国产日产欧美精品-亚洲国产综合久久精品-色综合色国产热无码一-亚洲欧美日本国产,免费观看一区二区三区_在线观看片A免费不卡观看_亚洲а∨天堂久久精品_99久无码中文字幕一本久道

 

作者： Mengfan Wang, Chenxi Jia, Wei Qi, , Qingxin Yu, Xin Peng, Rongxin Su, Zhimin He

State Key Laboratory of Chemical Engineering, Chemical Engineering Research Center, School of Chemical Engineering and Technology, Tianjin University, Tianjin 300072, PR China

 

摘要：Porous cross-linked enzyme aggregates (p-CLEAs) were prepared by adding starch as a pore-making agent, which facilitates CLEAs in cases where the substrates of enzyme are macromolecules. This novel strategy for preparation of p-CLEAs involves co-precipitation, cross-linking and removal of starch by α-amylase. The resulting papain p-CLEAs were characterized by scanning electron microscope (SEM) images, showing a porous structure. The 95.9% and 90.4% increased catalytic efficiencies of p-CLEAs than conventional CLEAs on bovine serum albumin (BSA) and ovalbumin verified the feasibility of this protocol.

 

關(guān)鍵詞： Enzymatic hydrolysis; Enzyme immobilization; Macromolecule; Papain; Porous cross-linked enzyme aggregates