Antiradical Potential of Food Products as a Comprehensive Measure of Their Quality.

Antiradical potential (ARP) is an important measure of food safety. In addition, it directly or indirectly affects the rate of occurrence of a number of human pathologies. Using a photocolorimetric analysis of DPPH (2,2-diphenyl-1-picrylhydrazyl) solutions, we estimated the antiradical potential of food raw materials, food concentrates, biologically active substances, and wild plants. We conducted approximately 1500 analyses of almost 100 food products selected from 11 food groups: vegetables, milk, meat, fish, cereals and bread, drinks (including tea and coffee), etc. With a confidence interval (CI) of 95%, the average values for animal products range from 15.87 to 18.70 ascorbic acid equivalents per gram of dry matter. For plant materials, the range is 474.54-501.50 equivalents when wild herbs are included and 385.02-408.83 equivalents without taking herbs into account. The antiradical potential of the biologically active substances we studied ranged from 706.84 to 847.77 equivalents per gram of dry matter, which makes it possible to use some of the components to repair products with low ARP values, for example, bread and baked goods, confectionery, milk and dairy products, carbonated drinks, and juice. In this study, a low ARP value is associated with a reduction in the shelf life of products and a deterioration in their organoleptic properties; therefore, we propose using ARP as an important reference for describing the quality of food products and raw food materials.

Potentials of polysaccharides, lipids and proteins in biodegradable food packaging applications.

Bio-based packaging materials are gaining importance due to their biodegradability, sustainability and environmental friendliness. To control the food quality and improve the food safety standards, proteins polysaccharide and lipid-based packaging films are enriched with bioactive and functional substances. However, poor permeability and mechanical characteristics are the challenging areas in their commercialization. Scientists and researchers are using a combination of techniques i.e. hydrogels, crosslinking, etc. to improve the intermolecular forces between different components of the film formulation to counter these challenges More recently, biodegradable packaging materials, sometimes edible, are also used for the delivery of functional ingredients which reveals their potential for drug delivery to counter the nutrient deficiency problems. This study highlights the potentials of bio-based materials i.e. proteins, polysaccharides, lipids, etc. to develop biodegradable packaging materials. It also explores the additives used to improve the physicochemical and mechanical properties of biodegradable packaging materials. Furthermore, it highlights the novel trends in biodegradable packaging from a food safety and quality point of view.

Actin cross-linking and inhibition of the actomyosin motor.

Intrastrand cross-linking of actin filaments by ANP, N-(4-azido-2-nitrophenyl) putrescine, between Gln-41 in subdomain 2 and Cys-374 at the C-terminus, was shown to inhibit force generation with myosin in the in vitro motility assays [Kim et al. (1998) Biochemistry 37, 17801-17809]. To clarify the immobilization of which of these two sites inhibits the actomyosin motor, the properties of actins with partially overlapping cross-linked sites were examined. pPDM (N,N'-p-phenylenedimaleimide) and ABP [N-(4-azidobenzoyl) putrescine] were used to obtain actin filaments cross-linked ( approximately 50%) between Cys-374 and Lys-191 (interstrand) and Gln-41 and Lys-113 (intrastrand), respectively. ANP, ABP, and pPDM cross-linked filaments showed similar inhibition of their sliding speeds and force generation with myosin ( approximately 25%) in the in vitro motility assays. In analogy to ANP cross-linking of actin, pPDM and ABP cross-linkings did not change the strong S1 binding to actin and the V(max) and K(m) parameters of actomyosin ATPase. The similar effects of these three cross-linkings reveal the tight coupling between structural elements of the subdomain 2/subdomain 1 interface and show the importance of its dynamic flexibility to force generation with myosin. The possibility that actin cross-linkings inhibit rate-limiting steps in motion and force generation during myosin cross-bridge cycle was tested in stopped-flow experiments. Measurements of the rates of mantADP release from actoS1 and ATP-induced dissociation of actoS1 did not reveal any differences between un-cross-linked and ANP cross-linked actin in these complexes. These findings are discussed in terms of the uncoupling between force generation and other aspects of actomyosin interactions due to a constrained dynamic flexibility of the subdomain 2/subdomain 1 interface in cross-linked actin filaments.