Polyester-based scaffolds are of research interest for the regeneration of a wide spectrum of tissues. However, there is a need to improve scaffold wettability and introduce bioactivity. Surface modification is a widely studied approach for improving scaffold performance and maintaining appropriate bulk properties. In this study, three methods to functionalize the surface of the poly(lactide-co-ε-caprolactone) PLCL fibres using gelatin immobilisation were compared. Hydrolysis, oxygen plasma treatment, and aminolysis were chosen as activation methods to introduce carboxyl (-COOH) and amino (-NH2) functional groups on the surface before gelatin immobilisation. To covalently attach the gelatin, carbodiimide coupling was chosen for hydrolysed and plasma-treated materials, and glutaraldehyde crosslinking was used in the case of the aminolysed samples. Materials after physical entrapment of gelatin and immobilisation using carbodiimide coupling without previous activation were prepared as controls. The difference in gelatin amount on the surface, impact on the fibres morphology, molecular weight, and mechanical properties were observed depending on the type of modification and applied parameters of activation. It was shown that hydrolysis influences the surface of the material the most, whereas plasma treatment and aminolysis have an effect on the whole volume of the material. Despite this difference, bulk mechanical properties were affected for all the approaches. All materials were completely hydrophilic after functionalization. Cytotoxicity was not recognized for any of the samples. Gelatin immobilisation resulted in improved L929 cell morphology with the best effect for samples activated with hydrolysis and plasma treatment. Our study indicates that the use of any surface activation method should be limited to the lowest concentration/reaction time that enables subsequent satisfactory functionalization and the decision should be based on a specific function that the final scaffold material has to perform.

Molecular recognition of saccharides is a growing field, which has many implications in cancer therapy, drug discovery, and cellular communication among others. The participation of CH/π interactions in this event is well known. Nevertheless, the intrinsic role of CH/π for modulating chemical reactions is still far from being applicable. In this experimental and computational work we have evaluated the participation of CH/π interactions in the aminolysis reaction of acetyl galactoside promoted with different 6-substituted 2(1H)-pyridones. Two features have been incorporated to the promoter molecular structure, on one end the promoting pyridone group and on the other end the recognition moiety, joined together by an alkyne spacer. The small increment in the observed pseudo-first-order rate constant values (kobs) was related to the stability of the transition state provided by noncovalent interactions, including CH/π interactions. A longer alkyne spacer was necessary to improve the molecular recognition of the galactoside substrate. The trend of the calculated activation energy values (ΔERTS) was in good accordance with the experimental rate constant values.

In this paper, a comprehensive study has been made on the detection of free fatty acids (FFAs) in palm oil via an optical technique based on enzymatic aminolysis reactions. FFAs in crude palm oil (CPO) were converted into fatty hydroxamic acids (FHAs) in a biphasic lipid/aqueous medium in the presence of immobilized lipase. The colored compound formed after complexation between FHA and vanadium (V) ion solution was proportional to the FFA content in the CPO samples and was analyzed using a spectrophotometric method. In order to develop a rapid detection system, the parameters involved in the aminolysis process were studied. The utilization of immobilized lipase as catalyst during the aminolysis process offers simplicity in the product isolation and the possibility of conducting the process under extreme reaction conditions. A good agreement was found between the developed method using immobilized Thermomyces lanuginose lipase as catalyst for the aminolysis process and the Malaysian Palm Oil Board (MPOB) standard titration method (R2 = 0.9453).