Effect of dry fractionation of peanut oil-based diacylglycerols on crystallization properties, oxidative stability and safety.

This research employed environmentally friendly dry fractionation to systematically modify the physicochemical properties of 80 % diacylglycerol derived from peanut oil (PDAG-80), expanding its potential food applications. The properties of olein and stearin were optimized by adjusting key parameters: crystallization temperatures (11, 13, 15 and 17 °C), cooling rates (2, 5, 8 and 11 °C/h), agitation speeds (10, 20, 30 and 40 rpm)and residence times (3, 6, 9 and 12 h). Lowering the crystallization temperature and extending the residence time increased the iodine value and solid fat content of olein.

Changes in stability, phytonutrients, 3-chloropropanol esters and glycidyl esters of peanut oil-based diacylglycerols during heat treatment.

Diacylglycerol (DAG) is generally considered one of the precursors of 3-chloropropanol esters (3-MCPDE) and glycidyl esters (GEs). This study aimed to evaluate static heating and stir-frying properties of peanut oil (PO) and PO based 58% and 82% DAG oils (PDAG-58 and PDAG-82). Observations revealed that, phytonutrient levels notably diminished during static heating, with PDAG exhibiting reduced oxidative stability, but maintaining a stability profile similar to PO over a short period.

Atomevo: a web server combining protein modelling, docking, molecular dynamic simulation and MMPBSA analysis of Candida antarctica lipase B (CalB) fusion protein.

Although current computational biology software is available and has prompted the development of enzyme-substrates simulation, they are difficult to install and inconvenient to use. This makes the time-consuming and error-prone process. By far there is still a lack of a complete tool which can provide a one-stop service for the enzyme-substrates simulation process.

Molecular Dynamic Simulation of the Porcine Pancreatic Lipase in Non-aqueous Organic Solvents.

This paper investigates the conformational stability of porcine pancreatic lipase (PPL) in three non-aqueous organic solvents, including dimethyl sulfoxide (DMSO), propylene glycol (PRG), and ethanol (EtOH) through molecular dynamic (MD) simulation. The root mean square deviations (RMSDs), radius of gyration (Rg), solution accessible surface area (SASA), radial distribution function (RDF), hydrogen bond (H-bond), Ramachandran plot analysis, secondary structure, and enzyme substrate affinity of the PPL in the various organic solvents were comparatively investigated. The results showed that the backbone and active pocket RMSD, and hydrophilic ASA of PPL in three solvents increase with the increase in the solvent LogP, while the Rg, hydrophobic ASA, and H-bond between the solvent and PPL decrease.