Buonocore V, Poerio E, Silano V, Tomasi M
Biochem J. 1976 Mar 1;153(3):621-5. doi: 10.1042/bj1530621.
The amylase from Tenebrio molitor L. larvae (yellow mealworm) was characterized according to a number of its molecular and catalytic properties. The insect amylase is a single polypeptide chain with mol.wt. 68000, an isoelectric point of 4.0 and a very low content of sulphur-containing amino acids. The enzyme is a Ca2+-protein and behaves as an alpha-amylase. Removal of Ca2+ by exhaustive dialysis against water causes the irreversible inactivation of the enzyme. Moreover, the enzyme is activated by the presence in the assay mixture of Cl-, or some other inorganic anions that are less effective than Cl-, and is inhibited by F-. Optimal conditions of pH and temperature for the enzymic activity are 5.8 and 37 degrees C. The insect amylase exhibits an identical kinetic behaviour toward starch, amylose and amylopectin; the enzyme hydrolyses glycogen with a higher affinity constant. Compared with the non-insect alpha-amylases described in the literature, Tenebrio molitor amylase has a lower affinity for starch.
对黄粉虫（Tenebrio molitor L.）幼虫的淀粉酶的一些分子和催化特性进行了表征。昆虫淀粉酶是一条单多肽链，分子量为68000，等电点为4.0，含硫氨基酸含量极低。该酶是一种钙蛋白，表现为α-淀粉酶。通过用水进行彻底透析去除Ca2+会导致酶不可逆失活。此外，在测定混合物中存在Cl-或一些比Cl-效果稍差的其他无机阴离子时，该酶会被激活，而F-会抑制它。酶活性的最佳pH和温度条件分别为5.8和37℃。昆虫淀粉酶对淀粉、直链淀粉和支链淀粉表现出相同的动力学行为；该酶以更高的亲和常数水解糖原。与文献中描述的非昆虫α-淀粉酶相比，黄粉虫淀粉酶对淀粉的亲和力较低。
