Scytalidin

Wood-staining fungal pigments have shown potential use as colorants for wood and textiles, with organic solvents as the pigment carrier. Natural oils have been suggested as an environmentally friendly and more available carrier; however, oils promoted color degradation. The current study examined the mechanism of said degradation and tested therapeutic and food-grade oils (instead of finishing oils) for their potential to carry draconin red, the pigment from Scytalidium cuboideum, without color loss over time. FTIR analysis from finishing oils indicated that oxidation was not likely the cause of color loss as the pigment could not be distinguished from the oils in the IR spectra. SEM was employed to determine if crystal degradation was contributing to color loss and indicated, surprisingly, that the crystals of draconin red formed rather than degraded over time. This suggested crystal breakdown was also not likely the cause of color loss. The pigment did not show degradation in hemp oil, flaxseed oil, and cold-pressed linseed oil when treated with β-carotene. Further in-depth chemical studies are needed to determine the mechanism of color loss in pigmented natural oils; however, food-grade oils appear to be a promising alternative to carry draconin red, without degradation of the color.

Scytalidium catalase is a homotetramer including heme d in each subunit. Its primary function is the dismutation of H2O2 to water and oxygen, but it is also able to oxidase various small organic compounds including catechol and phenol. The crystal structure of Scytalidium catalase reveals the presence of three linked channels providing access to the exterior like other catalases reported so far. The function of these channels has been extensively studied, revealing the possible routes for substrate flow and product release. In this report, we have focussed on the semi-conserved residue Val228, located near to the vinyl groups of the heme at the opening of the lateral channel. Its replacement with Ala, Ser, Gly, Cys, Phe and Ile were tested. We observed a significant decrease in catalytic efficiency in all mutants with the exception of a remarkable increase in oxidase activity when Val228 was mutated to either Ala, Gly or Ser. The reduced catalytic efficiencies are characterized in terms of the restriction of hydrogen peroxide as electron acceptor in the active centre resulting from the opening of lateral channel inlet by introducing the smaller side chain residues. On the other hand, the increased oxidase activity is explained by allowing the suitable electron donor to approach more closely to the heme. The crystal structures of V228C and V228I were determined at 1.41 and 1.47 Å resolution, respectively. The lateral channels of the V228C and V228I presented a broadly identical chain of arranged waters to that observed for wild-type enzyme.

Identification of effective natural dyes with the potential for low environmental impact has been a recent focus of the textile industry. Pigments derived from spalting fungi have previously shown promise as textile dyes; however, their use has required numerous organic solvents with human health implications. This research explored the possibility of using linseed oil as a carrier for the pigment from Scytalidium cuboideum as a textile dye. Colored linseed oil effectively dyed a range of fabrics, with natural fibers showing better coloration. Scanning electron microscopy (SEM) revealed a pigment film over the fabric surface. While mechanical testing showed no strength loss in treated fabric, colorfastness tests showed significant changes in color in response to laundering and bleach exposure with variable effects across fabric varieties. SEM investigation confirmed differences in pigmented oil layer loss and showed variation in pigment crystal formation between fabric varieties. Heating of the pigmented oil layer was found to result in a bright, shiny fabric surface, which may have potential for naturally weatherproof garments.