ABSTRACT
This study aimed to investigate the influence of modified starches on the quality of skins of glutinous rice dumplings (SGRDs), including changes in textural properties, pasting parameters, microstructure, color, transparency, and sensory quality. The results showed that the addition of a single acetylated-modified cassava or potato starch or composite modified cassava and potato starch in a ratio of 2:1 can improve the quality of SGRDs. The springiness and lightness of SGRDs increased, and the transparency increased from 3.22 % to 6.18 %. The cooked samples had delicate mouth-feel, uniform color and luster, good transparency, no depression, and low weight loss and did not stick to the teeth. Moreover, the total consumer acceptability score increased from 60.67 to 89.33, indicating that these products were widely accepted by consumers. However, the addition of hydroxypropyl-modified cassava starch or its composite with other two modified starches had no apparent effect on the quality of SGRDs. In conclusion, the quality of SGRDs were significantly improved by the addition of single or composite acetylated-modified starches. This study provides a theoretical basis for improving the quality of SGRDs.
Subject(s)
Oryza , Oryza/chemistry , Starch/chemistry , Food , CookingABSTRACT
BACKGROUND: The epithelial barrier dysfunction plays a critical role in the pathogenesis of a broad array of immune diseases. Alix protein is involved in the endolysosome system. This study aims to elucidate the role of Alix in the maintenance of epithelial barrier function. RESULTS: The results showed that Alix was detected in T84 cells at both mRNA and protein levels. Exposure to Staphylococcal enterotoxin B (SEB) markedly suppressed the expression of Alix in T84 cells, which could be blocked by knocking down the Toll like receptor 2. The exposure to SEB did not affect the TER, but markedly increased the permeability of T84 monolayers to OVA; the OVA passing through T84 monolayers still preserved the antigenicity manifesting inducing antigen specific T cells proliferation. CONCLUSIONS: Alix protein plays a critical role in the maintenance of the barrier function of T84 monolayers.
Subject(s)
Calcium-Binding Proteins/biosynthesis , Cell Cycle Proteins/biosynthesis , Endosomal Sorting Complexes Required for Transport/biosynthesis , Enterotoxins/administration & dosage , Immune System Diseases/pathology , Toll-Like Receptor 2/metabolism , Cell Line, Tumor , Cell Proliferation/drug effects , Epithelial Cells/drug effects , Epithelial Cells/metabolism , Humans , Immune System Diseases/metabolism , Intestinal Mucosa , Lysosomes/drug effectsABSTRACT
OBJECTIVE: To clone and express the arginine kinase (AK) gene of Blattella germanica and analyze its immune activity. METHODS: The cDNA of AK was cloned using specific primers from the total RNA of Blattella germanica The open reading frame (ORF) of AK was cloned into pET-28A vector, and expressed in Escherichia coli BL21(DE3) with IPTG induction. The recombinant protein was purified by Ni2+ chelating affinity chromatography. The recombinant protein was detected by SDS-PAGE, and its immune activity was analyzed by Western blotting. RESULTS: The cloned cDNA ORF sequence (GenBank accession No. FJ514482) contained 1071bp and encoded 356 amino acids. Its sequence homology with the published one (GenBank accession No. EU429466) was 97.2% at nucleotide level. The recombinant containing recombinant plasmid pET-28a-AK expressed a soluble protein of AK (Mr 45 000) after being induced with IPTG. The recombinant AK protein was recognized by sera of allergic patients, indicating that the recombinant AK protein has an adequate response activity. CONCLUSION: The AK gene of Blattella germanica has been cloned and the recombinant AK protein has been confirmed with immune activity.
