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Characterization of Two Novel Bacillus Phytases and Their Foreseeable Applications in Transgenic Plants

Characterization of Two Novel Bacillus Phytases and Their Foreseeable Applications in Transgenic Plants


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About the Book

This dissertation, "Characterization of Two Novel Bacillus Phytases and Their Foreseeable Applications in Transgenic Plants" by Angela Judith, Tye, 戴安琪, was obtained from The University of Hong Kong (Pokfulam, Hong Kong) and is being sold pursuant to Creative Commons: Attribution 3.0 Hong Kong License. The content of this dissertation has not been altered in any way. We have altered the formatting in order to facilitate the ease of printing and reading of the dissertation. All rights not granted by the above license are retained by the author. Abstract: Abstract of thesis entitled CHARACTERIZATION OF TWO NOVEL BACILLUS PHYTASES AND THEIR FORESEEABLE APPLICATIONS IN TRANSGENIC PLANTS submitted by TYE ANGELA JUDITH for the degree of Master of Philosophy at The University of Hong Kong in July 2002 Phytases are enzymes that are capable of dephosphorylating phytate, a well known phosphorus-locking molecule that is regarded as an anti-nutrient. Some monogastric animals lack an enzyme to degrade phytate content in food, inorganic phosphate or microbial phytases are added into feedstuff to provide sufficient phosphorus to animals. Well known of their capability to free phosphate from phytate, phytases play important roles in the agricultural and feed industries, and were under long term investigation. Recently, researchers have shifted their focus to the production of transgenic animals and plants that express microbial phytases. In our studies, a novel phytase-encoding gene (phyL) was cloned from Bacillus licheniformis using multiple steps of degenerate and inverse polymerase chain reaction. The phyL gene was about 1.1kb in size, and a 300bp upstream region was obtained. The phyL gene, together with a 1.3kb phytase-encoding open reading frame (168phyA) identified in the B. subtilis strain 168 genome, were employed for recombinant over-expression in B. subtilis strain MU331IA304. The adopted φ105MU331 prophage vector system was able to produce 36.9units/mL and 29units/mL of 168PhyA and PhyL enzymes in shaking flasks, respectively. The mature 168PhyA (44.6kDa) and PhyL (47kDa) enzymes were capable of releasing inorganic phosphate from dodesodium phytate, and exhibited broad temperature optima under neutral pH. Like other Bacillus phytases, the 2+ temperature stabilities of PhyL and 168PhyA phytases were dependent on Ca, while PhyL apparently showed lower calcium dependence at high temperatures. To investigate the effects of introducing a Bacillus phytase into plants, transgenic tobacco (Nicotina tabacum) lines that express the B. subtilis 168PhyA were created. Genomic southern blotting and northern blotting analyses showed successful inheritance of the transgene. Further investigation will focus on the activity profiles of the purified phytase from these lines, as well as the phosphorus-releasing capability and phenotypic changes of selected lines. In summary, we have developed a superior microbial expression system for recombinant phytase production and expressed the enzyme in transgenic plants. This transgenic technology may not only be an alternative for direct phytase/phosphorus supplementation in animal feeds, but may also shed light in reducing the consumption of phosphorus fertilizers in agriculture. DOI: 10.5353/th_b2987288 Subjects: Phytases - Genetics Transgenic plants


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Product Details
  • ISBN-13: 9781374720169
  • Publisher: Open Dissertation Press
  • Publisher Imprint: Open Dissertation Press
  • Height: 279 mm
  • No of Pages: 110
  • Weight: 272 gr
  • ISBN-10: 137472016X
  • Publisher Date: 27 Jan 2017
  • Binding: Paperback
  • Language: English
  • Spine Width: 6 mm
  • Width: 216 mm


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