Boccù E, Gianferrara T, Gardossi L, Veronese F M
Dipartimento di Scienze Farmaceutiche, Università di Trieste.
Farmaco. 1990 Feb;45(2):203-14.
Penicillin acylase (EC 3.5.1.11) from E. coli, both in solution and immobilized on solid supports, has been commercially exploited for the large scale production of 6-aminopenicillanic acid (6-APA), which is an important intermediate for the manufacturing of semisynthetic penicillins. In this paper a very simple procedure of penicillin acylase purification is reported, which employs only one affinity chromatographic step (Sepharose-phenylacetic column). The enzyme was obtained at a high degree of purity and could be used for immobilization on partially hydrolyzed and activated nylon. Since the support is chemically inert and mechanically stable the catalyst can be used several times without any significant loss of activity, making the process of great commercial importance.
来自大肠杆菌的青霉素酰化酶（EC 3.5.1.11），无论是在溶液中还是固定在固体载体上，都已被商业应用于大规模生产6-氨基青霉烷酸（6-APA），6-APA是制造半合成青霉素的重要中间体。本文报道了一种非常简单的青霉素酰化酶纯化方法，该方法仅采用一步亲和色谱法（琼脂糖-苯乙酸柱）。所获得的酶具有高度的纯度，可用于固定在部分水解和活化的尼龙上。由于载体化学惰性且机械稳定，催化剂可多次使用而活性无明显损失，这使得该工艺具有重大的商业价值。
