%0 Journal Article
%T STUDIES ON THE IMMOBILIZED PENICILLIN ACYLASE ON POLYMER BEADS<br>颗粒状固定化青霉素酰化酶的研究
%A Han Hui
%A Xu Guanzhu
%A <br>韩辉
%A 徐冠珠
%J 微生物学报
%D 2001
%I 
%X The extracellular penicillin acylase from Bacillus megaterium was immobilized on oxirane group of Eupergit C beads. The apparent activity of the immobilized enzyme was about 1400 u.g-1 (dry weight). The optimal pH and temperature were 8.0 and 55 degrees C for hydrolytic reaction of penicillin G, respectively. The immobilized enzyme was stable in the pH range of 6.0-8.5 and at temperature below 45 degrees C. The apparent Michaelis constant for penicillin G was inhibition constant of phenylacetic acid as competitive 2 x 10(-2) mol.L-1 and Vm was 1.33 mmol.g-1 min-1 (dry weight) at 37 degrees C and PH8.0. The inhibitor and 6-APA as non-competitive inhibitor were 2.8 x 10(-2) mol.L-1 and 0.125 mol.L-1 for the immobilized enzyme at pH 8.0 and 37 degrees C, respectively. The remained activity of the immobilized enzyme was about 80% after operating 200 times for hydrolysis of penicillin G to 6-APA, and the average yield of 6-APA was 89.48%.
%K Bacillus megaterium
%K Immobilized penicillin acylase
%K Oxirane
%K Eupergit C<br>巨大芽孢杆菌
%K 固定化青霉素酰化酶
%K 环氧基
%K Eupergit
%K C
%U http://www.alljournals.cn/get_abstract_url.aspx?pcid=90BA3D13E7F3BC869AC96FB3DA594E3FE34FBF7B8BC0E591&jid=A3C6BA55AB623B90FA9104CFFC826F3C&aid=35A7F1A7B56D913B&yid=14E7EF987E4155E6&vid=2001E0D53B7B80EC&iid=0B39A22176CE99FB&sid=02DC3A182A5530DF&eid=3D9746C06EC12B45&journal_id=0001-6209&journal_name=微生物学报&referenced_num=9&reference_num=8