Avdiyuk K V, Varbanets L D
Mikrobiol Z. 2015 Jul-Aug;77(4):15-24.
The effect of cations and anions on the activity of Aspergillus flavus var. oryzae and Bacillus subtilis α-amylases showed that the tested enzymes are sensitive to most of cations and resistant to anions. The most significant inhibitory effects on the activity of A. flavus var. oryzae α-amylase have been demonstrated by Al3+ and Fe3+ ions, while on the activity of B. subtilis α-amylase - Hg2+, Cu2+ and Fe3+ ions. Inactivation of A. flavus var. oryzae and B. subtilis α-amylases in the presence of EGTA is indicated on the presence within their structure of metal ions. An important role in the enzymatic catalysis of both enzymes play carboxyl groups as evidenced by their inhibition of 1-[3-(dimethylamino)propyl]-3-ethylcarbodiimide methiodide. Inhibition of B. subtilis α-amylase by p-chloromercuribenzoate, N-ethylmaleimide and sodium sulfite is indicated on the probable involvement of the sulfhydryl groups in the functioning of the enzyme. Unlike most studied glycosidases the tested enzymes do not contain histidine imidazole group in the active center.
阳离子和阴离子对米曲霉和枯草芽孢杆菌α-淀粉酶活性的影响表明，所测试的酶对大多数阳离子敏感，对阴离子具有抗性。Al3+和Fe3+离子对米曲霉α-淀粉酶的活性具有最显著的抑制作用，而Hg2+、Cu2+和Fe3+离子对枯草芽孢杆菌α-淀粉酶的活性有抑制作用。在EGTA存在的情况下，米曲霉和枯草芽孢杆菌α-淀粉酶的失活表明其结构中存在金属离子。1-[3-(二甲基氨基)丙基]-3-乙基碳二亚胺甲基碘对两种酶的抑制作用证明了羧基在酶催化中起重要作用。对氯汞苯甲酸、N-乙基马来酰亚胺和亚硫酸钠对枯草芽孢杆菌α-淀粉酶的抑制作用表明巯基可能参与了该酶的功能。与大多数已研究的糖苷酶不同，所测试的酶在活性中心不含组氨酸咪唑基团。
