Microencapsulation of multi-component traditional Chinese herbs extracts and its application to traditional Chinese medicines loaded textiles.

Extracts of traditional Chinese herbs (TCH) contain a variety of anti-allergic, anti-inflammatory and other bioactive factors. However, the defect of easy degradation or loss of active ingredients limits its application in traditional Chinese medicines (TCM) loaded textiles. In this work, TCH extracts containing different active ingredients were innovatively proposed as the core material of microcapsules. The feasibility of microencapsulation of multi-component TCH extracts in the essential oil state was initially demonstrated. Polyacrylate was also used as a binder to load the microcapsules onto the fabric to improve the durability and wash resistance of the treated fabric. Modeling the oil release of microcapsules for controlled release under different conditions may provide new possible uses for the materials. Results show that the constructed microcapsule has a smooth surface without depression and can be continuously released for over 30 days. The release behavior of microcapsules follows different release mechanisms and can be modulated by temperature and water molecules. The incorporation of microcapsules and polyacrylate does not significantly change the fabric's air permeability, water vapor transmission and hydrophilicity. The washing durability and friction properties of the microcapsule-based fabric are greatly improved, and it can withstand 30 washing tests and 200 friction tests. Moreover, the results of methyl thiazolyl tetrazolium (MTT) release assay using human dermal papilla cells (HDP) as an in vitro template confirm that the microcapsule has no toxic effects on human cells. Therefore, the successful microencapsulation of multi-component TCH extracts indicates their potential application in the field of TCM-loaded textiles.

Molecular cloning and expression of yak (Bos grunniens) lactoferrin cDNA in Pichia pastoris.

cDNA encoding lactoferrin from yak was isolated by RT-PCR and then sequenced. The cloned cDNA (2127 bp) encodes a 709 amino acid precursor molecule of yak lactoferrin with a signal peptide of 19 amino acids. The yak lactoferrin cDNA was expressed in Pichia pastoris. The recombinant protein, purified by Ni-NTA affinity column, had a molecular weight of 76 kDa and reacted with an antibody raised against native bovine lactoferrin. The iron-binding behavior and antimicrobial activity of the purified protein indicated that it was correctly folded and functional.