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Agglutinated blood transports differently onto paper than stable blood with well dispersed red cells. This difference was investigated to develop instantaneous blood typing tests using specific antibody-antigen interactions to trigger blood agglutination. Two series of experiments were performed. The first related the level of agglutination and the fluidic properties of blood on its transport in paper. Blood samples were mixed at different ratios with specific and nonspecific antibodies; a droplet of each mixture was deposited onto a filter paper strip, and the kinetics of wicking and red cell separation were measured. Agglutinated blood phase separated, with the red blood cells (RBC) forming a distinct spot upon contact with paper while the plasma wicked; in contrast, stable blood suspensions wicked uniformly. The second study analyzed the wicking and the chromatographic separation of droplets of blood deposited onto paper strips pretreated with specific and nonspecific antibodies. Drastic differences in transport occurred. Blood agglutinated by interaction with one of its specific antibodies phase separated, causing a chromatographic separation. The red cells wicked very little while the plasma wicked at a faster rate than the original blood sample. Blood agglutination and wicking in paper followed the concepts of colloids chemistry. The immunoglobin M antibodies agglutinated the red blood cells by polymer bridging, upon selective adsorption on the specific antigen at their surface. The transport kinetics was viscosity controlled, with the viscosity of red cells drastically increasing upon blood agglutination. Three arm prototypes were investigated for single-step blood typing.

The usage of renewable resources has become a hot topic upon the rising global awareness against fossil feedstock consumption. Lignin, the 2nd most abundant natural polymer on Earth, is an...

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Plastic waste, which is one of the major sources of pollution in the landfills and oceans, has raised global concern, primarily due to the huge production rate, high durability, and the lack of utilization of the available waste management techniques. Recycling methods are preferable to reduce the impact of plastic pollution to some extent. However, most of the recycling techniques are associated with different drawbacks, high cost and downgrading of product quality being among the notable ones. The sustainable option here is to upcycle the plastic waste to create high-value materials to compensate for the cost of production. Several upcycling techniques are constantly being investigated and explored, which is currently the only economical option to resolve the plastic waste issue. This Review provides a comprehensive insight on the promising chemical routes available for upcycling of the most widely used plastic and mixed plastic wastes. The challenges inherent to these processes, the recent advances, and the significant role of the science and research community in resolving these issues are further emphasized.

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Three of the major ligninolytic enzymes, lignin peroxidase (LiP), manganese peroxidase (MnP), and laccase (LA), as well as the secretome of a white-rot fungi, Grammothele fuligo, are tested on three industrial lignins (organosolv, alkali, and Kraft), to investigate and study the differences in biodegradation reactions and mechanism of these three lignins. Strategies involving additives in laccase mediated systems were also considered to produce small phenolic compounds. Three new or underreported additives including 2,4,6-tri-tert-butylphenol (TTBP), 4-tert-butyl-2,6-dimethylphenol (TBDMP), and 3hydroxyanthranilic acid (HAA) are compared to three classic laccase mediators violuric acid (VA), 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS), and 1-hydroxybenzotriazole (1-HBT). Decrease of molecular weight by up to 73% could be obtained on organosolv lignin with LA−VA systems, and by 49%, 43%, and 39% when LA was used with ABTS, TBDMP, and 1-HBT, respectively. In-depth analysis of the degradation products by quantitative 2D HMQC NMR indicated that the oxidation is mediator-dependent and provides new insights on the enzymatic mechanism.