Effects of adenosine extract from Pholiota adiposa (Fr.) quel on mRNA expressions of superoxide dismutase and immunomodulatory cytokines.

Pholiota adiposa is a kind of edible mushroom which has long been known for its health care applications. To reveal the exact mechanism of its protective functions in humans, in this study we isolated and identified the active compound PB3 of P. adiposa for the first time by a combination of chromatography techniques, including NKA macroporous resin and Sephadex G-15. PB3, with molecular mass of 267.2 Da and molecular formula of C10H13N5O4 discovered by mass spectrum (MS) was identified to be adenosine. Mice were injected intraperitoneally with purified fraction PB3. Seven days after injection, we found a 1.5-fold increase of IL10 at the mRNA level, while a down regulated expression of IL-2, IL-6 and IFN-γ to 49.0%, 56.9% and 73.4%, respectively, was detected in spleen by real-time quantitative PCR. What's more, SOD expression level was significantly increased by 1.6-fold compared to control. Fraction PB3 displayed anti-inflammatory potency and heightened SOD activity on the transcriptional level, which could be considered of further pharmaceutical or medication value.

Research Progress of Bioactive Proteins from the Edible and Medicinal Mushrooms.

For centuries, mushrooms have been widely used as traditional Chinese medicine in Asia. Apart from polysaccharides and some small-molecule components, such as flavones, polyphenols and terpenes, mushrooms produce a large number of pharmaceutically active proteins, which have become popular sources of natural antitumor, antimicrobial, immunoenhancing agents. These bioactive proteins include lectins, laccases, Ribosome Inactivating Proteins (RIPs), nucleases, and Fungal Immunomodulatory Proteins (FIPs). The review is to summarize the characterstics of structure and bioactivities involved in antitumor, antiviral, antifungal, antibacterial and immunoenhancing activities of proteins from edible mushrooms, to better understand their mechanisms, and to direct research.

Purification and characterization of antioxidant components from the fruiting bodies of Pleurotus abalonus including 9-beta-d-ribofuranosidoadenine, 5'-deoxy-5'-(methylthio)adenosine, and a triterpenoid.

Although Pleurotus abalonus is a well-known edible mushroom in Asia, there is a dearth of information on its antioxidant activity. The present report is the first one focused on the purification and characterization of 9-beta-d-ribofuranosidoadenine (ADO), 5'-deoxy-5'-(methylthio) adenosine (MTA) and a triterpenoid complex from P. abalonus. Different antioxidant activities including inhibitory effects on hemolysis and lipid peroxidation in brain and kidney homogenates as well as significant synergistic effect on scavenging of hydroxyl radicals were demonstrated, which lays a foundation for the development of P. abalonus as a natural antioxidant applied in medicine.

Separation and purification of the antioxidant compounds, caffeic acid phenethyl ester and caffeic acid from mushrooms by molecularly imprinted polymer.

Caffeic acid phenethyl ester (CAPE) and caffeic acid (CA), two naturally occurring phenolic antioxidants, have been reported to have a diversity of biological activities. In this investigation, a novel approach to separate and enrich CAPE and CA from 25 species of mushrooms using molecularly imprinted polymers (MIPs) as the sorbent material is reported. The MIPs were synthesized using CAPE as the template, and its adsorption behavior was investigated in detail. In comparison with C18-solid phase extraction (SPE), MIP-SPE displayed high selectivity and good affinity for CAPE and CA. The antioxidant potential of the mushroom extracts, before and after preconcentration using MIPs, was assayed by inhibition of erythrocyte hemolysis and lipid peroxidation. Application of MIPs with a high affinity toward CAPE and CA provides a novel method for obtaining active compounds from natural products.

Expression, purification, and characterization of phosphatidylserine synthase from Escherichia coli K12 in Bacillus subtilis.

Although phosphatidylserine synthase (PSS) from Escherichia coli is an ideal enzyme for phospholipid production, its application in the food industry has been limited because of the low PSS yield. In this study, the pss gene was cloned from E. coli K(12) and expressed in Bacillus subtilis DB104, and the recombinant PSS was characterized subsequently. PSS was purified to 39.59-fold, and the highest activity was detected as 13.62 U/mg. The enzyme was found to be stable in a pH range of 6.5-9.5, with optimal pH values of 8.0 for hydrolysis and 7.0 for transphosphatidylation, respectively. The optimal temperature for PSS activity was 35 degrees C. The enzyme activity could be detected after 1 h of heating at 65 degrees C. Among the detected detergents and metal ions, Triton X-100, Ca(2+), Mn(2+), and Co(2+) could improve PSS activity. The transformation of phosphatidylcholine to phosphatidylserine under PSS catalyzation was carried out in a biphasic system, which confirmed the actual catalyzing ability of the recombinant protein.