Konecny J, Voser W
Biochim Biophys Acta. 1977 Dec 8;485(2):367-78. doi: 10.1016/0005-2744(77)90172-3.
A very stable esterase (EC 3.1.1.-), which hydrolyses ethyl acetate, cephalosporin C and other acetyl esters with a maximum turnover number of 3-10(2) s-1, was isolated from Bacillus subtilis ATCC 6633 and immobilized on two supports: controlled-pore glass and powdered brick, a representative of carriers having a wide pore-size distribution. Carrier morphology determines diffusion rates and the expression of activity. Rate-limiting mass transfer of buffer leads to apparent losses of activity, gross distortions of molecular pH vs. activity profiles and to apparent deviations from Michaelis-Menten kinetics.
从枯草芽孢杆菌ATCC 6633中分离出一种非常稳定的酯酶（EC 3.1.1.-），它能水解乙酸乙酯、头孢菌素C和其他乙酰酯，最大周转数为3 - 10(2) s-1，并固定在两种载体上：可控孔径玻璃和粉末砖，后者是具有宽孔径分布载体的代表。载体形态决定扩散速率和活性表达。缓冲液的限速传质导致活性明显损失、分子pH与活性曲线严重扭曲以及与米氏动力学明显偏离。
