Enzymatic cross-linking to improve the handling properties of dough prepared within a normal and reduced NaCl environment.

This research examines the use of three enzymes [glucose oxidase (GOX), hexose oxidase (HOX), and xylanase (XYL)] and their combinations [GOX-XYL and HOX-XYL] on the dough handling properties of CDC Plentiful and Stettler wheat cultivars prepared at reduced (1.0% wt. by flour) and normal (2.0% wt. by flour) NaCl levels. Properties investigated include dough rheology, stickiness, and ratio of resistance to extension and extensibility. The inclusion of XYL and its combinations with GOX and HOX increased the stickiness, yielded lower dough strength indicated by rheology, and reduced the ratio of resistance to extension and extensibility. The inclusion of oxidative enzymes yielded a stronger dough, where HOX addition to dough had the lowest stickiness values and highest |G*| values, whereas GOX addition led to the highest ratio of resistance to extension-extensibility. NaCl only had minor effects overall on dough strength and stickiness for the cultivars studied. Overall, superior dough handling properties were observed with oxidative enzyme addition (GOX and HOX) suggesting that the increased crosslinking that occurs could aid in improving low sodium bread dough properties.

Single electron reduction of xenobiotic compounds by glucose oxidase from Aspergillus niger.

Various species of fungi express glucose oxidase that catalyzes formation of gluconolactone from glucose with concomitant, direct divalent reduction of molecular oxygen to hydrogen peroxide. A physiological function ascribed to this extracellular enzyme is production of hydrogen peroxide for use in lignin degradation catalyzed by lignin peroxidases. Herein, we show that glucose oxidase can catalyze one-electron reduction of several different classes of xenobiotic compounds resulting in generation of free radical products. Electron spin resonance (ESR) spectroscopy was used to visualize the one-electron reduction products of 4-nitropyridine-N-oxide (4NPO), 1,4-naphthoquinone (1,4NQ), and dichlorophenolindolphenol (DCPIP). Hyperfine splitting constants were used to generate computer simulations of the spectra confirming the presence of free radical products.

Davallialactone reduces inflammation and repairs dentinogenesis on glucose oxidase-induced stress in dental pulp cells.

INTRODUCTION: The chronic nature of diabetes mellitus (DM) raises the risk of oral complication diseases. In general, DM causes oxidative stress to organs. This study aimed to evaluate the cellular change of dental pulp cells against glucose oxidative stress by glucose oxidase with a high glucose state. The purpose of this study was to test the antioxidant character of davallialactone and to reduce the pathogenesis of dental pulp cells against glucose oxidative stress. METHODS: The glucose oxidase with a high glucose concentration was tested for hydroxy peroxide (H2O2) production, cellular toxicity, reactive oxygen species (ROS) formation, induction of inflammatory molecules and disturbance of dentin mineralization in human dental pulp cells. The anti-oxidant effect of Davallilactone was investigated to restore dental pulp cells' vitality and dentin mineralization via reduction of H2O2 production, cellular toxicity, ROS formation and inflammatory molecules. RESULTS: The treatment of glucose oxidase with a high glucose concentration increased H2O2 production, cellular toxicity, and inflammatory molecules and disturbed dentin mineralization by reducing pulp cell activity. However, davallialactone reduced H2O2 production, cellular toxicity, ROS formation, inflammatory molecules, and dentin mineralization disturbances even with a long-term glucose oxidative stress state. CONCLUSIONS: The results of this study imply that the development of oral complications is related to the irreversible damage of dental pulp cells by DM-induced oxidative stress. Davallialactone, a natural antioxidant, may be useful to treat complicated oral disease, representing an improvement for pulp vital therapy.

Interaction of Nectarin 4 with a fungal protein triggers a microbial surveillance and defense mechanism in nectar.

Understanding the biochemical mechanisms by which plants respond to microbial infection is a fundamental goal of plant science. Extracellular dermal glycoproteins (EDGPs) are widely expressed in plant tissues and have been implicated in plant defense responses. Although EDGPs are known to interact with fungal proteins, the downstream effects of these interactions are poorly understood. To gain insight into these phenomena, we used tobacco floral nectar as a model system to identify a mechanism by which the EDGP known as Nectarin IV (NEC4) functions as pathogen surveillance molecule. Our data demonstrates that the interaction of NEC4 with a fungal endoglucanase (XEG) promotes the catalytic activity of Nectarin V (NEC5), which catalyzes the conversion of glucose and molecular oxygen to gluconic acid and H(2)O(2). Significantly enhanced NEC5 activity was observed when XEG was added to nectar or nectarin solutions that contain NEC4. This response was also observed when the purified NEC4:XEG complex was added to NEC4-depleted nectarin solutions, which did not respond to XEG alone. These results indicate that formation of the NEC4:XEG complex is a key step leading to induction of NEC5 activity in floral nectar, resulting in an increase in concentrations of reactive oxygen species (ROS), which are known to inhibit microbial growth directly and activate signal transduction pathways that induce innate immunity responses in the plant.

Protein stabilisation using additives based on multiple electrostatic interactions.

A method of elevating the storage lifetime of purified proteins has been discovered which appears to confer stability to all proteins investigated and may therefore be classed as generic in action. The basic methodology involves the formation of multiple electrostatic complexes between the protein and selected soluble polyelectrolytes to give protein-polyelectrolyte (PP) complexes and then to add solutions of polyalcohols or other compounds containing multiple hydroxyl groups. Dehydration of the resulting solution by vacuum evaporation, freeze drying or forced air convection produces a dry film or powder of stabilised protein. The method has been used mainly in the preparation of active enzymes for analytical tests. It has also been found that the formation of PP complexes also enhances the stability of enzymes in solution and the technique may be applicable to the stabilisation of virus suspensions by polycations. Examples of stabilised enzymes prepared by these methods are given and the proposed mechanism of stabilisation and applicability of the method to shelf-stable vaccine products are discussed.