Edible bird's nest (EBN) is derived from the saliva of certain types of swiftlets. It is consumed in many parts of the world for its nutritional and medicinal values. Although many claims have been made on the therapeutic and health-promoting effects of EBN, scientific documentations regarding these effects are very limited in published literature. It is not until recently that the biological effects of EBN are being investigated and evidence-based studies are being conducted. Several studies have found that EBN may enhance cell proliferation and differentiation and various beneficial effects have been reported in vitro as well as in vivo. While these studies point towards the potential use of EBN in the treatment or even prevention of several diseases, the mechanisms of action of EBN remain largely unknown and more explorations are needed. This review is one of the very few scientific reviews on EBN which focuses on recent evidence-based discoveries.
The concentrations of calcium, phosphate, protein and nitrite in whole unstimulated saliva, and the salivary flow rate under fasting conditions (saliva collected at least after 6 h without food and water) were compared with those under control conditions (saliva collected within 30 min to 1 h after food). The flow rate of fasting saliva was half that of control (0.098 ml/min vs 0.208 ml/min) and no significant differences in the flow rate were observed between sexes. The concentration of nitrite under fasting conditions was 50% higher than that in control saliva (p less than 0.05). The protein concentration was decreased, but not significantly, under fasting conditions. The composition of fasting saliva with regard to calcium and phosphate concentrations was comparable to that of the control. No significant variations in these components between sexes were observed under either condition.
Edible bird's nest (EBN) is made of the swiftlets' saliva, which has attracted rather more attention owing to its nutritious and medical properties. Although protein constitutes the main composition and plays an important role in EBN, few studies have focused on the proteomic profile of EBN. The purpose of this study was to produce a proteomic map and clarify common EBN proteins. Liquid-phase isoelectric focusing (LIEF) was combined with two-dimensional electrophoresis (2-DE) for comprehensive analysis of EBN proteins. From 20 to 100 protein spots were detected on 2-DE maps of EBN samples from 15 different sources. The proteins were mainly distributed in four taxa (A, B, C, and D) according to their molecular mass. Taxa A and D both contained common proteins and proteins that may be considered another characteristic of EBN. Taxon A was identified using MALDI-TOF-TOF/MS and found to be homologous to acidic mammalian chitinase-like ( Meleagris gallopavo ), which is in glycosyl hydrolase family 18.