Self-adhesive PMIA membranes with virus-like silica immobilized lipase for efficient biological aging of Chinese liquor

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.

Automated summary

The novel CALB@VLS/PMIA membranes exhibited excellent separation and biocatalysis performance, with enhanced efficiency in catalyzing the synthesis of esters. The membranes have great potential for broad applications in various fields due to their superior catalytic capabilities.