10.22376/ijpbs.2019.10.1.p1-12 Volume 8 Issue 2 2017 (April - June) The present study was conducted to screen the proteinaceous α-amylase inhibitory activity of lessThan i greaterThan Bacillus pumilus lessThan /i greaterThan NGP-1. The culture free supernatant was precipitated by ammonium sulfate at 10-80% saturation for overnight at 4ºC. The precipitated proteins were desalted by dialysis and the protein content was estimated to be 1.3 mg/ml. The α-amylase inhibitory activity of partially purified proteinaceous α-amylase inhibitor was found to be 56%. The proteinaceous α-amylase inhibitor was characterized by Analytical High Performance Liquid Chromatography. The molecular weight of the α-amylase inhibitor was determined by Sodium Dodecyl Sulphate Polyacrylamide Gel Electrophoresis as 29kDa. The results suggested that the proteinaceous α-amylase inhibitor from lessThan i greaterThan Bacillus pumilus lessThan /i greaterThan NGP-1 lessThan i greaterThan lessThan /i greaterThan is first of its kind and may be an important candidate in research of diabetes. SHANMUGARAJU VEERAMUTHU, SURAYYA MOHAMMED AND BIVYA GOPALAN Post prandial hyperglycemia, α-amylase inhibitor, Diabetes mellitus, Starch blockers,Porcine pancreatic α-amylase. 691-695