Natural rubber (NR) gloves manufactured from NR latex are widely utilized in various applications as a personal protective device due to their exceptional barrier characteristics in infection control. However, the use of NR gloves was associated with concerns on NR protein allergy. With comprehensive leaching procedures now a common practice in NR latex glove factories to eliminate latent rubber proteins and chemical allergens, occurrences and complaints of protein allergy from medical glove users have decreased drastically over the past two decades. The present work aims to eliminate further the residual rubber allergens in NR latex through effective purification of the NR latex and compounding the thus purified latex with an established formulation for allergy-free NR for glove applications. NR latex was purified by deproteinization and saponification, respectively. Several analytical techniques were used to verify rubber allergens eliminated in the purified latexes. Saponified NR (SPNR) latex was the purified NR latex of choice since it is devoid of allergenic proteins and poses the lowest risk of Type I allergy. The purified NR latex was compounded with zinc diethyldithiocarbamate (ZDEC), zinc dibutyldithiocarbamate (ZDBC), and zinc 2-mercaptobenzothiazole (ZMBT), respectively, for glove dipping. Among the investigated accelerators, only ZDBC was not detected in the artificial sweat that came into contact with the dipped articles. Thus, it is deduced that ZDBC poses the lowest risk of Type IV allergy to consumers. Additionally, the morphological and physical properties of dipped articles were assessed. It was revealed that the dipped film from the SPNR latex compounded with ZDBC provided thinner and less yellow products with a more uniform internal structure and a tensile strength comparable to those of commercial NR gloves.
Natural rubber (NR) latex derived from Hevea brasiliensis is a complex colloid comprising mainly rubber hydrocarbons (latex particles) and a multitude of minor non-rubber constituents such as non-rubber particles, proteins, lipids, carbohydrates, and soluble organic and inorganic substances. NR latex is susceptible to enzymatic attack after it leaves the trees. It is usually preserved with ammonia and, to a lesser extent, with other preservatives to enhance its colloidal stability during storage. Despite numerous studies in the literature on the influence of rubber proteins on NR latex stability, issues regarding the effect of protein hydrolysis in the presence of ammonia on latex stability during storage are still far from resolved. The present work aims to elucidate the interplay between protein hydrolysis and ammoniation in NR latex stability. Both high- and low-ammonia (with a secondary preservative) NR latexes were used to monitor the changes in their protein compositions during storage. High-ammonia (FNR-A) latex preserved with 0.6% (v/v) ammonia, a low 0.1% ammonia/TMTD/ZnO (FNR-TZ) latex, and a deproteinized NR (PDNR) latex were labeled with fluorescence agents and observed using confocal laser scanning microscopy to determine their protein composition. Protein hydrolysis was confirmed via sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The results revealed that protein hydrolysis increased with the storage duration. The change in protein composition accompanying hydrolysis also allows the spatial distribution of allergenic proteins to be estimated in the latex. Concurrently, the latex stability increased with the storage duration, as measured by the latex's mechanical stability time (MST) and the zeta potential of the latex particles. As monitored by AFM, the surface roughness of the NR latex film increased markedly during extended storage compared with that of the DPNR latex, which remained smooth. These results underscore the pivotal role of ammonia in bolstering NR latex stability brought on by protein hydrolysis, which greatly impacts latex film's formation behavior. NR latex stability underpins the quality of latex-dipped goods during manufacturing, particularly those for medical gloves.
The stabilization mechanism of natural rubber (NR) latex from Hevea brasiliensis was studied to investigate the components involved in base-catalyzed ester hydrolysis, namely, hydrolyzable lipids, ammonia, and the products responsible for the desired phenomenon observed in ammonia-preserved NR latex. Latex stability is generally thought to come from a rubber particle (RP) dispersion in the serum, which is encouraged by negatively charged species distributed on the RP surface. The mechanical stability time (MST) and zeta potential were measured to monitor field latices preserved in high (FNR-HA) and low ammonia (FNR-LA) contents as well as that with the ester-containing components removed (saponified NR) at different storage times. Amounts of carboxylates of free fatty acids (FFAs), which were released by the transformation and also hypothesized to be responsible for the like-charge repulsion of RPs, were measured as the higher fatty acid (HFA) number and corroborated by confocal laser scanning microscopy (CLSM) both qualitatively and quantitatively. The lipids and their FFA products interact differently with Nile red, which is a lipid-selective and polarity-sensitive fluorophore, and consequently re-emit characteristically. The results were confirmed by conventional ester content determination utilizing different solvent extraction systems to reveal that the lipids hydrolyzed to provide negatively charged fatty acid species were mainly the polar lipids (glycolipids and phospholipids) at the RP membrane but not those directly linked to the rubber molecule and, to a certain extent, those suspended in the serum. From new findings disclosed herein together with those already reported, a new model for the Hevea rubber particle in the latex form is proposed.