摘要
天然的苯丙氨酸解氨酶(phenylalanine ammonialyase,PAL)存在稳定性差、可操作性低等问题,限制了其在医药、食品和生物化工领域的应用.为了提高PAL的催化性能,本研究将PAL吸附固定在金属有机骨架UiO-66-NH_(2)载体上,制备出PAL@UiO-66-NH_(2)固定化酶颗粒.通过优化固定化酶颗粒的制备条件,PAL@UiO-66-NH_(2)最大酶活回收率达到(90.01±3.18)%,比优化前提高了约35%;并对其pH耐受性、温度耐受性和重复使用性等催化性能进行研究.结果表明:PAL@UiO-66-NH_(2)对pH和温度的耐受性优于游离PAL;在重复使用5次后,PAL@UiO-66-NH_(2)仍能保持初始酶活力的80%左右,表现出较好的重复使用性.本研究结果可为PAL的工业化应用提供参考.
Natural phenylalanine ammonialyase(PAL)has the problems of poor stability and low operability,which has limited its applications in the fields of medicine,food and biochemical industry.In order to improve the catalytic performance of PAL,in this study PAL was immobilized on the metal-organic framework UiO-66-NH_(2) carrier by adsorption method to prepare PAL@UiO-66-NH_(2) immobilized enzyme particles.By optimizing the preparation conditions of the immobilized enzyme particles,the maximum activity recovery rate of prepared PAL@UiO-66-NH_(2) particles reached(90.01±3.18)%,about 35%higher than that before optimization;the catalytic performances of PAL@UiO-66-NH_(2),such as pH tolerance,temperature tolerance and reusability were also studied.The results showed that the stability of PAL@UiO-66-NH_(2) particles was better than that of free PAL;after repeated use for 5 times,PAL@UiO-66-NH_(2) maintained about 80%of the initial enzyme activity,indicating better stability of reusability.Therefore,this study can provide a reference for the industrial application of PAL.
作者
孙宝婷
崔建东
贾士儒
SUN Baoting;CUI Jiandong;JIA Shiru(College of Biotechnology,State Key Laboratory of Food Nutrition and Safety,Tianjin University of Science&Technology,Tianjin 300457,China)
出处
《天津科技大学学报》
CAS
2022年第4期9-15,22,共8页
Journal of Tianjin University of Science & Technology
基金
国家自然科学基金项目(21676069)
天津市自然科学基金重点项目(19JCZDJC38100)。
