Cantarella M, Gianfreda L, Palescandolo R, Scardi V
Biochem J. 1977 Oct 1;167(1):313-5. doi: 10.1042/bj1670313.
Yeast invertase was co-reticulated with glutaraldehyde to bovine serum albumin to give a soluble bound enzyme that was immobilized as a tightly adhering layer on the active surface of an ultrafiltration membrane. The Michaelis constant and stability of this immobilized-enzyme system are compared with those of the enzyme either in the native form or immobilized as a dynamically formed gel layer on an ultrafiltration membrane, as previously described by us [Drioli, Gianfreda, Palescandolo & Scardi (1975) Biotechnol, Bioeng, 17, 1365-1367].
酵母转化酶与戊二醛共同交联到牛血清白蛋白上,形成一种可溶性结合酶,该酶以紧密附着层的形式固定在超滤膜的活性表面。将这种固定化酶系统的米氏常数和稳定性与天然形式的酶或如我们之前所述[Drioli, Gianfreda, Palescandolo & Scardi (1975) Biotechnol, Bioeng, 17, 1365 - 1367]在超滤膜上以动态形成的凝胶层形式固定的酶的米氏常数和稳定性进行了比较。