Enhanced Performance of Rhizopus oryzae Lipase by Reasonable Immobilization on Magnetic Nanoparticles and Its Application in Synthesis 1,3-Diacyglycerol.

Nano-sized FeO was synthesized by chemical co-precipitation and subsequently modified with 3-aminopropyltriethoxysilane (APTES) and glutaraldehyde to introduce aldehyde group on its surface. With the help of "interface activation" by adding sucrose esters-11 as surfactant, lipase from Rhizopus oryzae was successfully immobilized onto the carrier with great enhancement of activity. The hydrolysis activity of immobilized enzyme were 9.

Enhancing the thermostability of lipase by combined mutation of hot-spots and engineering a disulfide bond.

lipase (ROL) is important because of its extreme -1,3-regioselectivity, but it shows poor thermostability, which severely restricts its application. In this work, the thermostability of ROL was greatly enhanced by rational design. First, several sites that may affect the thermostability of ROL were identified by multiple-sequence alignment.

Design, identification, antifungal evaluation and molecular modeling of chlorotetaine derivatives as new anti-fungal agents.

It is feasible to rationally modify existing bioactive components for new drug development, achieving molecules with improved biological activities. In this study, rational modification of chlorotetaine was carried out following molecular modelling to enhance interactions between the fungal oligopeptide transmembrane transporter PTR22 and the ligand. The peptide obtained with the lowest docking energy, Lys-chlorotetaine (LC), displayed an improved antifungal effect compared with chlorotetaine.