摘要
通过X射线粉末衍射、红外光谱等手段考察了α 磷酸锆层柱材料作为载体固定青霉素酰化酶及其对载体结构影响。结果表明无论是否加入戊二醛固定化酶后 ,层柱材料的结晶度都下降。酶活性和回收率较高 ,分别为139 5nmol/s和 2 8 9%。间歇操作稳定性较好 ,连续操作 10次 ,酶活性下降 2 4%
Penicillin acylase immobilized on triethylaminetetramine intercalacated α ZrP was prepared and characterized by the techniques of X ray powder diffraction and infrared spectrophotometry.Immobilization of the enzyme led to a decrease in crystallinity of the host solid whether there was glutaraldehyde. The activity of the immobilized enzyme was 139 5 nmol/s, and decreased by only 24% after reusing 10 times.
出处
《北京化工大学学报(自然科学版)》
CAS
CSCD
2002年第1期64-67,共4页
Journal of Beijing University of Chemical Technology(Natural Science Edition)
基金
国家自然科学基金资助项目 (2 99730 0 4)
北京市自然科学基金资助项目 (5 82 0 14)