PHYSICAL AND CATALYTIC PROPERTIES OF ALPHA-AMYLASE FROM TENEBRIO-MOLITOR-L LARVAE
PHYSICAL AND CATALYTIC PROPERTIES OF ALPHA-AMYLASE FROM TENEBRIO-MOLITOR-L LARVAE
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DOI：
10.1042/bj1530621
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发表时间：
1976-01-01
影响因子：
4.1
通讯作者：
TOMASI, M
中科院分区：
文献类型：
--
作者：
BUONOCORE, V;POERIO, E;TOMASI, M
T.根据许多分子和催化性质来表征黄粉虫幼虫（黄粉虫）。Ir是一种单链多肽，分子量为68，000，等电点为4.0，含硫氨基酸含量极低。该酶是一种Ca 2+蛋白，其行为与x-淀粉酶类似[EC 3.2.1.1]。通过对水的彻底透析去除Ca 2+导致酶的不可逆失活。该酶被Cl-或其他一些无机阴离子激活，而F-则被抑制。该酶的最适pH和温度分别为5、8和37 ℃。C.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;该酶以较高的亲和常数水解糖原。与文献报道的非昆虫α-淀粉酶相比，T.黄粉虫淀粉酶对淀粉的亲和力较低。
The amylase from T. molitor larvae (yellow mealworm) was characterized according to a number of molecular and catalytic properties. Ir is a single polypeptide chain with a molecular weight of 68,000, an isoelectric point of 4.0 and a very low content of S-containing amino acids. The enzyme is a Ca2+-protein and behaves as an x-amylase [EC 3.2.1.1]. Removal of Ca2+ by exhaustive dialysis against water causes the irreversible inactivation of the enzyme. 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.degree. C. The insect amylase exhibits an identical kinetic behavior toward starch, amylose and amylopectin; the enzyme hydrolyzes glycogen with a higher affinity constant. Compared with non-insect a-amylases described in the literature, T. molitor amylase has a lower affinity for starch.