Oxidative stress has been linked with the pathogenesis of many human diseases including cancer, aging, and atherosclerosis. The present study investigates the antioxidant activities of peptides isolated from the medicinal mushroom, Ganoderma lucidum. G. lucidum has been shown to possess potent antioxidant activity with little or no side effects. Polysaccharide, polysaccharide-peptide complex, and phenolic components of G. lucidum have been proposed to be responsible for this antioxidant effect. However, research has shown that the G. lucidum peptide (GLP) is the major antioxidant component of G. lucidum. The objective of this study was to evaluate the antioxidant activity of this peptide using different oxidation systems. GLP showed potent antioxidant activities in both lightproof soybean oil and lard systems, assessed by lipid peroxidant value. Compared to butylated hydroxytoluene, GLP showed a higher antioxidant activity in the soybean oil system. Soybean lipoxygenase activity was blocked by GLP in a dose-dependent manner with an IC50 value of 27.1 microg/mL. GLP showed scavenging activity toward hydroxyl radicals produced in a deoxyribose system with an IC50 value of 25 microg/mL, and GLP effectively quenched superoxide radical anion produced by pyrogallol autoxidation in a dose-dependent manner. Malondialdehyde level has been used as the oxidation index in many biological systems. GLP showed substantial antioxidant activity in the rat liver tissue homogenates and mitochondrial membrane peroxidation systems. The auto-hemolysis of rat red blood cells was also blocked by GLP in a dose-dependent manner. On the basis of these results, it is concluded that GLP is the major constituent responsible for the antioxidant activity of G. lucidum. GLP could play an important role in the inhibition of lipid peroxidation in biological systems through its antioxidant, metal chelating, and free radical scavenging activities.

Protease-producing bacteria are known to play an important role in degrading sedimentary particular organic nitrogen, and yet, their diversity and extracellular proteases remain largely unknown. In this paper, the diversity of the cultivable protease-producing bacteria and their extracellular proteases in the sediments of the South China Sea was investigated. The richness of the cultivable protease-producing bacteria reached 10(6) cells/g in all sediment samples. Analysis of the 16S rRNA gene sequences revealed that the predominant cultivated protease-producing bacteria are Gammaproteobacteria affiliated with the genera Pseudoalteromonas, Alteromonas, Marinobacter, Idiomarina, Halomonas, Vibrio, Shewanella, Pseudomonas, and Rheinheimera, with Alteromonas (34.6%) and Pseudoalteromonas (28.2%) as the predominant groups. Inhibitor analysis showed that nearly all the extracellular proteases from the bacteria are serine proteases or metalloproteases. Moreover, these proteases have different hydrolytic ability to different proteins, reflecting they may belong to different kinds of serine proteases or metalloproteases. To our knowledge, this study represents the first report of the diversity of bacterial proteases in deep-sea sediments.

Food-grade phycocyanin was obtained from Spirulina platensis cultured in seawater-based medium and purified by ammonium sulfate precipitation. The stability of phycocyanin under different conditions, including different pH, temperature, light, and edible stabilizing agents, was systematically investigated by spectroscopy methods. The optimum pH range for phycocyanin was found to be 5.0-6.0. Phycocyanin was kept stable at temperatures up to 45ºC over short time periods (i.e., no significant changes were observed in the relative concentration of phycocyanin, C R ). In contrast, incubation at a relatively high temperature resulted in a decrease in the C R and half-life in a temperature-dependent manner. Constant exposure to light at 100 μmol m -2 s -1 for 36 h, decreased the C R value of phycocyanin (pH5.0) to 78.4%. Sodium chloride was an effective stabilizing agent for phycocyanin, and its efficacy increased in a concentration-dependent manner for all concentration ranges assessed in this study. Moreover, phycocyanin exhibited concentration-dependent antioxidant activities in 2,2′-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) and α,α-Diphenyl-β-pricrylhydrazyl assays. Taken together, our results suggest that the optimal conditions for preserving the stability of food-grade phycocyanin isolated from S. platensis are a pH of 5.0-6.0, low temperature, darkness, and the addition of edible stabilizing agents.