Proteomic profile of edible bird's nest proteins.

Journal of agricultural and food chemistry (2012-12-12)
Xiaoqing Liu, Xintian Lai, Shiwei Zhang, Xiuli Huang, Quanxue Lan, Yun Li, Bifang Li, Wei Chen, Qinlei Zhang, Dezhi Hong, Guowu Yang

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.

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灰链霉菌来源几丁质酶, lyophilized powder (essentially salt free), ≥200 units/g solid
壳质酶 来源于绿色木霉, lyophilized powder, ≥600 units/g solid