Formation of lipase Candida sp. 99–125 CLEAs in mesoporous silica: characterization and catalytic properties

Abstract

Mesoporous silica (MPS) was synthesized and used as a support for lipase Candida sp. 99–125 immobilization. The immobilization procedure was simple and effective: lipase Candida sp. 99–125 was first immobilized in the MPS by adsorption (named ADL@MPS), then chemical crosslinking was conducted for stabilizing the lipase and inhibiting leakage, and cross-linked enzyme aggregates (CLEAs) of Candida sp. 99–125 lipase in the MPS were obtained (named CLL@MPS). The stability of ADL@MPS and CLL@MPS was investigated. Compared with ADL@MPS and native lipase, CLL@MPS showed outstanding stability under vigorous shaking conditions and the thermal stability of CLL@MPS in the presence of organic solvents was also improved. Additionally, CLL@MPS exhibited high catalytic performance in hydrolysis, esterification, and transesterification reactions with increased stability and recyclability.