A highly efficient and thermostable alpha-amylase from soya bean seeds

作者：Prakash Om; Jaiswal Nivedita^*

来源：Biotechnology and Applied Biochemistry, 2010, 57: 105-110.

DOI：10.1042/BA20100262

• affinity precipitation
• metal ion
• starch
• thermostability

The alpha-amylase from soya bean seeds was purified by affinity precipitation, resulting in approx. 20-fold purification with approx. 84% recovery. The purified a-amylase had an optimum pH of 5.5, optimum temperature of 75 degrees C, Arrhenius energy of activation of 6.03 kcal/mol (1 kcal approximate to 4.184 kJ) and a K(m) of 2.427 mg/ml (starch substrate). The enzyme had maximum substrate specificity for starch. Among the various metal ion!, tested, Co(2+) and Mn(2+) were found to be strong activators. The effect of thiol group modifying agents showed that the thiols of soya bean alpha-amylase are not directly involved in catalysis. The thermostability of the enzyme makes it suitable for starch liquefaction and the detergent industry respectively.

• 出版日期2010-11