A highly efficient and thermostable α-amylase from soya bean seeds.
The α-amylase from soya bean seeds was purified by affinity precipitation, resulting in approx. 20-fold purification with approx. 84% recovery. The purified α-amylase had an optimum pH of 5.5, optimum temperature of 75 °C, Arrhenius energy of activation of 6.03 kcal/mol (1 kcal≈4.184 kJ) and a Km of 2.427 mg/ml (starch substrate). The enzyme had maximum substrate specificity for starch. Among the various metal ions tested, Co2+ and Mn2+ were found to be strong activators. The effect of thiol group modifying agents showed that the thiols of soya bean α-amylase are not directly involved in catalysis. The thermostability of the enzyme makes it suitable for starch liquefaction and the detergent industry respectively.
Department of Biochemistry, Banaras Hindu University, Varanasi 221005, UP, India.
Om
O
Prakash
Nivedita
N
Jaiswal
D004795:Enzyme Stability; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D008670:Metals / Q000378:metabolism; D012639:Seeds / Q000737:chemistry / Q000201:enzymology*; D013025:Glycine max / Q000737:chemistry / Q000201:enzymology*; D013213:Starch / Q000378:metabolism; D013379:Substrate Specificity; D000516:alpha-Amylases / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism
D008670:Metals; D013213:Starch; D000516:alpha-Amylases