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The full abstract for this thesis is available in the body of the thesis, and will be available when the embargo expires.
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The attached files are supplements to the author’s doctoral dissertation at https://circle.library.ubc.ca/handle/2429/73446.
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The attached files are supplements to the author’s doctoral dissertation at https://circle.library.ubc.ca/handle/2429/73156
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The full abstract for this thesis is available in the body of the thesis, and will be available when the embargo expires.
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This is a collection of Matlab functions and scripts, designed to aid the processing and analysis of high-resoltution mass spectrometry data from real-time breath analysis measurements. Details on the usage of the functions can be found in the individual help sections, as well as in appendix A of the dissertation "On-line Breath Analysis with Ambient High-Resolution Mass Spectrometry" by Martin Thomas Gaugg (2019), available on the ETH Research Collection.,MATLAB 2018a,
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The attached file is a supplement to the author's master's thesis at https://circle.library.ubc.ca/handle/2429/68122
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Demonstration of the 200fps imaging capabilities of our digital ultrasound probe (LightProbe)
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The full abstract for this thesis is available in the body of the thesis, and will be available when the embargo expires.
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Intracellular α-amylase was a special glycoside hydrolase in the cytoplasm. We cloned and expressed an intracellular α-amylase, Amy, from Paenibacillus sp. SSG-1. The recombinant enzyme was purified by metal-affinity chromatography, exhibited a molecular mass of 71.7 kDa. Amy exhibited unexpectedly sequence similarity and evolutionary relationships with alpha-glucanotransferase. The docked results of Amy with maltose showed it had similar catalytic residues with α-amylase and glucanotransferase. The substrate specificity experiment showed that Amy could hydrolyze typical substrates into glucose and maltose. It was noteworthy that Amy showed the catalytic capacity of cyclomaltodextrinase and pullulanase. Meanwhile, Amy could transfer sugar molecules and form maltotetraose upon the hydrolysis of substrates. These results indicated that Amy was a novel intracellular α-amylase with distinct catalytic ability characteristics of hydrolyzing glycogen/cyclodextrin/pullulan and transglycosylation. We deduced that Amy may play an important role in utilizing maltooligosaccharides that released from extracellular α-glucan or storage α-glucan (glycogen) in Paenibacillus sp. SSG-1.
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