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Saptadip Samanta1, Malabendu Jana2, Sanjay Kar3,Saswati Parua4, Pradeep Kumar Das Mohapatra5,Bikash Ranjan Pati5, Keshab Chandra Mondal5
1 Department of Physiology, Midnapore College, Midnapore, Paschim Medinipur 721101, West Bengal, India._2 Department of Neurological Sciences, Rush University Medical Center, Chicago, IL 60612,USA_3 Department of Botany, Midnapore College, Midnapore, Paschim Medinipur 721101, WestBengal, India._4 Department of Physiology, Bajkul Milani Mahavidyalaya, Bajkul, Purba Medinipur, West Bengal, India._5 Department of Microbiology, Vidyasagar University, Midnapore, 721102, West Bengal, India.
Ind.J.Applied.Microbiol. 2017 .20(2) : 55-71
An extracellular amylase was purified upto homogeneity from the culture broth of Bacillus licheniformis SKB4 by a combination of 80% (NH4)2SO4 precipitation, DEAE cellulose column chromatography, and sephadex G-100 gel filtration technique. The purified ï¡-amylase exhibited specific activity of 827 U/mg with 64.8% yield having a molecular weight of 60 kDa and retained 80% of its original activity in the presence of 5 M NaCl solution. Starch is the best substrate (100%) for enzymatic digestion followed by amylopectin, potato starch, corn starch, amylose and glycogen. The non-inhibitory effect of β-specific inhibitor p-chloromercuro benzoate and iodoacetamide (10 mm), rapid blue loss percentage of starch-iodine complex and formation of α-anomeric products of starch hydrolysis indicated that the purified enzyme was an endoattacking ï¡-amylase. This enzyme hydrolyzes starch to maltooligosaccharides like materials maltotriose (G3), maltotetrose (G4), maltopentose (G5) at an early stage of the reaction which were further hydrolyzed to maltose. This salt-tolerant and maltooligomer producing ï¡-amylase has commercial value, especially in the food industry.
Keywords: Purification, amylase, maltooligosaccharide, Bacillus licheniformis SKB4
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