3D printed personalized wound dressings using a hydrophobic deep eutectic solvent (HDES)-formulated emulgel.

Curcuminoids, known for their antibacterial, anti-inflammatory, and wound healing properties, face challenges in medical applications due to their limited water solubility, resulting in poor bioavailability and clinical efficacy. This study introduces a novel approach to formulating 3D printing ink for personalized wound dressings by utilizing hydrophobic deep eutectic solvents (HDES) to incorporate poorly water-soluble compounds from (, curcuminoids and ar-turmerone) into hydrogels. The use of HDES, comprising either acetic acid or octanoic acid combined with menthol in a 2 : 1 molar ratio, significantly improved the solubility of curcuminoid derivatives and ar-turmerone by approximately 10 to 600 times, depending on the intrinsic chemical polarities of each compound, compared to conventional extraction solvents (, ethanol and water).

Effects of Signal Peptide and Chaperone Co-Expression on Heterologous Protein Production in .

Various host systems have been employed to increase the yield of recombinant proteins. However, some recombinant proteins were successfully produced at high yields but with no functional activities. To achieve both high protein yield and high activities, molecular biological strategies have been continuously developed.

A kinetic spectrophotometric method for the determination of pyridoxal-5'-phosphate based on coenzyme activation of apo-d-phenylglycine aminotransferase.

A new PLP assay method based on the coenzyme activation of apo-d-phenylglycine aminotransferase (apo-d-PhgAT) is reported. The assay process is comprised of two steps. First, PLP present in plasma samples is allowed to reconstitute apo-d-PhgAT, forming active holo-d-PhgAT.

Improvement of extracellular bacterial protein production in Pichia pastoris by co-expression of endoplasmic reticulum residing GroEL-GroES.

Pichia pastoris is an established host system for heterologous protein expression. However, the potential productivity of this system can be limited. In this study, the Escherichia coli chaperones (GroES-GroEL) were expressed from the P promoter and targeted to the secretory pathway through the endoplasmic reticulum (ER).

Effects of halophilic peptide fusion on solubility, stability, and catalytic performance of D-phenylglycine aminotransferase.

D-Phenylglycine aminotransferase (D-PhgAT) from Pseudomonas stutzeri ST-201 is useful for enzymatic synthesis of enantiomerically pure D-phenylglycine. However, its low protein solubility prevents its application at high substrate concentration. With an aim to increase the protein solubility, the N-terminus of D-PhgAT was genetically fused with short peptides (A1 α- helix, A2 α-helix, and ALAL, which is a hybrid of A1 and A2) from a ferredoxin enzyme of a halophilic archaeon, Halobacterium salinarum.

Sensitive non-radioactive determination of aminotransferase stereospecificity for C-4' hydrogen transfer on the coenzyme.

A sensitive non-radioactive method for determination of the stereospecificity of the C-4' hydrogen transfer on the coenzymes (pyridoxal phosphate, PLP; and pyridoxamine phosphate, PMP) of aminotransferases has been developed. Aminotransferase of unknown stereospecificity in its PLP form was incubated in (2)H(2)O with a substrate amino acid resulted in PMP labeled with deuterium at C-4' in the pro-S or pro-R configuration according to the stereospecificity of the aminotransferase tested. The [4'-(2)H]PMP was isolated from the enzyme protein and divided into two portions.