The defatted seed meal of Camellia oleifera has been used as a natural detergent and its extract is commercially utilized as a foam-stabilizing and emulsifying agent. The goal of this study was to investigate the foam properties and detergent ability of the saponins from the defatted seed meal of C. oleifera. The crude saponin content in the defatted seed meal of C. oleifera was 8.34 and the total saponins content in the crude saponins extract was 39.5% (w/w). The foaming power of the 0.5 crude saponins extract solution from defatted seed meal of C. oleifera was 37.1 of 0.5 SLS solution and 51.3% to that of 0.5% Tween 80 solution. The R5 value of 86.0% represents good foam stability of the crude saponins extracted from the defatted seed meal of the plant. With the reduction of water surface tension from 72 mN/m to 50.0 mN/m, the 0.5% crude saponins extract solution has wetting ability. The sebum-removal experiment indicated that the crude saponins extract has moderate detergency. The detergent abilities of the saponins from C. oleifera and Sapindus mukorossi were also compared.

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This study examined the effects of different extracts of adlay seed on the growth of human lung cancer cells in vitro and in vivo. The data showed that a methanolic extract, but not a water extract, of adlay seed exerted an antiproliferative effect on A549 lung cancer cells by inducing cell cycle arrest and apoptosis. It was also found that tumor growth in vivo was inhibited by the methanolic extract in a dose-dependent manner. The chemopreventive effect of adlay seed on the tobacco-specific carcinogen 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone (NNK)-induced lung tumorigenesis in A/J mice was also investigated. Groups of mice were pre-fed with different diets, followed by feeding with NNK-containing drinking water for 8 months. The results indicated that feeding with diet containing 30% of powdered adlay seed reduced the number of surface lung tumors by approximately 50%. Taken together, these results indicate that the components of adlay seed exert an anticancer effect in vitro and in vivo and may be useful for the prevention of lung tumorigenesis.

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Our previous study demonstrate that vitamin D3 induces the binding of vitamin D3 receptor (VDR) to Sp1 transcription factor and stimulates p27Kip1 expression via the Sp1 consensus sequences in the promoter. Both VDR and Sp1 are transcriptional activators, it is unclear which protein functions as the transcription component of the VDR/Sp1 complex. To address this issue, we constructed the AF-2 deletion mutant of VDR and tested the effect of vitamin D3 on p27Kip1 expression. In consistent with our previous results, we found that expression of wild-type VDR in SW620 colon cancer cells, which expressed very low level of endogenous VDR, increased vitamin D3-stimulated p27Kip1 promoter activity and protein expression. On the contrary, expression of AF-2 deletion mutant had little effect. DNA affinity precipitation assay (DAPA) showed that both wild-type and deletion mutant of VDR bound to the DNA probe corresponding to the Sp1 binding site in the p27Kip1 promoter in a vitamin D3-dependent manner indicating deletion of AF-2 domain does not affect the interaction between VDR and Sp1. Chromatin immunoprecipitation (CHIP) assay also confirmed that VDR and its AF-2 deletion mutant bound to p27Kip1 promoter in vivo. We found that deletion of AF-2 domain abolished the interaction of coactivators SRC-1 and DRIP205 with VDR. Taken together, our results suggest that VDR functions as the transactivation component of the VDR/Sp1 complex to trigger gene expression.

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A gene encoding the thermostable raw starch digesting alpha-amylase in Thermobifida fusca NTU22 was amplified by PCR, sequenced and cloned into Pichia pastoris X-33 host strain using the vector pGAPZalphaA, allowing constitutive expression and secretion of the protein. Recombinant expression resulted in high levels of extracellular amylase production, as high as 510 U/l in the Hinton flask culture broth. The purified amylase showed a single band at about 65 kDa by SDS-polyacrylamide gel electrophoresis after being treated with endo-beta-N-acetylglycosaminidase H, and this agrees with the predicted size based on the nucleotide sequence. About 75% of the original activity remained after heat treatment at 60 degrees C for 3 h. The optimal pH and temperature of the purified amylase were 7.0 and 60 degrees C, respectively. The purified amylase exhibited a high level of activity with raw sago starch. After 48-h treatment, the DPw of raw sago starch obviously decreased from 830,945 to 378,732. The surface of starch granules was rough, and some granules displayed deep cavities.