License
This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.

                AR Journals

Street 1st, Gaytri Vihar, Pinto Park, Gwalior, M.P. India

              Copyright@arjournals.org (Design) 2009-2021


Follow @arjournals on Twitter