Enhancing emulsification and antioxidant ability of egg albumin by moderately acid hydrolysis: Modulating an emulsion-based system for mulberry seed oil.

Mulberry seed oil (MSO) is a kind of potential health-care lipids. This study, we investigated unsaturated fatty acids profiles of freshly squeezed MSO by GC-MS and modulated an oil-in-water emulsion system stabilized by acid hydrolyzed egg albumin (AHEA) to protect MSO from oxidation. The results showed that the content of total unsaturated fatty acids in MSO was almost 80%, of which 9, 12- and 10, 13-linoleic acid was over 60% and 10% respectively. In the case of the MSO-in-AHEA emulsions, it was observed that acid hydrolysis improved emulsifying effect, emulsifying stability and antioxidant activity of egg albumin (EA). The hydrolysates of EA (1%, w/w) acid hydrolyzed for 4 h at 85 °C had the best DPPH radical scavenging efficiency. It was suitable for EA to hydrolyze for 4 to 12 h at pH 2.5 and 85 °C because of their better emulsification and oxidation stability than the others. The results about AHEA could be valuable for designing delivery and protect systems for MSO or other bioactive component to avoid their oxidative damage or control their release.

A novel extracellular protease with fibrinolytic activity from the culture supernatant of Cordyceps sinensis: purification and characterization.

A novel serine protease with fibrinolytic activity named CSP was purified from the culture supernatant of the fungus Cordyceps sinensis, a kind of Chinese herbal medicine. Analysis of the purified enzyme by SDS-PAGE indicated that CSP was a single polypeptide chain with an apparent molecular weight of 31 kDa, and N-terminal sequencing revealed that the first ten amino acid residues of the enzyme were Ala-Leu-Ala-Thr-Gln-His-Gly-Ala-Pro-Trp-. When casein was used as a substrate, the proteolytic activity of CSP reached its maximum at pH 7.0 and 40 degrees C. The effect of chemical agents on the enzyme activity indicated that CSP is a serine protease with a free cysteine residue near the active site. It hydrolysed fibrinogen, fibrin and casein with a high efficiency, while hydrolysing bovine serum albumin (BSA) and human serum albumin (HSA) to a lesser extent. CSP was found to be a plasmin-like protease, but not a plasminogen activator, and it preferentially cleaved the A alpha chain of fibrinogen and the alpha-chain of fibrin. Therefore, the extracellular protein CSP may represent a potential new therapeutic agent for the treatment of thrombosis.