LAUSR

Abstract Excellent separation and biocatalysis performance of novel CALB@virus-like silica/Poly (m-phthaloyl-m-phenylenediamine) (CALB@VLS/PMIA) membranes were fabricated by the self-adhesion method via introducing the immobilized biological enzyme (CALB@VLS) on the surface of PMIA membrane, in which the interconnection of CALB@VLS and PMIA was able to improve the ability of one-step refining Chinese liquor and catalytic synthesis of aromatic esters. The outcomes stated clearly that the increment of dosage of CALB@VLS and ratio of ethanol/water coagulation bath led a raise of the lipase loading on the surfaces of membrane yet overdose caused an abatement in the lipase activity. With the optimal conditions of 0.5 g L−1 dosage and 60 %v/v ratio, the CALB@VLS decorated PMIA membrane achieved the supreme lipase relative activity at 95.3% of its initial activity. Meanwhile, the rejection rate of turbid advanced fatty acid ethyl esters attached the highest 92.5% under satisfactory liquor flux (432.5 L m−2 h−1). The pH, thermal, organic solvent and storage stability of the lipase immobilized on the membrane were markedly enhanced. The effect of CALB@VLS dosage, liquor concentration and operating temperature on the efficiency of catalytic esterification was explored. Additionally, the immobilized lipase on the membrane could be readily maintained at 75.7% after repeated use ten times. Consequently, the PMIA membrane promised to be an excellent carrier for lipase, and the bioactive membrane could have broad applications in food, medicine, etc.