Water‐dispersible microparticles of polyunsaturated oils

Health benefits of polyunsaturated oils are well known; nevertheless, incorporating these oils into food/feed products is not possible due to their chemical instability. Here purified fish oil with 32% (w/w) polyunsaturated fatty acids is co‐encapsulated with the antioxidant butylhydroxyanisole, into 1.0 ± 0.7 μm cellulose‐based microspheres by solvent precipitation method, at the fish oil loading content of 41% and encapsulation efficiency of 81%. Aqueous suspension of the encapsulated fish oil particles shows significantly improved oxidative stability, thermal stability, photostability and shelf‐life stability. Dry powder of the fish oil particles shows excellent shelf‐life stability. Double bond functionality of the encapsulated oil can tolerate high production temperature such as the shrimp feed production process (95 °C for 10 min) or spray dry process (outlet temperature of 120 °C). This encapsulation strategy using biocompatible cellulose polymer should enable effective and versatile applications of polyunsaturated oils in foods, feeds and cosmetics.     

A thermostable lectin from the rhizomes of Kaempferia parviflora

BACKGROUND: Kaempferia parviflora, or black galingale (Kra‐Chai‐Dam), belongs to the Zingiberaceae family and is used as both a food ingredient and a medicinal plant. There are diverse reports on the biological activities of compounds extracted from the plant, such as antimalarial, antifungal and an effective sexual‐enhancing role, but not on the lectins. RESULTS: A lectin was isolated from the rhizomes of Kaempferia parviflora using affinity chromatography on Concanavalin A followed by gel filtration chromatography on Sephacryl S‐100. The molecular weight of the purified lectin was about 41.7 kDa. This lectin showed haemagglutinating activity against erythrocytes from several sources, with the highest level being against those from rabbits. Moreover, the lectin was thermostable, with significant haemagglutinating activity detectable up to 75 °C. The results of trypsin digestion and liquid chromatography/tandem mass spectrometry analysis suggested that this protein could be a member of the lectin/endochitnase1 family. CONCLUSION: A lectin that showed thermotolerant haemagglutinating activity against erythrocytes from several sources was successfully purified from K. paviflora rhizomes. Peptide sequence analysis indicated that this lectin is similar to lectin/endochitinase 1 (Urtica dioica) or Hevein‐like protein (Hevea brasiliensis). Copyright © 2010 Society of Chemical Industry