| Summary: | 碩士 === 國立嘉義大學 === 農業生物技術研究所 === 95 === β-glucanase is one of the hemicellulose hydrolytic enzymes. The enzyme hydrolysis character of the plant cell wall's β-glucans polysaccharide component. Phytate is the main storage form of phosphorus in many plant seeds. Most animal feed cereal or legumes as processing material. However, the β-glucans and phytate are indigestible for monogastric animal, including pigs, poultry, and fishs, due to the lack of digestive enzymes to hydrolyze the β-glucans and phytate. It will reduce the monogastric animals the right nutrition absorption and utilization.In this study, gluT expression was controlled by GluB–1 promoter, PR–1a promoter, and SAG promoter; E. coli (appA) was controlled by PR–1a promoter and SAG promoter. Purpose is to be rice-products as animal feed additives. Five different expression vectors pGluG, pPRG, pSG, pPRA, and pSA were Agrobacterium-mediated transformation of rice. There were 41, 22, 24, 25 and 8 transgenic line respectively, and copy numbers of the 1-3 range; estimated 20, 10, 15, 18 and 5 transgenic lines of single copy number respectively. The RNA dot blot analysis results show that five expression vectors have high expression levels of the amount of transgenic lines. These transgenic plants are the number 8, and 41of pGluG, the number 13, 24, 44, 45, 46, 47, 48, 52, and 53 of pPRG, the 56, and 58 of pSG, the number 6, 15, 16, 18, 44, 69, and 71 of pPRA, and the number 17 of pSA. Assay for gluT activity, there were high level expression in transgenic lines of 1, 41, 48, and speculated optimum temperature of 45°C, the optimal pH of 6.0.
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