Chloroperoxidase-catalyzed oxidation of N-methyl-4-chloroaniline
Chloroperoxidase catalyzed the H2O2 oxidative conversion of N-methyl-4-chloroaniline to 4-chloronitrosobenzene, 4-chloroaniline and a mixture of complex products.
New Trends in Fungal Biooxidation
Biooxidations using isolated biocatalysts for the oxidative conversion of organic compounds and materials are becoming more and more important in the industrial sector. Research in this direction is part of the rapidly developing field of White Biotechnology and is carried out not least against the background of sustainable development and the need to replace environmentally risky technologies by eco-friendly processes. Whereas whole cells are already widely used as oxidative biocatalysts, the application of isolated enzymes is still limited to a few examples. One reason for that is the cost-intensive production and laborious purification of enzymes which are mostly intracellular and sometimes membrane-bound proteins with low stability and complex co-factor requirements. The use of secreted oxidoreductases offers several advantages: they are easier to separate and purify, need only cheap co-substrates such as dioxygen or peroxides and are far more stable than intracellular enzymes. Filamentous fungi secrete a broad spectrum of oxidative biocatalysts which are involved, amongst others, in the degradation of recalcitrant biopolymers, the synthesis of melanins as well as the detoxification of plant ingredients, microbial metabolites and organopollutants. We focus here on novel secreted enzymes - peroxygenases and DyP-type peroxidases - with remarkable catalytic properties. Furthermore selected features of “classic” fungal oxidoreductases, such as laccase, tyrosinase and chloroperoxidase, are discussed against the background of innovative recent developments in the field of enzyme application.
Thermal stability of reconstituted collagen fibrils. Shrinkage characteristics upon in vitro maturation
Thermal stability measured as area shrinkage without tension during heating was determined for membranes of collagen fibrils reconstituted from solutions of highly purified rat skin collagens. Shrinkage in per cent of area at 25 degrees C and shrinkage temperature were quantitated in a standardized way and determined as a function of in vitro maturation time for 11 to 104 days after aggregation for the collagen membranes. Similar to reports on intact rat skin, shrinkage temperature remained constant and shrinkage per cent declined with a rate decreasing with time during maturation. Solubility in water at 80 degrees C for 2 hours was 95-96% and remained unchanged for the maturation time (about 2 months) studied. The decreased shrinkage reflecting a lower degree of collapse is ascribed to an increasing thermal stability of the membranes during maturation. Development of heat-stable bonds in the reconstituted collagen fibrils is taken up to be amenable to this increased stability. Similarity in changes of shrinkage characteristics during in vivo and in vitro maturation indicates that maturation changes in reconstituted collagen fibrils reflect those occurring in intact collagen during in vivo aging.