Functional Magnetic Particles as the Concentrating Probes for Ochratoxin A and as the Chiral Stationary Phase for DL-Tryptophan

碩士 === 國立交通大學 === 應用化學系所 === 94 === Ochratoxin A (OTA), a secondary metabolite generated from either Aspergillus or Penicillium, is toxic for animals. One of the objectives of this dissertation is to develop a method for the analysis of OTA. Human serum albumin (HSA) immobilized Fe3O4 magnetic par...

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Bibliographic Details
Main Authors: Hsin-Lan Hsueh, 薛杏嵐
Other Authors: Yu-Chie Chen
Format: Others
Language:zh-TW
Published: 2006
Online Access:http://ndltd.ncl.edu.tw/handle/49400700751357225620
Description
Summary:碩士 === 國立交通大學 === 應用化學系所 === 94 === Ochratoxin A (OTA), a secondary metabolite generated from either Aspergillus or Penicillium, is toxic for animals. One of the objectives of this dissertation is to develop a method for the analysis of OTA. Human serum albumin (HSA) immobilized Fe3O4 magnetic particles (Fe3O4@HSA) have two binding domains to OTA dianions. On the basis of this feature, HAS immobilized magnetic particles were employed to selectively concentrate OTA from sample solution. The affinity probes-OTA conjugates could be readily isolated from the sample solution after extraction. The results were confirmed by both matrix-assisted laser desorption/ionization mass spectrometry (MALDI MS) and capillary electrophoresis electrospray ionization mass spectrometry (CE ESI MS). Furthermore, off-line and on-line extraction using CE ESI MS as the detection method were developed. The results demonstrated that the detection limit of OTA using MALDI MS as the detection method was 0.5 μg/L (1.5 mL), while it was 4.0 μg/L (1 mL) using CE ESI MS as the analysis tool. Additionally, Fe3O4@HSA magnetic particles were employed to be as the chiral stationary phase for DL-tryptophan in CE ESI MS. The Fe3O4@HSA magnetic particles were injected into a capillary and fixed on the capillary by an external magnetic field prior to CE ESI MS analysis. The results demonstrated that this approach was able to separate the chiral DL-tryptophan.