Immobilization of α-Amylase by Pseudomonas sp isolated from Indian Chicken

ABSTRACT Control of α-Amylase formed by a Pseudomonas sp isolated from Indian Chicken feather was deliberate. Partly cleansed enzyme with 486.77 IU and specific activity of 811.28 units mg (protein) was used for immobilization study. An easily obtainable and cheap 3% Sodium alginate matrix with easy control gel entrapment procedure was used for tricking the enzyme showed 555.5 IU activity. The optimization was carried out to study the catalytic properties which showed the optimum pH, temperature and substrate concentration at pH 7, 450C and 16mg, respectively. The reusability of the arrested enzyme preparation presented its use in incessant starch hydrolysis for up to 10 cycles. This immobilized enzyme can be used as a standby of profitable enzyme since it has shown same greater operational flexibility and enzymatic activity of the pure enzyme. Keywords: Immobilization, Calcium alginate, Immobilization, Pseudomonas sp. REFERENCES Om Prakash and Nivedita Jaiswal. Immobilization of a Thermostable - Amylase on Agarose and Agar Matrices and its Application in Starch Stain Removal. World Applied Sciences Journal, 13 (3), 572-577, (2011). Devendra kumar, Muthukumar M. and Neelima Garg. Kinetics of fungal extracellular α-amylase from Fusarium solani immobilized in calcium alginate beads. J. Environ. Biol., 33, 1021-1025, (2012). Sachin Talekar and Sandeep Chavare. Optimization of immobilization of α- amylase in alginate gel and its comparative biochemical studies with free α-amylase. Recent Research in Science and Technology, 4(2), 01-05, (2012). Talekar S., Ghodake V., Kate A., Samant N., Kumar C. and Gadagkar S. Preparation and characterization of crosslinked enzyme aggregates of Saccharomyces cerevisiae invertase. Aust. J. Basic Appl. Sci., 4, 4760-4765, (2010). Dey G., Singh B. and Banerjee R. Immobilization of α- amylaseProduced by Bacillus circulans GRS 313. Braz. Arch. Biol.Techn., 46(2), 167-176, (2003) Porika Raju and Estari Mamidala (2015). Anti-diabetic activity of compound isolated from Physalis angulata fruit extracts in alloxan induced diabetic rats. The Ame J Sci & Med Res, 2015,1(1); Pages 1 -6. doi:10.17812/ajsmr2015.11.1 Elif demirkan, Serhan dincbas, Nihan sevinc and Figen ertan. Immobilization of B. amyloliquefaciens α-amylase and comparison of some of its enzymatic properties with the free form. Romanian Biotechnological Letters, 16(6), (2011). Bucke C. Cell immobilization in calcium alginate. Methods Enzymol, 135,175- 189, (1987). Vandana Singh and Devendra Singh. Diastase α-amylase immobilization on sol-gel derived guar gum-gelatin-silica monohybrid. Adv. Mat. Lett., 5(1), 17-23, (2014). Lily N. Meyer. Effect of Immobilization Method on Activity of Alpha-Amylase. Published PhD thesis, The Ohio State University, (2007). http://hdl.handle.net/1811/25118. Khardenavis A. A., Kapley A., and Purohit H. J. Processing of poultry feathers by alkaline keratin hydrolysing enzyme from Serratia sp. HPC 1383. Waste Managemen, 29(4), 1409–1415, (2009). Venkatesh Chaturvedi and Pradeep Verma. Metabolism of Chicken Feathers and Concomitant Electricity Generation by Pseudomonas aeruginosa by Employing Microbial Fuel Cell (MFC). Journal of Waste Management, 2014, 1- 9, (2014). Menandro N. Acda. Sustainable Use of Waste Chicken Feather for Durable and Low Cost Building Materials in the Tropics Nova publishers, New York, 353- 366, (2011). Janhavi S., Shobha G., Pallavi P., Manya K., Amrutha V and Ananda S. Biological transesterification of poultry waste to biodiesel using bacteria isolated from chicken feather. International Journal of Recent Scientific Research Research, 5(9), 1729-1732, (2014). Bergey D. H. and Holt, J. G. Bergey's Manual of Determinative Bacteriology, 9th edition, Baltimore: Williams & Wilkins, USA, 93-94, (1994). Basabrani Devi, Unni B. G., Wann S.B. and Samanta R. Immobilization of partially purified alpha-amylase enzyme produced by a soil born Bacillus sp. Advances in Applied Science Research, 3(5), 2739-2744, (2012). Lowry O. H, Rosenbrough N. J and Randall A.L.F. J.Biol.Chem.,193, 265 - 275, (1951). Kumar R.S.S, Vishwanath R.K.S, Singh S.A and Appu Rao A.G.. Entrapment of α-amylase in alginate in beads: Single step protocol for purification and thermal stabilization. Process Biochem., 41, 2282- 2288 (2006). Mahajan R., Gupta V. K and Sharma J. Comparison and Suitability of Gel Matrix for Entrapping Higher Content of Enzymes for Commercial Applications. Indian J Pharm Sci., 72(2): 223–228, (2010). Williamson DA, Heffernan H, Sidjabat H, Roberts SA, Paterson DL, Smith M, 2008.: Impact of antibiotic resistance in gram-negative bacilli on empirical and definitive antibiotic therapy. Clin Infect Dis 1, 14–20