Abstract
Starch phosphorhylase extracted from mature potato tubers (Solanum tuberosum L. var. Kufri Badshah) was partially purified and immobilized on brick dust as solid support via glutaraldehyde. The percentage retention of the enzyme activity on brick dust was nearly 80 %. After immobilization specific activity of the enzyme increased from 0.92 to 3.25 U mg−1 protein with about 3.5-fold enrichment. The optimum pH and temperature of soluble enzyme were determined as pH 6.0 and 37 °C, respectively whereas immobilized enzyme showed at pH 6.5 and 47 °C, respectively. The immobilized enzyme displayed higher thermal stability than soluble enzyme and retained about 50 % of its initial activity after 10 reuses. Immobilized enzyme was packed in an indigenously designed double walled glass bed reactor for continuous production of glucose-1-phosphate.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
References
Mukerjea R, Falconer DJ, Yoon S-H, Robyt JF (2010) Large-scale isolation, fractionation, and purification of soluble starch-synthesizing enzymes: starch synthase and branching enzyme from potato tubers. Carbohyd Res 345:1555–1563
Rathore RS, Garg N, Garg S, Kumar A (2009) Starch phosphorylase: role in starch metabolism and biotechnological applications. Crit Rev Biotech 29:214–224
Weinhausel A, Nidetzky B, Rohrbach M, Blauensteiner B, Kulbe KD (1994) A new maltodextrin phosphorylase from Corynebacterium callunae for the production of glucose-1-phosphate. Appl Microbiol Biotechnol 1:510–516
Zhang Y-HP, Mielenz J (2007) Biohydrogen production by an artificial enzymatic pathway. US Patent Application 20070264534, 11 May 2007
Kawchuk LM, Armstrong JD, Lynch DR, Knowles NR (1999) Potatoes having improved quality characteristics and methods for their production. US Patent 5: 998–701, 7 Dec 1999
Venkaiah B, Kumar A (1994) Egg shell bound starch phosphorylase packed bed reactor for the continuous production of glucose-1-phosphate. J Biotechnol 36:11–17
Venkaiah B, Kumar A (1995) A process for the recovery and immobilization of starch phosphorylase from starch-based industrial wastewater. Biotechnol Appl Biochem 21:77–85
Kumar A, Sanwal GG (1981) Immobilization of starch phosphorylase from mature banana leaves. Indian J Biochem Biophys 18:114–119
Srivastava S, Nighojkar A, Kumar A (1996) Immobilization of Cuscuta reflexa starch phosphorylase: production of glucose-1-phosphate using bioreactors. J Ferment Bioeng 81:355–357
Upadhye SP, Kumar A (1996) Immobilization of starch phosphorylase from Bengal gram seeds: production of glucose-1-phosphate. Genet Eng Biotechnol 16:145–151
Garg S, Kumar A (2007) Immobilization of starch phosphorylase from seeds of Indian millet (Pennisetum typhoides) variety KB560. Afr J Biotech 6:2715–2720
Garg N, Kumar A (2008) Immobilization of starch phosphorylase from cabbage leaves: production of glucose-1-phosphate. Braz J Chem Eng 25:1–7
Fiske CH, Subbarow Y (1925) The colorimetric determination of phosphorus. J Biol Chem 66:375–400
Lowry OH, Rosebrough NJ, Farr AL, Randall RJ (1951) Protein measurement with folin phenol reagent. J Biol Chem 193:265–275
Gupta SM, Gupta S, Kumar A (2009) Development of bed reactor using brick dust immobilized CM-cellulase from seeds of cowpea (Vigna sinensis L.). J Plant Biochem Biotech 18:113–116
Bergmeyer HU, Klotzsch H (1965) d-Glucose-1-phosphate, methods of enzymatic analysis. Academic Press, New York, pp 131–133
Acknowledgments
The present work was supported by the grants from the Department of Biotechnology (DBT), New Delhi. SG acknowledges award of Senior Research Fellowship provided by Council of Scientific & Industrial Research (CSIR), New Delhi.
Author information
Authors and Affiliations
Corresponding author
Rights and permissions
About this article
Cite this article
Gupta, S., Gupta, S.M. & Kumar, A. Preparation of Bed Reactor Using Brick Dust Immobilized Starch Phosphorhylase from Potato Tubers (Solanum tuberosum L. var. Kufri Badshah) for Production of Glucose-1-phosphate. Natl. Acad. Sci. Lett. 36, 133–137 (2013). https://doi.org/10.1007/s40009-013-0117-3
Received:
Revised:
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1007/s40009-013-0117-3