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.
Prakash
Om
O
Department of Biochemistry, Banaras Hindu University, Varanasi 221005, UP, India.
Jaiswal
Nivedita
N
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